_EC 2.7.2.3 Phosphoglycerate kinase. 49 PDB entries  
EC 2.-.-.- Transferases. [18,188 PDB entries]
EC 2.7.-.- Transferring phosphorous-containing groups. [11,027 PDB entries]
EC 2.7.2.- Phosphotransferases with a carboxyl group as acceptor. [138 PDB entries]
EC 2.7.2.3 Phosphoglycerate kinase. [49 PDB entries]    
13pk

Pathway: Calvin Cycle (carbon fixation stages)
Reaction: Atp + 3-phospho-D-glycerate = adp + 3-phospho-D-glyceroyl phosphate.
 


ATP
+
3-phospho-D-glycerate
=
ADP
+
3-phospho-D-glyceroyl phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 49 PDB entries in enzyme class E.C.2.7.2.3

  PDB code Protein
13pk
Ternary complex of phosphoglycerate kinase from trypanosoma brucei
Source: Trypanosoma brucei. Organism_taxid: 5691. Variant: glycosomal version. Organelle: glycosome. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Chains: A, B, C, D (415 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
16pk
Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog
Source: Trypanosoma brucei. Organism_taxid: 5691. Variant: glycosomal version. Organelle: glycosome. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Chain: A (415 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group BIS is 65.00% similar to enzyme product ADP
1b9b
Triosephosphate isomerase of thermotoga maritima
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (252 residues) CATH domain: 3.20.20.70
1fw8
Circularly permuted phosphoglycerate kinase from yeast: pgk
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Chain: A (416 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group GOL is 54.55% similar to enzyme reactant 3-phospho-D-glycerate
1hdi
Pig muscle 3-phosphoglycerate kinase complexed with 3-pg and mgadp.
Source: Sus scrofa. Pig. Organism_taxid: 9823. Tissue: muscle
Chain: A (413 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group AMP is 85.00% similar to enzyme product ADP
1kf0
Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg
Source: Sus scrofa. Pig. Organism_taxid: 9823. Other_details: muscle
Chain: A (416 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ACP is 81.00% similar to enzyme product ADP
1lgi
Plasmodium falciparum 3-phosphoglycerate kinase
Source: Plasmodium falciparum. Strain: k1
Chain: A (413 residues)
1ltk
Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
Source: Plasmodium falciparum. Malaria parasite p. Falciparum. Organism_taxid: 5833. Gene: pgk. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C (417 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group AMP is 85.19% similar to enzyme product ADP
  Het Group GOL is 40.00% similar to enzyme product 3-phospho-D-glyceroyl
1php
Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms
Source: Geobacillus stearothermophilus. Organism_taxid: 1422
Chain: A (394 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group ADP corresponds to enzyme product ADP
1qpg
3-phosphoglycerate kinase, mutation r65q
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Chain: A (415 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group MAP is 78.00% similar to enzyme product ADP
1v6s
Crystal structure of phosphoglycerate kinase from thermus th hb8
Source: Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (390 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group GOL is 54.55% similar to enzyme reactant 3-phospho-D-glycerate
1vjc
Structure of pig muscle pgk complexed with mgatp
Source: Sus scrofa. Pig. Organism_taxid: 9823. Tissue: muscle
Chain: A (416 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group ATP corresponds to enzyme reactant ATP
1vjd
Structure of pig muscle pgk complexed with atp
Source: Sus scrofa. Pig. Organism_taxid: 9823. Tissue: muscle
Chain: A (416 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group ATP corresponds to enzyme reactant ATP
  Het Group PO4 is 45.00% similar to enzyme reactant 3-phospho-D-glycerate
1vpe
Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (398 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ANP is 81.00% similar to enzyme product ADP
1zmr
Crystal structure of the e. Coli phosphoglycerate kinase
Source: Escherichia coli. Organism_taxid: 562. Gene: pgk. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (386 residues) CATH domains: 3.40.50.1260 3.40.50.1260
2cun
Crystal structure of phosphoglycerate kinase from pyrococcus horikoshii ot3
Source: Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (405 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
2ie8
Crystal structure of thermus caldophilus phosphoglycerate kinase in the open conformation
Source: Thermus caldophilus. Organism_taxid: 272. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (390 residues) CATH domains: 3.40.50.1260 3.40.50.1260
2p9q
Crystal structure of phosphoglycerate kinase-2
Source: Mus musculus. House mouse. Organism_taxid: 10090. Strain: c3h/he. Gene: pgk2, pgk-2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (404 residues) CATH domains: 3.40.50.1260 3.40.50.1260
2p9t
Crystal structure of phosphoglycerate kinase-2 bound to 3- phosphoglycerate
Source: Mus musculus. House mouse. Organism_taxid: 10090. Strain: c3h/he. Gene: pgk2, pgk-2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (413 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
2paa
Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg
Source: Mus musculus. House mouse. Organism_taxid: 10090. Strain: c3h/he. Gene: pgk2, pgk-2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (413 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group ATP corresponds to enzyme reactant ATP
  Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
2pgk
The use of phase combination in the refinement of phosphoglycerate kinase at 2.5 angstroms resolution
Source: Equus caballus. Horse. Organism_taxid: 9796. Tissue: muscle
Chain: A (408 residues)
2wzb
The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (405 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
2wzc
The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (405 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
2wzd
The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (405 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
2x13
The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 3phosphogly
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (408 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
2x14
The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with amp-pc 3pg
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (405 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ACP is 81.00% similar to enzyme product ADP
