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PDBsum entry 2x14

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protein ligands metals links
Transferase PDB id
2x14
Jmol
Contents
Protein chain
405 a.a. *
Ligands
3PG
ACP
Metals
_MG
Waters ×218
* Residue conservation analysis
PDB id:
2x14
Name: Transferase
Title: The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with amp-pc 3pg
Structure: Phosphoglycerate kinase 1. Chain: a. Synonym: primer recognition protein 2, prp 2, cell migration-inducing gene 10 protein. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.90Å     R-factor:   0.189     R-free:   0.228
Authors: M.W.Bowler,M.J.Cliff,J.P.M.Marston,N.J.Baxter,A.M.H.Hownslow A.V.Varga,J.Szabo,M.Vas,G.M.Blackburn,J.P.Waltho
Key ref: M.W.Bowler et al. The structure of human phosphoglycerate kinase in its active conformation in complex with ground state anal. To be published, .
Date:
21-Dec-09     Release date:   29-Dec-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00558  (PGK1_HUMAN) -  Phosphoglycerate kinase 1
Seq:
Struc:
417 a.a.
405 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.2.3  - Phosphoglycerate kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Calvin Cycle (carbon fixation stages)
      Reaction: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
ATP
+
3-phospho-D-glycerate
Bound ligand (Het Group name = 3PG)
corresponds exactly
=
ADP
Bound ligand (Het Group name = ACP)
matches with 81.00% similarity
+ 3-phospho-D-glyceroyl phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   4 terms 
  Biological process     small molecule metabolic process   7 terms 
  Biochemical function     nucleotide binding     6 terms