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PDBsum entry 4bxc

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protein ligands Protein-protein interface(s) links
Lyase PDB id
4bxc
Jmol
Contents
Protein chains
929 a.a.
Ligands
G6P ×2
SO4 ×2
EDO ×2
TRS
Waters ×13
PDB id:
4bxc
Name: Lyase
Title: Resolving the activation site of positive regulators in plant phosphoenolpyruvate carboxylase
Structure: C4 phosphoenolpyruvate carboxylase. Chain: a, b. Synonym: c4 pepc, c4 pepcase, ppca, photosynthetic pepcase. Engineered: yes
Source: Flaveria trinervia. Organism_taxid: 4227. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.86Å     R-factor:   0.184     R-free:   0.220
Authors: D.Schlieper,K.Foerster,J.K.Paulus,G.Groth
Key ref: D.Schlieper et al. (2014). Resolving the activation site of positive regulators in plant phosphoenolpyruvate carboxylase. Mol Plant, 7, 437-440. PubMed id: 24043710 DOI: 10.1093/mp/sst130
Date:
10-Jul-13     Release date:   02-Oct-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P30694  (CAPPA_FLATR) -  C4 phosphoenolpyruvate carboxylase
Seq:
Struc:
 
Seq:
Struc:
966 a.a.
929 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 = G6P)
matches with 47.06% 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!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1093/mp/sst130 Mol Plant 7:437-440 (2014)
PubMed id: 24043710  
 
 
Resolving the activation site of positive regulators in plant phosphoenolpyruvate carboxylase.
D.Schlieper, K.Förster, J.K.Paulus, G.Groth.
 
  ABSTRACT  
 
No abstract given.