_EC 4.2.1.11 phosphopyruvate hydratase.

112 PDB entries

EC 4.-.-.- Lyases. [10,232 PDB entries] EC 4.2.-.- Carbon-oxygen lyases. [5,835 PDB entries] EC 4.2.1.- Hydro-lyases. [4,241 PDB entries] EC 4.2.1.11 phosphopyruvate hydratase. [112 PDB entries]

1e9i

Reaction:		(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O.
		(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Other name(s):		2-phosphoglycerate dehydratase. enolase.
Comments:		Also acts on 3-phospho-D-erythronate.
Links:		[IntEnz]   [ExPASy]   [KEGG]

There are 112 PDB entries in enzyme class E.C.4.2.1.11

PDB code		Protein
1e9i		Enolase from e.Coli Source: Escherichia coli. Organism_taxid: 562. Gene: eno. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B, C, D (430 residues) CATH domains: 3.30.390.10 3.20.20.120
1ebg		Chelation of ser 39 to mg2+ latches a gate at the active site of enolase: structure of the bis(mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1 angstroms resolution Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120
1ebh		Octahedral coordination at the high affinity metal site in enolase; crystallographic analysis of the mg++-enzyme from yeast at 1.9 angstroms resolution Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120
1els		Catalytic metal ion binding in enolase: the crystal structure of enolase-mn2+-phosphonoacetohydroxamate complex at 2.4 angstroms resolution Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chain: A (436 residues) CATH domains: 3.30.390.10 3.20.20.120
1iyx		Crystal structure of enolase from enterococcus hirae Source: Enterococcus hirae. Organism_taxid: 1354 Chains: A, B (431 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group GOL is 45.45% similar to enzyme product phosphoenolpyruvate
1l8p		Mg-phosphonoacetohydroxamate complex of s39a yeast enolase 1 Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: eno1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B, C, D (436 residues) CATH domains: 3.30.390.10 3.20.20.120
1nel		Fluoride inhibition of yeast enolase: crystal structure of the enolase-mg2+-f--pi complex at 2.6-angstroms resolution Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chain: A (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
1oep		Structure of trypanosoma brucei enolase reveals the inhibitory divalent metal site Source: Trypanosoma brucei brucei. Organism_taxid: 5702. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chain: A (422 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group EDO is 40.00% similar to enzyme product phosphoenolpyruvate
1one		Yeast enolase complexed with an equilibrium mixture of 2'- phosphoglyceate and phosphoenolpyruvate Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
1p43		Reverse protonation is the key to general acid-base catalysis in enolase Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: eno1 or enoa or hsp48 or ygr254w or g9160. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
1p48		Reverse protonation is the key to general acid-base catalysis in enolase Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: eno1 or enoa or hsp48 or ygr254w or g9160. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
1pdy		X-ray structure and catalytic mechanism of lobster enolase Source: Homarus gammarus. European lobster. Organism_taxid: 6707. Organ: tail. Tissue: tail muscle Chain: A (434 residues) CATH domains: 3.30.390.10 3.20.20.120
1pdz		X-ray structure and catalytic mechanism of lobster enolase Source: Homarus gammarus. European lobster. Organism_taxid: 6707. Organ: tail. Tissue: tail muscle Chain: A (434 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PGA is 90.00% similar to enzyme product phosphoenolpyruvate
1te6		Crystal structure of human neuron specific enolase at 1.8 angstrom Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B (434 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
1w6t		Crystal structure of octameric enolase from streptococcus pneumoniae Source: Streptococcus pneumoniae. Pneumococci. Organism_taxid: 170187. Strain: tigr4. Atcc: 11733, baa-255/r6. Expressed in: escherichia coli. Expression_system_taxid: 511693. Chains: A, B (429 residues) CATH domains: 3.30.390.10 3.20.20.120
2akm		Fluoride inhibition of enolase: crystal structure of the inhibitory complex Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
2akz		Fluoride inhibition of enolase: crystal structure of the inhibitory complex Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (435 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
