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PDBsum entry 3tgm

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protein ligands Protein-protein interface(s) links
Oxidoreductase/oxidoreductase inhibitor PDB id
3tgm
Jmol
Contents
Protein chain
214 a.a.
Ligands
HEM-3TG ×2
HEZ
Waters ×26
PDB id:
3tgm
Name: Oxidoreductase/oxidoreductase inhibitor
Title: X-ray crystal structure of human heme oxygenase-1 in complex (1h-imidazol-1-yl)-4,4-diphenyl-2 butanone
Structure: Heme oxygenase 1. Chain: a, b. Fragment: residues 1-233. Synonym: ho-1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho, ho1. Expressed in: escherichia coli. Expression_system_taxid: 668369.
Resolution:
2.85Å     R-factor:   0.225     R-free:   0.264
Authors: M.N.Rahman,Z.Jia
Key ref: M.N.Rahman et al. (2012). A novel, "double-clamp" binding mode for human heme oxygenase-1 inhibition. PLoS One, 7, e29514. PubMed id: 22276118
Date:
17-Aug-11     Release date:   01-Feb-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09601  (HMOX1_HUMAN) -  Heme oxygenase 1
Seq:
Struc:
288 a.a.
214 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.14.99.3  - Heme oxygenase (biliverdin-producing).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O
Protoheme
Bound ligand (Het Group name = HEM)
matches with 95.45% similarity
+ 3 × AH(2)
+ 3 × O(2)
= biliverdin
+ Fe(2+)
+ CO
+ 3 × A
+ 3 × H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     heme oxygenase (decyclizing) activity     1 term  

 

 
    reference    
 
 
PLoS One 7:e29514 (2012)
PubMed id: 22276118  
 
 
A novel, "double-clamp" binding mode for human heme oxygenase-1 inhibition.
M.N.Rahman, J.Z.Vlahakis, D.Vukomanovic, W.Lee, W.A.Szarek, K.Nakatsu, Z.Jia.
 
  ABSTRACT  
 
No abstract given.