Function and Biology Details
Reactions catalysed:
(1a) 2 L-arginine + 2 NADPH + 2 O(2) = 2 N(omega)-hydroxy-L-arginine + 2 NADP(+) + 2 H(2)O
Acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Chloramphenicol acetyltransferase
- Nitric oxide synthase, N-terminal
- Chloramphenicol acetyltransferase, active site
- Chloramphenicol acetyltransferase-like domain superfamily
- Nitric oxide synthase, domain 3 superfamily
- Nitric oxide synthase, domain 2 superfamily
- Nitric oxide synthase, oxygenase subunit
- Nitric oxide synthase, N-terminal domain superfamily
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
Nitric oxide synthase, inducible (preferred)
PDBe Complex ID:
PDB-CPX-151525 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nitric oxide synthase, inducible
Molecule details ›
Chain: A
Length: 388 amino acids
Theoretical weight: 45.14 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:
Length: 388 amino acids
Theoretical weight: 45.14 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P29477 (Residues: 115-498; Coverage: 34%)
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:
Chloramphenicol acetyltransferase
Molecule details ›
Chain: B
Length: 219 amino acids
Theoretical weight: 25.69 KDa
Source organism: Escherichia coli
UniProt:
Sequence domains: Chloramphenicol acetyltransferase
Structure domains: Chloramphenicol acetyltransferase-like domain
Length: 219 amino acids
Theoretical weight: 25.69 KDa
Source organism: Escherichia coli
UniProt:
- Canonical: P62577 (Residues: 1-219; Coverage: 100%)
Sequence domains: Chloramphenicol acetyltransferase
Structure domains: Chloramphenicol acetyltransferase-like domain
