3get

X-ray diffraction
2.01Å resolution

Crystal structure of putative histidinol-phosphate aminotransferase (NP_281508.1) from Campylobacter jejuni at 2.01 A resolution

Released:
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Reaction catalysed:
L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 365 amino acids
Theoretical weight: 41.94 KDa
Source organism: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9PII2 (Residues: 1-364; Coverage: 100%)
Gene names: Cj0317, hisC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

2 bound ligands:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 53.745Å b: 79.42Å c: 166.918Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.235
Expression system: Escherichia coli