2al1		Crystal structure analysis of enolase mg subunit complex at ph 8.0 Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Other_details: genes eno1, enoa, hsp48 Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
2al2		Crystal structure analysis of enolase mg subunit complex at ph 8.0 Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: eno1, enoa, hsp48. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligands:   Het Group 2PG corresponds to enzyme reactant 2-phospho-D-glycerate   Het Group PEP corresponds to enzyme product Phosphoenolpyruvate
2fym		Crystal structure of e. Coli enolase complexed with the minimal binding segment of rnase e. Source: Escherichia coli. Organism_taxid: 562. Gene: eno. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: the e. Coli rnase e peptide was synthesized. Chains: A, C, D, F (431 residues) CATH domains: 3.30.390.10 3.20.20.120
2one		Asymmetric yeast enolase dimer complexed with resolved 2'- phosphoglycerate and phosphoenolpyruvate Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
2pa6		Crystal structure of mj0232 from methanococcus jannaschii Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: eno. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (427 residues) CATH domains: 3.30.390.10 3.20.20.120
2psn		Crystal structure of enolase1 Source: Homo sapiens. Human. Gene: eno1, eno1l1, mbpb1, mpb1. Expressed in: escherichia coli. Chains: A, B, C, D (432 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
2ptw		Crystal structure of the t. Brucei enolase complexed with sulphate, identification of a metal binding site iv Source: Trypanosoma brucei. Organism_taxid: 5691. Expressed in: escherichia coli. Expression_system_taxid: 562. Chain: A (406 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group EDO is 40.00% similar to enzyme product phosphoenolpyruvate
2ptx		Crystal structure of the t. Brucei enolase complexed with sulphate in closed conformation Source: Trypanosoma brucei. Organism_taxid: 5691. Expressed in: escherichia coli. Expression_system_taxid: 562. Chain: A (431 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group EDO is 40.00% similar to enzyme product phosphoenolpyruvate
2pty		Crystal structure of the t. Brucei enolase complexed with pep Source: Trypanosoma brucei. Organism_taxid: 5691. Expressed in: escherichia coli. Expression_system_taxid: 562. Chain: A (431 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
2ptz		Crystal structure of the t. Brucei enolase complexed with phosphonoacetohydroxamate (pah), his156-out conformation Source: Trypanosoma brucei. Organism_taxid: 5691. Expressed in: escherichia coli. Expression_system_taxid: 562. Chain: A (431 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group EDO is 40.00% similar to enzyme product phosphoenolpyruvate
2pu0		Crystal structure of the t. Brucei enolase complexed with phosphonoacetohydroxamate (pah), his156-in conformation Source: Trypanosoma brucei. Organism_taxid: 5691. Expressed in: escherichia coli. Expression_system_taxid: 562. Chain: A (431 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group EDO is 40.00% similar to enzyme product phosphoenolpyruvate
2pu1		Crystal structure of the t. Brucei enolase complexed with fluoro- phosphonoacetohydroxamate (fpah) Source: Trypanosoma brucei. Organism_taxid: 5691. Expressed in: escherichia coli. Expression_system_taxid: 562. Chain: A (431 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group EDO is 40.00% similar to enzyme product phosphoenolpyruvate
2xgz		Engineering the enolase active site pocket: crystal structure of the s39n d321r mutant of yeast enolase 1 Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 511693. Chains: A, B (438 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
2xh0		Engineering the enolase active site pocket: crystal structure of the s39n q167k d321r mutant of yeast enolase 1 Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 511693. Chains: A, B, C, D (438 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
2xh2		Engineering the enolase active site pocket: crystal structure of the s39n d321a mutant of yeast enolase 1 Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 511693. Chains: A, B, C, D (438 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
2xh4		Engineering the enolase active site pocket: crystal structure of the s39a d321a mutant of yeast enolase 1 Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 511693. Chains: A, B, C, D (438 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
