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PDBsum entry 3nqs

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Oxidoreductase PDB id
3nqs

 

 

 

 

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Contents
Protein chains
412 a.a. *
Ligands
HEM ×2
H4B-_NO ×2
AT2 ×2
GOL
EDO ×3
SO4 ×5
BOG
Waters ×598
* Residue conservation analysis
PDB id:
3nqs
Name: Oxidoreductase
Title: Crystal structure of inducible nitric oxide synthase with n- nitrosated-pterin
Structure: Nitric oxide synthase, inducible. Chain: a, b. Fragment: unp residues 66-498. Synonym: inducible no synthase, inducible nos, inos, nos type ii, macrophage nos, mac-nos. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Strain: macrophage. Gene: inosl, nos2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.204     R-free:   0.229
Authors: R.J.Rosenfeld,E.D.Getzoff,J.A.Tainer
Key ref: R.J.Rosenfeld et al. (2010). Nitric-oxide synthase forms N-NO-pterin and S-NO-cys: implications for activity, allostery, and regulation. J Biol Chem, 285, 31581-31589. PubMed id: 20659888
Date:
29-Jun-10     Release date:   21-Jul-10    
PROCHECK
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 Headers
 References

Protein chains
P29477  (NOS2_MOUSE) -  Nitric oxide synthase, inducible from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1144 a.a.
413 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.14.13.39  - nitric-oxide synthase (NADPH).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 L-arginine + 3 NADPH + 4 O2 + H+ = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
2 × L-arginine
+ 3 × NADPH
+ 4 × O2
+ H(+)
= 2 × L-citrulline
+ 2 × nitric oxide
+ 3 × NADP(+)
+ 4 × H2O
Bound ligand (Het Group name = NO)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Biol Chem 285:31581-31589 (2010)
PubMed id: 20659888  
 
 
Nitric-oxide synthase forms N-NO-pterin and S-NO-cys: implications for activity, allostery, and regulation.
R.J.Rosenfeld, J.Bonaventura, B.R.Szymczyna, M.J.MacCoss, A.S.Arvai, J.R.Yates, J.A.Tainer, E.D.Getzoff.
 
  ABSTRACT  
 
No abstract given.

 

 

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