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PDBsum entry 3n9y

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protein ligands Protein-protein interface(s) links
Oxidoreductase, electron transport PDB id
3n9y
Jmol
Contents
Protein chains
471 a.a.
68 a.a.
Ligands
HEM ×2
CLR ×2
FES ×2
Waters ×505
PDB id:
3n9y
Name: Oxidoreductase, electron transport
Title: Crystal structure of human cyp11a1 in complex with cholester
Structure: Cholesterol side-chain cleavage enzyme. Chain: a, b. Fragment: unp residues 41-521. Synonym: cytochrome p450 11a1, cypxia1, cytochrome p450(scc cholesterol desmolase. Engineered: yes. Adrenodoxin. Chain: c, d. Fragment: unp residues 62-175.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cyp11a, cyp11a1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: adrenodoxin, adx, fdx1.
Resolution:
2.10Å     R-factor:   0.207     R-free:   0.242
Authors: N.V.Strushkevich,F.Mackenzie,W.Tempel,A.Botchkarev,C.H.Arrow A.M.Edwards,C.Bountra,J.U.Weigelt,H.Park,Structural Genomic Consortium (Sgc)
Key ref: N.Strushkevich et al. (2011). Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system. Proc Natl Acad Sci U S A, 108, 10139-10143. PubMed id: 21636783 DOI: 10.1073/pnas.1019441108
Date:
31-May-10     Release date:   08-Jun-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P05108  (CP11A_HUMAN) -  Cholesterol side-chain cleavage enzyme, mitochondrial
Seq:
Struc:
 
Seq:
Struc:
521 a.a.
471 a.a.
Protein chains
Pfam   ArchSchema ?
P10109  (ADX_HUMAN) -  Adrenodoxin, mitochondrial
Seq:
Struc:
184 a.a.
68 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   7 terms 
  Biological process     small molecule metabolic process   62 terms 
  Biochemical function     electron carrier activity     11 terms  

 

 
DOI no: 10.1073/pnas.1019441108 Proc Natl Acad Sci U S A 108:10139-10143 (2011)
PubMed id: 21636783  
 
 
Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system.
N.Strushkevich, F.MacKenzie, T.Cherkesova, I.Grabovec, S.Usanov, H.W.Park.
 
  ABSTRACT  
 
No abstract given.