2xh7		Engineering the enolase active site pocket: crystal structure of the d321a mutant of yeast enolase 1 Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 511693. Chains: A, B (437 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
2xsx		Crystal structure of human beta enolase enob Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: r3-prare2. Chains: A, B (434 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
3b97		Crystal structure of human enolase 1 Source: Homo sapiens. Human. Organism_taxid: 9606 Chains: A, B, C, D (432 residues) CATH domains: 3.30.390.10 3.20.20.120
3enl		Refined structure of yeast apo-enolase at 2.25 angstroms resolution Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chain: A (436 residues) CATH domains: 3.30.390.10 3.20.20.120
3h8a		Crystal structure of e. Coli enolase bound to its cognate rnase e recognition domain Source: Escherichia coli. Organism_taxid: 562. Synthetic: yes. Organism_taxid: 83333. Other_details: the sequence occurs naturally in e. Coli Chains: A, B, C, D (430 residues) CATH domains: 3.30.390.10 3.20.20.120
3otr		2.75 angstrom crystal structure of enolase 1 from toxoplasma gondii Source: Toxoplasma gondii. Organism_taxid: 508771. Strain: me49. Gene: tgme49_068860. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B, C, D, E, F (444 residues) CATH domains: 3.30.390.10 3.20.20.120
3qn3		Phosphopyruvate hydratase from campylobacter jejuni. Source: Campylobacter jejuni. Organism_taxid: 197. Strain: subsp. Jejuni nctc 11168. Gene: cj1672c, eno. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B, C, D (415 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group GOL is 45.45% similar to enzyme product phosphoenolpyruvate
3qtp		Crystal structure analysis of entamoeba histolytica enolase Source: Entamoeba histolytica. Organism_taxid: 5759. Gene: enl-1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B (438 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG corresponds to enzyme reactant 2-phospho-D-glycerate
3tqp		Structure of an enolase (eno) from coxiella burnetii Source: Coxiella burnetii. Organism_taxid: 777. Strain: rsa493. Gene: eno, cbu_1674. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B (418 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
3ucc		Asymmetric complex of human neuron specific enolase-1-pga/pep Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
3ucd		Asymmetric complex of human neuron specific enolase-2-pga/pep Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
3uj2		Crystal structure of an enolase from anaerostipes caccae (efi target efi-502054) with bound mg and sulfate Source: Anaerostipes caccae. Organism_taxid: 411490. Strain: dsm 14662. Gene: eno1, anacac_00540. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B, C, D, E, F, G, H (423 residues) CATH domains: 3.30.390.10 3.20.20.120
3uje		Asymmetric complex of human neuron specific enolase-3-pga/pep Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
3ujf		Asymmetric complex of human neuron specific enolase-4-pga/pep Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
3ujr		Asymmetric complex of human neuron specific enolase-5-pga/pep Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
3ujs		Asymmetric complex of human neuron specific enolase-6-pga/pep Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group XSP is 90.91% similar to enzyme product phosphoenolpyruvate
3zlf		Structure of group a streptococcal enolase k312a mutant Source: Streptococcus pyogenes mgas10394. Organism_taxid: 286636. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B, C, D (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
3zlg		Structure of group a streptococcal enolase k362a mutant Source: Streptococcus pyogenes mgas10394. Organism_taxid: 286636. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B, C, D (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
3zlh		Structure of group a streptococcal enolase Source: Streptococcus pyogenes mgas10394. Organism_taxid: 286636. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B, C, D (430 residues) CATH domains: 3.30.390.10 3.20.20.120
4a3r		Crystal structure of enolase from bacillus subtilis. Source: Bacillus subtilis. Organism_taxid: 1423. Strain: 168. Expressed in: escherichia coli. Expression_system_taxid: 511693. Chains: A, B, C, D (428 residues) CATH domains: 3.30.390.10 3.20.20.120
