› 1tjc

X-ray diffraction
2.3Å resolution

Crystal structure of peptide-substrate-binding domain of human type I collagen prolyl 4-hydroxylase

Released:
DOI: 10.2210/pdb1tjc/pdb
PDB entry 1tjc coloured by chain, front view.
PDB entry 1tjc coloured by chain, side view.
PDB entry 1tjc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues.
Pekkala M, Hieta R, Bergmann U, Kivirikko KI, Wierenga RK, Myllyharju J
J Biol Chem 279 52255-61 (2004)
PMID: 15456751

Function and Biology Details

Reaction catalysed: 
L-proline-[procollagen] + 2-oxoglutarate + O(2) = trans-4-hydroxy-L-proline-[procollagen] + succinate + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prolyl 4-hydroxylase subunit alpha-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 108 amino acids
Theoretical weight: 12.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P13674 (Residues: 161-261; Coverage: 20%)
Gene names: P4HA, P4HA1
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P32
Unit cell:
a: 55.98Å b: 55.98Å c: 105.43Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.224 0.259
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

5 mentions without citation

TPRpred: a tool for prediction of TPR-, PPR- and SEL1-like repeats from protein sequences.
Karpenahalli et al. (2007)
4 more