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PDBsum entry 3odm

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protein ligands Protein-protein interface(s) links
Lyase PDB id
3odm
Jmol
Contents
Protein chains
(+ 2 more) 525 a.a. *
Ligands
AUC ×36
MLI ×5
Waters ×200
* Residue conservation analysis
PDB id:
3odm
Name: Lyase
Title: Archaeal-type phosphoenolpyruvate carboxylase
Structure: Phosphoenolpyruvate carboxylase. Chain: a, b, c, d, e, f, g, h. Synonym: pepcase, pepc. Engineered: yes
Source: Clostridium perfringens. Organism_taxid: 1502. Gene: cpe1094, ppca. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.95Å     R-factor:   0.178     R-free:   0.223
Authors: P.W.Dunten
Key ref: L.Dharmarajan et al. (2011). Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate. Proteins, 79, 1820-1829. PubMed id: 21491491
Date:
11-Aug-10     Release date:   02-Feb-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8XLE8  (CAPPA_CLOPE) -  Phosphoenolpyruvate carboxylase
Seq:
Struc:
 
Seq:
Struc:
537 a.a.
525 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.1.1.31  - Phosphoenolpyruvate carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-
Phosphate
+
oxaloacetate
Bound ligand (Het Group name = MLI)
matches with 60.00% similarity
= H(2)O
+ phosphoenolpyruvate
+ HCO(3)(-)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbon fixation   3 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    reference    
 
 
Proteins 79:1820-1829 (2011)
PubMed id: 21491491  
 
 
Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate.
L.Dharmarajan, J.L.Kraszewski, B.Mukhopadhyay, P.W.Dunten.
 
  ABSTRACT  
 
No abstract given.