4enl		Crystal structure of holoenzyme refined at 1.9 angstroms resolution: trigonal-bipyramidal geometry of the cation binding site Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chain: A (436 residues) CATH domains: 3.30.390.10 3.20.20.120
4ewj		Structure of the enloase from streptococcus suis serotype 2 Source: Streptococcus suis. Organism_taxid: 1307. Strain: 05zyh33. Gene: eno, eno2, enolase, ssust3_1361. Expressed in: escherichia coli. Expression_system_taxid: 562. Chains: A, B (428 residues) CATH domains: 3.30.390.10 3.20.20.120
4g7f		Crystal structure of enolase from trypanosoma cruzi Source: Trypanosoma cruzi. Organism_taxid: 353153. Strain: cl brener. Gene: tc00.1047053504105.140. Expressed in: escherichia coli. Expression_system_taxid: 562. Chain: A (419 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group EDO is 40.00% similar to enzyme product phosphoenolpyruvate
4mks		Crystal structure of enolase from lactobacillus gasseri Source: Lactobacillus gasseri. Organism_taxid: 324831. Strain: dsm 20243. Atcc: 33323. Gene: eno2, lgas_1305. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B (400 residues) CATH domains: 3.30.390.10 3.20.20.120
4rop		Crystal structure of enolase from synechococcus elongatus Source: Synechococcus elongatus (strain atcc 33912 / pcc 7942 / fachb-805). Organism_taxid: 1140. Strain: atcc 33912 / pcc 7942 / fachb-805. Gene: eno. Expressed in: escherichia coli. Expression_system_taxid: 562 Chain: A (424 residues) CATH domains: 3.30.390.10 3.20.20.120
4yws		Thermostable enolase from chloroflexus aurantiacus Source: Chloroflexus aurantiacus (strain atcc 29366 / dsm 635 / j-10-fl). Organism_taxid: 324602. Strain: atcc 29366 / dsm 635 / j-10-fl. Atcc: 29366 Chains: A, B (405 residues) CATH domains: 3.30.390.10 3.20.20.120
4z17		Thermostable enolase from chloroflexus aurantiacus Source: Chloroflexus aurantiacus (strain atcc 29366 / dsm 635 / j-10-fl). Organism_taxid: 324602. Strain: atcc 29366 / dsm 635 / j-10-fl. Atcc: 29366 Chains: A, B (424 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
4z1y		Thermostable enolase from chloroflexus aurantiacus with substrate 2- phosphoglycerate Source: Chloroflexus aurantiacus (strain atcc 29366 / dsm 635 / j-10-fl). Organism_taxid: 324602. Strain: atcc 29366 / dsm 635 / j-10-fl. Atcc: 29366 Chains: A, B (424 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
4za0		Structure of human enolase 2 in complex with phosphonoacetohydroxamate Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Chains: A, B (434 residues) CATH domains: 3.30.390.10 3.20.20.120
4zcw		Structure of human enolase 2 in complex with sf2312 Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120
5boe		Crystal structure of staphylococcus aureus enolase in complex with pep Source: Staphylococcus aureus. Organism_taxid: 1280. Gene: eno. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B (433 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
5bof		Crystal structure of staphylococcus aureus enolase Source: Staphylococcus aureus. Organism_taxid: 1280. Gene: eno. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B (434 residues) CATH domains: 3.30.390.10 3.20.20.120
5enl		Inhibition of enolase: the crystal structures of enolase-ca2+- phosphoglycerate and enolase-zn2+-phosphoglycolate complexes at 2.2- angstroms resolution Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chain: A (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
5eu9		Structure of human enolase 2 in complex with ((3s,5s)-1,5-dihydroxy-3- methyl-2-oxopyrrolidin-3-yl)phosphonic acid Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Chains: A, B, C, D, E, F, G, H (433 residues) CATH domains: 3.30.390.10 3.20.20.120
5idz		Structure of human enolase 2 in complex with (s)-(1-hydroxy-2- oxopiperidin-3-yl)phosphonate Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (436 residues) CATH domains: 3.30.390.10 3.20.20.120
5j04		Crystal structure of enolase from synechococcus elongatus, complex with phosphoenolpyruvate Source: Synechococcus elongatus pcc 7942 = fachb-805. Organism_taxid: 1140. Strain: pcc 7942. Gene: eno, synpcc7942_0639. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B (424 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
5jlz		Crystal structure of hla-drb1 04:01 In complex with modified alpha- enolase peptide 26-40 with citrulline at the position 32 Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-dra, hla-dra1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: hla-drb1. Synthetic: yes. Organism_taxid: 9606 Chains: E, F (14 residues) Bound ligand:   Het Group MLA is 41.67% similar to enzyme product phosphoenolpyruvate