2x15
The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (408 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group ATP corresponds to enzyme reactant ATP
  Het Group ADP corresponds to enzyme product ADP
  Het Group X15 corresponds to enzyme product 3-phospho-D-glyceroyl
2xe6
The complete reaction cycle of human phosphoglycerate kinase: the open binary complex with 3pg
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (413 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
2xe7
The complete reaction cycle of human phosphoglycerate kinase: the open ternary complex with 3pg and adp
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (413 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
2xe8
The complete reaction cycle of human phosphoglycerate kinase: the open ternary complex with 3pg and amp-pnp
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (413 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ACP is 81.25% similar to enzyme product ADP
2y3i
The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chains: A, D (414 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group LA8 corresponds to enzyme product ADP
2ybe
The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride at 2.0 a resolution
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (410 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group LA8 corresponds to enzyme product ADP
2zgv
Crystal structure of human phosphoglycerate kinase bound to d-adp
Source: Homo sapiens. Human. Gene: pgk1. Expressed in: escherichia coli.
Chain: A (403 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group ADP corresponds to enzyme product ADP
3b2b
Crystal structure of phosphoglycerate kinase from bacillus a
Source: Bacillus anthracis. Anthrax. Organism_taxid: 260799. Strain: sterne. Gene: pgk, bas4988, ba_5367, gbaa_5367. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (392 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group UNL is 46.15% similar to enzyme reactant 3-phospho-D-glycerate
3c39
Crystal structure of human phosphoglycerate kinase bound to 3-phosphoglycerate
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pgk1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
3c3a
Crystal structure of human phosphoglycerate kinase bound to 3-phosphoglycerate and l-adp
Source: Homo sapiens. Human. Gene: pgk1. Expressed in: escherichia coli.
Chains: A, B (406 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
3c3b
Crystal structure of human phosphoglycerate kinase bound to d-cdp
Source: Homo sapiens. Human. Gene: pgk1. Expressed in: escherichia coli.
Chains: A, B (403 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group PO4 is 45.00% similar to enzyme reactant 3-phospho-D-glycerate
  Het Group CDP is 85.00% similar to enzyme product ADP
3c3c
Crystal structure of human phosphoglycerate kinase bound to 3-phosphoglycerate and l-cdp
Source: Homo sapiens. Human. Gene: pgk1. Expressed in: escherichia coli.
Chains: A, B (403 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group CDP is 85.00% similar to enzyme product ADP
3oz7
Crystal structure of 3-phosphopglycerate kinase of plasmodiu falciparum
Source: Plasmodium falciparum. Organism_taxid: 36329. Strain: 3d7. Gene: pgk, pfi1105w. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (416 residues) CATH domains: 3.40.50.1260 3.40.50.1260
3oza
Crystal structure of plasmodium falciparum 3-phosphoglycerat
Source: Plasmodium falciparum. Organism_taxid: 36329. Strain: 3d7. Gene: pgk, pfi1105w. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C (417 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group GOL is 54.55% similar to enzyme reactant 3-phospho-D-glycerate
3pgk
The structure of yeast phosphoglycerate kinase at 0.25 nm re
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932
Chain: A (416 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group ATP corresponds to enzyme reactant ATP
  Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
3q3v
Crystal structure of phosphoglycerate kinase from campylobac jejuni.
Source: Campylobacter jejuni subsp. Jejuni nct organism_taxid: 192222. Gene: cj1402c, pgk. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (394 residues) CATH domains: 3.40.50.1260 3.40.50.1260
3uwd
Crystal structure of phosphoglycerate kinase from bacillus a
Source: Bacillus anthracis. Anthrax,anthrax bacterium. Organism_taxid: 1392. Strain: sterne. Gene: bas4988, ba_5367, gbaa_5367, pgk. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (392 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group UNL is 46.15% similar to enzyme reactant 3-phospho-D-glycerate
3zlb
Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae
Source: Streptococcus pneumoniae. Organism_taxid: 373153. Strain: d39. Atcc: 7466. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (398 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group GOL is 54.55% similar to enzyme reactant 3-phospho-D-glycerate
  Het Group ANP is 81.25% similar to enzyme product ADP
3zoz
The structure of human phosphoglycerate kinase with bound br stimulating anion.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (405 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
4axx
The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycer beryllium trifluoride
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (407 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligands:   Het Group 3PG corresponds to enzyme reactant 3-phospho-D-glycerate
  Het Group ADP corresponds to enzyme product ADP
4dg5
Crystal structure of staphylococcal phosphoglycerate kinase
Source: Staphylococcus aureus. Organism_taxid: 282458. Strain: mrsa252. Gene: pgk, sar0829. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (395 residues) CATH domains: 3.40.50.1260 3.40.50.1260
4ehj
An x-ray structure of a putative phosphogylcerate kinase fro francisella tularensis subsp. Tularensis schu s4
Source: Francisella tularensis subsp. Tularens organism_taxid: 177416. Strain: schu s4/schu 4. Gene: ftt_1367c, pgk. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (390 residues) CATH domains: 3.40.50.1260 3.40.50.1260
4fey
An x-ray structure of a putative phosphogylcerate kinase wit adp from francisella tularensis subsp. Tularensis schu s4
Source: Francisella tularensis subsp. Tularens organism_taxid: 177416. Strain: schu s4 / schu 4. Gene: ftt_1367c, pgk. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (392 residues) CATH domains: 3.40.50.1260 3.40.50.1260
Bound ligand:   Het Group ADP corresponds to enzyme product ADP