› 1e5s

X-ray diffraction
2.4Å resolution

Proline 3-hydroxylase (type II) - Iron form

Released:
DOI: 10.2210/pdb1e5s/pdb
PDB entry 1e5s coloured by chain, front view.
PDB entry 1e5s coloured by chain, side view.
PDB entry 1e5s coloured by chain, top view.
Source organism: Streptomyces sp. TH1
Primary publication:
Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.
Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ
Eur J Biochem 268 6625-36 (2001)
PMID: 11737217

Function and Biology Details

Reaction catalysed: 
L-proline + 2-oxoglutarate + O(2) = cis-3-hydroxy-L-proline + succinate + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126722 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-proline cis-3-hydroxylase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 290 amino acids
Theoretical weight: 33.62 KDa
Source organism: Streptomyces sp. TH1
UniProt:
  • Canonical: O09345 (Residues: 1-290; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand FE2 2 x FE2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P3121
Unit cell:
a: 72.78Å b: 72.78Å c: 224.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.271

Quick links

Citations

15 review citations

Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia.
Guzy et al. (2006)
14 more

7 mentions without citation

Prolyl 4-hydroxylase.
Gorres et al. (2010)
6 more