› 1e5r

X-ray diffraction
2.3Å resolution

Proline 3-hydroxylase (type II) -apo form

Released:
DOI: 10.2210/pdb1e5r/pdb
PDB entry 1e5r coloured by chain, front view.
PDB entry 1e5r coloured by chain, side view.
PDB entry 1e5r 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P3121
Unit cell:
a: 72.54Å b: 72.54Å c: 223.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.225 0.225 0.275

Quick links

Citations

16 review citations

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

3 mentions without citation

Recent examples of α-ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses.
Gao et al. (2018)
2 more