5lax		Crystal structure of hla_drb1 04:01 In complex with alpha-enolase peptide 26-40 Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-dra, hla-dra1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star. Gene: hla-drb1. Hhman. Chains: E, F (14 residues) Bound ligand:   Het Group MLA is 41.67% similar to enzyme product phosphoenolpyruvate
5ni9		Crystal structure of hla-drb1 04:01 With the alpha-enolase peptide 326-340 Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-dra, hla-dra1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hla-drb1. Synthetic: yes. Organism_taxid: 9606 Chain: C (14 residues)
5nig		Crystal structure of hla-drb1 04:01 With modified alpha-enolase peptide 326-340 (arginine 327 to citrulline) Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-dra, hla-dra1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hla-drb1. Synthetic: yes. Organism_taxid: 9606 Chain: C (15 residues)
5ock		Crystal structure of acpa e4 in complex with cep1 Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: expi293f (tm). Expression_system_cell: expi293f (tm). Synthetic: yes. Organism_taxid: 9606 Chain: A (18 residues)
5ohg		Enolase in complex with rnase e Source: Escherichia coli (strain k12). Organism_taxid: 83333. Gene: eno, b2779, jw2750. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: rne, ams, hmp1, b1084, jw1071. Expression_system_taxid: 562 Chains: A, B, H, I (431 residues) Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
5td9		Structure of human enolase 2 Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B (434 residues)
5tij		Structure of human enolase 2 with ((3s,5s)-1,5-dihydroxy-3-methyl-2- oxopyrrolidin-3-yl)phosphonate (purified enantiomer) Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (433 residues)
5wro		Crystal structure of drosophila enolase Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: eno, cg17654. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: codonplus Chain: A (439 residues) Bound ligand:   Het Group GOL is 45.45% similar to enzyme product phosphoenolpyruvate
6bfy		Crystal structure of enolase from escherichia coli with bound 2- phosphoglycerate substrate Source: Escherichia coli. Organism_taxid: 562. Gene: eno, ecs88_3047. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B, C, F, D, E (439 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
6bfz		Crystal structure of enolase from e. Coli with a mixture of apo form, substrate, and product form Source: Escherichia coli. Organism_taxid: 562. Gene: eno, ecs88_3047. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B, E, F, D, C (439 residues) Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
6d3q		Crystal structure of escherichia coli enolase complexed with a natural inhibitor sf2312. Source: Escherichia coli. Organism_taxid: 562. Gene: eno. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, C, B, E, F, D (438 residues) Bound ligand:   Het Group GOL is 45.45% similar to enzyme product phosphoenolpyruvate
6enl		Inhibition of enolase: the crystal structures of enolase-ca2+- phosphoglycerate and enolase-zn2+-phosphoglycolate complexes at 2.2- angstroms resolution Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chain: A (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group PGA is 90.00% similar to enzyme product phosphoenolpyruvate
6j36		Crystal structure of mycoplasma hyopneumoniae enolase Source: Mycoplasma hyopneumoniae. Organism_taxid: 2099. Gene: eno. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B (459 residues) Bound ligand:   Het Group GOL is 45.45% similar to enzyme product phosphoenolpyruvate
6l7d		Mycobacterium tuberculosis enolase mutant - s42a Source: Mycobacterium tuberculosis h37rv. Organism_taxid: 83332. Strain: atcc 25618 / h37rv. Gene: eno, rv1023, mtcy10g2.26c. Expressed in: mycolicibacterium smegmatis. Expression_system_taxid: 1772 Chain: A (423 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
6nb2		Crystal structure of enolase from legionella pneumophila bound to 2- phosphoglyceric acid and magnesium Source: Legionella pneumophila subsp. Pneumophila (strain philadelphia 1 / atcc 33152 / dsm 7513). Organism_taxid: 272624. Strain: philadelphia 1 / atcc 33152 / dsm 7513. Gene: eno, lpg2037. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (423 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
