Function and Biology Details
Reaction catalysed:
[Protein]-L-arginine + 2-oxoglutarate + O(2) = [protein]-(3R)-3-hydroxy-L-arginine + succinate + CO(2)
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185372 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bifunctional peptidase and arginyl-hydroxylase JMJD5
Molecule details ›
Chain: A
Length: 255 amino acids
Theoretical weight: 29.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Cupin-like domain
Structure domains: Cupin
Length: 255 amino acids
Theoretical weight: 29.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q8N371 (Residues: 183-416; Coverage: 56%)
Sequence domains: Cupin-like domain
Structure domains: Cupin
RCC1 domain-containing protein 1
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 584 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 5 amino acids
Theoretical weight: 584 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: A6NED2 (Residues: 139-143; Coverage: 1%)
