Function and Biology Details
Reaction catalysed:
L-proline-[procollagen] + 2-oxoglutarate + O(2) = trans-4-hydroxy-L-proline-[procollagen] + succinate + CO(2)
Biochemical function:
Biological process:
- not assigned
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Prolyl 4-hydroxylase subunit alpha-1 and peptide (preferred)
PDBe Complex ID:
PDB-CPX-146696 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Prolyl 4-hydroxylase subunit alpha-1
Molecule details ›
Chains: A, B
Length: 251 amino acids
Theoretical weight: 29.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Prolyl 4-Hydroxylase alpha-subunit, N-terminal region
Structure domains:
Length: 251 amino acids
Theoretical weight: 29.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P13674 (Residues: 18-261; Coverage: 47%)
Sequence domains: Prolyl 4-Hydroxylase alpha-subunit, N-terminal region
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup:
P21212
Expression system: Escherichia coli BL21(DE3)
