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protein ligands metals links
Lyase PDB id
2py7
Jmol
Contents
Protein chain
535 a.a. *
Ligands
ATP
Metals
_MG
_MN ×2
Waters ×570
* Residue conservation analysis
PDB id:
2py7
Name: Lyase
Title: Crystal structure of e. Coli phosphoenolpyruvate carboxykina lys213ser complexed with atp-mg2+-mn2+
Structure: Phosphoenolpyruvate carboxykinase. Chain: x. Synonym: pep carboxykinase, phosphoenolpyruvate carboxylase engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: pcka. Expressed in: escherichia coli k12. Expression_system_taxid: 83333.
Resolution:
2.20Å     R-factor:   0.158     R-free:   0.218
Authors: L.T.J.Delbaere,J.J.H.Cotelesage,H.Goldie
Key ref: L.T.J.Delbaere et al. Crystal structure of e. Coli phosphoenolpyruvate carboxykinase mutant lys213ser. To be published,
Date:
15-May-07     Release date:   22-Apr-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P22259  (PCKA_ECOLI) -  Phosphoenolpyruvate carboxykinase [ATP]
Seq:
Struc: 		 
Seq:
Struc: 		540 a.a.
535 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.4.1.1.49  - Phosphoenolpyruvate carboxykinase (ATP).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2
ATP
Bound ligand (Het Group name = ATP)
corresponds exactly 		+ oxaloacetate
 = ADP
 + phosphoenolpyruvate
 + CO(2)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   2 terms 
  Biochemical function     catalytic activity     8 terms