5iat

X-ray diffraction
1.67Å resolution

Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - apo-BaP4H

Released:

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-105243 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fe2OG dioxygenase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 24.71 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A4Y1WAP5 (Residues: 2-216; Coverage: 100%)
Gene name: GBAA_4459
Sequence domains: 2OG-Fe(II) oxygenase superfamily
Structure domains: q2cbj1_9rhob like domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P212121
Unit cell:
a: 51.563Å b: 80.117Å c: 103.827Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.211
Expression system: Escherichia coli