› 4bt9

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-238) TYPE I FROM HUMAN

Released:
DOI: 10.2210/pdb4bt9/pdb
PDB entry 4bt9 coloured by chain, front view.
PDB entry 4bt9 coloured by chain, side view.
PDB entry 4bt9 coloured by chain, top view.
Source organisms:
Primary publication:
The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase.
Anantharajan J, Koski MK, Kursula P, Hieta R, Bergmann U, Myllyharju J, Wierenga RK
Structure 21 2107-18 (2013)
PMID: 24207127

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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146695 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Prolyl 4-hydroxylase subunit alpha-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 239 amino acids
Theoretical weight: 27.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13674 (Residues: 18-255; Coverage: 46%)
Gene names: P4HA, P4HA1
Sequence domains: Prolyl 4-Hydroxylase alpha-subunit, N-terminal region
Structure domains:
(PRO-PRO-GLY)3 PEPTIDE Chain: C
Molecule details ›
Chain: C
Length: 9 amino acids
Theoretical weight: 772 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P21212
Unit cell:
a: 72.28Å b: 100.93Å c: 68.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.174 0.222
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

3 review citations

2-Oxoglutarate-Dependent Oxygenases.
Islam et al. (2018)
2 more

1 mention without citation

Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): High affinity peptides have a PxGP sequence motif.
Murthy et al. (2018)