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PDBsum entry 2izz

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
2izz
Jmol
Contents
Protein chains
272 a.a. *
Ligands
NAD ×5
EDO ×7
Waters ×695
* Residue conservation analysis
PDB id:
2izz
Name: Oxidoreductase
Title: Crystal structure of human pyrroline-5-carboxylate reductase
Structure: Pyrroline-5-carboxylate reductase 1. Chain: a, b, c, d, e. Fragment: catalytic domain, residues 1-300. Synonym: pyrroline-5-carboxylate reductase, p5cr 1, p5c red engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Biol. unit: Decamer (from PDB file)
Resolution:
1.95Å     R-factor:   0.167     R-free:   0.190
Authors: A.C.W.Pike,K.Guo,K.Kavanagh,E.S.Pilka,G.Berridge,S.Colebrook E.Salah,P.Savitsky,E.Papagrigoriou,A.P.Turnbull,F.Von Delft C.Arrowsmith,A.Edwards,J.Weigelt,M.Sundstrom,U.Oppermann
Key ref: A.C.W.Pike et al. Crystal structure of human pyrroline-5-Carboxylate reductase. To be published, .
Date:
31-Jul-06     Release date:   01-Aug-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P32322  (P5CR1_HUMAN) -  Pyrroline-5-carboxylate reductase 1, mitochondrial
Seq:
Struc:
319 a.a.
272 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.5.1.2  - Pyrroline-5-carboxylate reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Proline Biosynthesis
      Reaction: L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H
L-proline
+
NAD(P)(+)
Bound ligand (Het Group name = NAD)
matches with 91.67% similarity
= 1-pyrroline-5-carboxylate
+ NAD(P)H
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrion   2 terms 
  Biological process     small molecule metabolic process   9 terms 
  Biochemical function     protein binding     4 terms