› 5hv4

X-ray diffraction
2.35Å resolution

Crystal Structure of a Prolyl 4-Hydroxylase Complexed with Alpha-ketoglutarate from the Pathogenic Bacterium Bacillus anthracis in C2221

Released:
DOI: 10.2210/pdb5hv4/pdb
PDB 5hv4 coloured by chain and viewed from the front.
PDB 5hv4 coloured by chain and viewed from the side.
PDB 5hv4 coloured by chain and viewed from the top.
Source organism: Bacillus anthracis
Primary publication:
Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis.
Schnicker NJ, Dey M
Acta Crystallogr D Struct Biol 72 675-81 (2016)
PMID: 27139630

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fe2OG dioxygenase domain-containing protein Chain: A
Molecule details ›
Chain: A
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

3 bound ligands:
Ligand CD 5 x CD
Ligand AKG 1 x AKG
Ligand K 6 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2221
Unit cell:
a: 42.551Å b: 146.189Å c: 75.075Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.245
Expression system: Escherichia coli

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Citations

2 citation in other articles

Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.
Schnicker et al. (2017)
1 more