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PDBsum entry 3n8v

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3n8v

 

 

 

 

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Contents
Protein chains
553 a.a. *
Ligands
NAG-NDG ×2
NAG-NAG ×2
NAG-NDG-BMA-MAN-
MAN
NAG-NDG-BMA-BMA
HEM ×2
BOG ×5
GOL
Waters ×224
* Residue conservation analysis
PDB id:
3n8v
Name: Oxidoreductase
Title: Crystal structure of unoccupied cyclooxygenase-1
Structure: Prostaglandin g/h synthase 1. Chain: a, b. Synonym: cyclooxygenase-1, cox-1, prostaglandin-endoperoxide synthase 1, prostaglandin h2 synthase 1, pgh synthase 1, pghs-1, phs 1. Engineered: yes
Source: Ovis aries. Sheep. Organism_taxid: 9940. Strain: sheep. Gene: cox1, ptgs1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Resolution:
3.05Å     R-factor:   0.204     R-free:   0.235
Authors: R.S.Sidhu
Key ref: R.S.Sidhu et al. (2010). Comparison of cyclooxygenase-1 crystal structures: cross-talk between monomers comprising cyclooxygenase-1 homodimers. Biochemistry, 49, 7069-7079. PubMed id: 20669977
Date:
28-May-10     Release date:   28-Jul-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P05979  (PGH1_SHEEP) -  Prostaglandin G/H synthase 1 from Ovis aries
Seq:
Struc:
 
Seq:
Struc:
600 a.a.
553 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.14.99.1  - prostaglandin-endoperoxide synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = prostaglandin H2 + A + H2O
(5Z,8Z,11Z,14Z)-eicosatetraenoate
+ AH2
+ 2 × O2
= prostaglandin H2
+
+ H2O
Bound ligand (Het Group name = HEM)
matches with 51.11% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Biochemistry 49:7069-7079 (2010)
PubMed id: 20669977  
 
 
Comparison of cyclooxygenase-1 crystal structures: cross-talk between monomers comprising cyclooxygenase-1 homodimers.
R.S.Sidhu, J.Y.Lee, C.Yuan, W.L.Smith.
 
  ABSTRACT  
 
No abstract given.

 

 

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