6npf		Structure of e.Coli enolase in complex with an analog of the natural product sf-2312 metabolite. Source: Escherichia coli. Organism_taxid: 562. Gene: eno, ecs88_3047. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B, C, D, F, E (438 residues) Bound ligand:   Het Group TLA is 42.86% similar to enzyme product phosphoenolpyruvate
6o4n		Crystal structure of enolase from chlamydia trachomatis Source: Chlamydia trachomatis serovar l2b (strain uch- 1/proctitis). Organism_taxid: 471473. Strain: uch-1/proctitis. Gene: eno, ctlon_0844. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chains: A, B (422 residues) Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
7ckp		Mycobacterium tuberculosis enolase Source: Mycobacterium tuberculosis (strain atcc 25618 / h37rv). Organism_taxid: 83332. Strain: atcc 25618 / h37rv. Gene: eno, rv1023, mtcy10g2.26c. Expressed in: mycolicibacterium smegmatis. Expression_system_taxid: 1772 Chain: A (415 residues)
7clk		Mycobacterium tuberculosis enolase in complex with alternate 2- phosphoglycerate Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: eno, ayj03_005430, dsi38_18100, ers007663_02163, ers013471_01432, ers024276_01771, ers027659_01730, ers075361_03197, ers094182_03347, f6w99_03724, samea2683035_03102. Expressed in: mycolicibacterium smegmatis. Expression_system_taxid: 1772 Chain: A (423 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
7cll		Mycobacterium tubeculosis enolase in complex with 2-phosphoglycerate Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: eno, ayj03_005430, dsi38_18100, ers007663_02163, ers013471_01432, ers024276_01771, ers027659_01730, ers075361_03197, ers094182_03347, f6w99_03724, samea2683035_03102. Expressed in: mycolicibacterium smegmatis. Expression_system_taxid: 1772 Chains: A, B, C, D (425 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
7dlr		Mycobacterium tuberculosis enolase mutant - e163a Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: eno, dsi38_18100, ers007663_02163, ers013471_01432, ers024276_01771, ers027659_01730, ers075361_03197, ers094182_03347, f6w99_03724, samea2683035_03102. Expressed in: mycolicibacterium smegmatis. Expression_system_taxid: 1772 Chain: A (423 residues) Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
7e2q		Crystal structure of mycoplasma pneumoniae enolase Source: Mycoplasma pneumoniae. Organism_taxid: 2104. Gene: eno, nctc10119_00092. Expressed in: escherichia coli o104:h4 str. 2009el-2050. Expression_system_taxid: 1134782 Chains: A, B, C, D (450 residues)
7e4f		Mycobacterium tuberculosis enolase mutant - e204a complex with phosphoenolpyruvate Source: Mycobacterium tuberculosis (strain atcc 25618 / h37rv). Organism_taxid: 83332. Strain: atcc 25618 / h37rv. Gene: eno, rv1023, mtcy10g2.26c. Expressed in: mycolicibacterium smegmatis. Expression_system_taxid: 1772 Chain: A (424 residues) Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
7e4x		Structure of enolase from mycobacterium tuberculosis Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: eno, ayj03_005430, dsi38_18100, ers007663_02163, ers013471_01432, ers024276_01771, ers027659_01730, ers075361_03197, ers094182_03347, f6w99_03724, samea2683035_03102. Expressed in: mycolicibacterium smegmatis. Expression_system_taxid: 1772 Chains: A, B, C, D, E, F, G, H (423 residues)
7e51		Structure of pep bound enolase from mycobacterium tuberculosis Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: eno, ayj03_005430, dsi38_18100, ers007663_02163, ers013471_01432, ers024276_01771, ers027659_01730, ers075361_03197, ers094182_03347, f6w99_03724, samea2683035_03102. Expressed in: mycolicibacterium smegmatis. Expression_system_taxid: 1772 Chains: A, B, C, D, E, F, G, H (423 residues) Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
7enl		Mechanism of enolase: the crystal structure of enolase-mg2+- phosphoglycerate(slash) phosphoenolpyruvate complex at 2.2-angstroms resolution Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932 Chain: A (436 residues) CATH domains: 3.30.390.10 3.20.20.120 Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
7mbh		Structure of human enolase 2 in complex with phosphoserine Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: eno2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008 Chains: A, B (436 residues) Bound ligand:   Het Group SEP is 50.00% similar to enzyme product phosphoenolpyruvate
7rhv		Aspergillus fumigatus enolase Source: Neosartorya fumigata (strain atcc mya-4609 / af293 / cbs 101355 / fgsc a1100). Aspergillus fumigatus. Organism_taxid: 330879. Strain: atcc mya-4609 / af293 / cbs 101355 / fgsc a1100. Gene: enoa, afua_6g06770. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (424 residues)
