_EC 4.2.1.11 Phosphopyruvate hydratase. 62 PDB entries  
EC 4.-.-.- Lyases. [3,638 PDB entries]
EC 4.2.-.- Carbon-oxygen lyases. [1,772 PDB entries]
EC 4.2.1.- Hydro-lyases. [1,376 PDB entries]
EC 4.2.1.11 Phosphopyruvate hydratase. [62 PDB entries]    
1e9i

Reaction: 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.
 


2-phospho-D-glycerate
=
phosphoenolpyruvate
+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): 2-phosphoglycerate dehydratase. Enolase.
Cofactor(s): Mg(2+).
Comments: Also acts on 3-phospho-D-erythronate.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 62 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 structur enolase-mn2+-phosphonoacetohydroxamate complex at 2.4 angst 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 54.55% similar to enzyme reactant D-glycerate
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 ligands:   Het Group 2PG corresponds to enzyme reactant D-glycerate 2-phosphate
  Het Group PEP corresponds to enzyme product Phosphoenolpyruvate
1p43
Reverse protonation is the key to general acid-base catalysi 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 corresponds to enzyme reactant D-glycerate
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 ligands:   Het Group 2PG corresponds to enzyme reactant D-glycerate 2-phosphate
  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 D-glycerate 2-phosphate
  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
2ge6
Protein modeling of enolase (neocallimastix frontalis)
Source: Neocallimastix frontalis. Rumen fungus
Chain: A (435 residues)
2gua
Protein model of enolase (gallus gallus)
Source: Gallus gallus. Chicken
Chain: A (433 residues)
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 corresponds to enzyme reactant D-glycerate 2-phosphate
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 pe
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 corresponds to enzyme reactant D-glycerate
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 corresponds to enzyme reactant D-glycerate
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 corresponds to enzyme reactant D-glycerate
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 rn 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
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 54.55% similar to enzyme reactant D-glycerate
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 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/pe
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 corresponds to enzyme reactant 2-phospho-D-glycerate
3ucd
Asymmetric complex of human neuron specific enolase-2-pga/pe
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 corresponds to enzyme reactant 2-phospho-D-glycerate
3uj2
Crystal structure of an enolase from anaerostipes caccae (ef 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/pe
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 corresponds to enzyme reactant 2-phospho-D-glycerate
3ujf
Asymmetric complex of human neuron specific enolase-4-pga/pe
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 corresponds to enzyme reactant 2-phospho-D-glycerate
3ujr
Asymmetric complex of human neuron specific enolase-5-pga/pe
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 corresponds to enzyme reactant 2-phospho-D-glycerate
3ujs
Asymmetric complex of human neuron specific enolase-6-pga/pe
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 corresponds to enzyme reactant 2-phospho-D-glycerate
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
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 corresponds to enzyme reactant D-glycerate 2-phosphate
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
7enl
Mechanism of enolase: the crystal structure of enolase-mg2+- phosphoglycerate(slash) phosphoenolpyruvate complex at 2.2- 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 corresponds to enzyme reactant D-glycerate