› 2g6n

X-ray diffraction
1.9Å resolution

Strcture of rat nNOS heme domain (BH2 bound) complexed with CO

Released:
DOI: 10.2210/pdb2g6n/pdb
PDB entry 2g6n coloured by chain, front view.
PDB entry 2g6n coloured by chain, side view.
PDB entry 2g6n coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structural studies of constitutive nitric oxide synthases with diatomic ligands bound.
Li H, Igarashi J, Jamal J, Yang W, Poulos TL
J Biol Inorg Chem 11 753-68 (2006)
PMID: 16804678

Function and Biology Details

Reaction catalysed: 
(1a) 2 L-arginine + 2 NADPH + 2 O(2) = 2 N(omega)-hydroxy-L-arginine + 2 NADP(+) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151520 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide synthase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 48.61 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P29476 (Residues: 299-718; Coverage: 29%)
Gene names: Bnos, Nos1
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
5 bound ligands:
Ligand ACT 2 x ACT
Ligand ZN 1 x ZN
Ligand HBI 2 x HBI
Ligand ARG 2 x ARG
Ligand CMO 2 x CMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 51.97Å b: 111.53Å c: 164.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.262
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Carbon monoxide--physiology, detection and controlled release.
Heinemann et al. (2014)
4 more