Function and Biology Details
Reaction catalysed:
Cholesterol + O(2) = cholest-5-en-3-one + H(2)O(2)
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Vanillyl-alcohol oxidase, C-terminal subdomain 2
- Cholesterol oxidase, substrate-binding
- FAD-linked oxidase-like, C-terminal
- Cytokinin dehydrogenase, C-terminal domain superfamily
- FAD-binding, type PCMH, subdomain 2
- FAD linked oxidase, N-terminal
- FAD-binding domain, PCMH-type
- L-gulonolactone/D-arabinono-1,4-lactone oxidase-like
2 more domains
Structure domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
FAD-binding PCMH-type domain-containing protein (preferred)
PDBe Complex ID:
PDB-CPX-181962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-binding PCMH-type domain-containing protein
Molecule details ›
Chains: A, B
Length: 561 amino acids
Theoretical weight: 61.58 KDa
Source organism: Brevibacterium sterolicum
Expression system: Escherichia coli
UniProt:
Structure domains:
Length: 561 amino acids
Theoretical weight: 61.58 KDa
Source organism: Brevibacterium sterolicum
Expression system: Escherichia coli
UniProt:
- Canonical:
Q7SID9 (Residues: 1-561; Coverage: 100%)
Structure domains:
