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:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143921 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-1
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: EF-hand domain pair
Length: 148 amino acids
Theoretical weight: 16.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P0DP23 (Residues: 2-149; Coverage: 99%)
Sequence domains: EF-hand domain pair
Nitric oxide synthase, inducible
Molecule details ›
Chain: B
Length: 17 amino acids
Theoretical weight: 1.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Length: 17 amino acids
Theoretical weight: 1.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P35228 (Residues: 515-531; Coverage: 2%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
71%
Refinement method:
DGSA-distance geometry simulated annealing
Expression system: Escherichia coli