7rhw		Aspergillus fumigatus enolase bound to 2-phosphoglycerate Source: Neosartorya fumigata (strain atcc mya-4609 / af293 / cbs 101355 / fgsc a1100). Aspergillus fumigatus. Organism_taxid: 330879. Strain: atcc mya-4609 / af293 / cbs 101355 / fgsc a1100. Gene: enoa, afua_6g06770. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (437 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
7ri0		Aspergillus fumigatus enolase bound to phosphoenolpyruvate and 2- phosphoglycerate Source: Neosartorya fumigata (strain atcc mya-4609 / af293 / cbs 101355 / fgsc a1100). Aspergillus fumigatus. Organism_taxid: 330879. Strain: atcc mya-4609 / af293 / cbs 101355 / fgsc a1100. Gene: enoa, afua_6g06770. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (430 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
7ugh		Crystal structure of enolase family protein from naegleria fowleri with bound 2-phosphoglyceric acid Source: Naegleria fowleri. Organism_taxid: 5763. Strain: atcc 30863. Gene: nf0118810. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B (436 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
7ugu		Structure of enolase from streptococcus pyogenes Source: Streptococcus pyogenes. Organism_taxid: 1314. Gene: eno, e0f66_01300, e0f67_02490, fgo82_08975, samea1711581_01820, samea864267_00487. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008 Chains: G, H, E, F, C, D, A, B (436 residues)
7v67		Crystal structure of enolase1 from candida albicans Source: Candida albicans sc5314. Organism_taxid: 237561. Strain: sc5314. Gene: eno1. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B, C, D (439 residues)
7vrd		Crystal structure of enolase1 from candida albicans complexed with 2'- phosphoglyceric acid sodium Source: Candida albicans sc5314. Yeast. Organism_taxid: 237561. Strain: sc5314. Gene: eno1. Expressed in: escherichia coli. Expression_system_taxid: 562 Chains: A, B, C, D (439 residues) Bound ligand:   Het Group 2PG is 90.91% similar to enzyme product phosphoenolpyruvate
7xml		Cryo-em structure of peip-bs_enolase complex Source: Bacillus subtilis (strain 168). Organism_taxid: 224308. Gene: eno, bsu33900. Expressed in: escherichia coli. Expression_system_taxid: 562. Bacillus phage sp01. Bacillus virus spo1. Organism_taxid: 10685. Gene: 60. Chains: A, B (428 residues)
8dg4		Group a streptococcus enolase k252a, k255a, k434a, k435a mutant Source: Streptococcus sp. 'Group a'. Organism_taxid: 36470. Gene: eno, spy_0731, m5005_spy0556. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008 Chains: E, F, G, H, C, D, A, B (436 residues)
8trl		T cell recognition of citrullinated alpha-enolase peptide presented by hla-dr4 Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-dra, hla-dra1. Expressed in: homo sapiens. Expression_system_taxid: 9606. Gene: hla-drb1. Synthetic: yes. Expressed in: escherichia coli bl21(de3). Chains: C, F (13 residues)
8uel		Crystal structure of enolase from litopenaeus vannamei Source: Penaeus vannamei. Organism_taxid: 6689 Chains: A, B (433 residues) Bound ligand:   Het Group PEP corresponds to enzyme product phosphoenolpyruvate
8uop		Major interface of streptococcal surface enolase dimer from ap53 group a streptococcus bound to a lipid vesicle Source: Streptococcus pyogenes. Organism_taxid: 1314. Gene: eno, e0f66_01300, e0f67_02490, fgo82_08975, samea1711581_01820, samea864267_00487. Expressed in: escherichia coli 'bl21-gold(de3)plyss ag'. Expression_system_taxid: 866768 Chains: A, B (436 residues)
8uoy		Major interface of streptococcal surface enolase dimer from ap53 group a streptococcus bound to a lipid vesicle Source: Streptococcus pyogenes. Organism_taxid: 1314. Gene: eno, e0f66_01300, e0f67_02490, fgo82_08975, samea1711581_01820, samea864267_00487. Expressed in: escherichia coli 'bl21-gold(de3)plyss ag'. Expression_system_taxid: 866768 Chains: B, C (436 residues)
8w21		Crystal structure of enolase from chlamydia trachomatis (p43212 form) Source: Chlamydia trachomatis. Organism_taxid: 272561. Strain: d/uw-3/cx. Gene: eno, ct_587. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Chains: A, B, C, D, E, F, G, H (417 residues) Bound ligand:   Het Group PO4 is 50.00% similar to enzyme product phosphoenolpyruvate
9no2		Cryoem structure of ribd-enolase complex Source: Francisella tularensis subsp. Novicida. Organism_taxid: 264. Strain: strain u112. Strain: strain u112 Chains: A, C (428 residues)