3euc

X-ray diffraction
2.05Å resolution

Crystal structure of histidinol-phosphate aminotransferase (YP_297314.1) from RALSTONIA EUTROPHA JMP134 at 2.05 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)
PDBe Complex ID:
PDB-CPX-175205 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 367 amino acids
Theoretical weight: 40.45 KDa
Source organism: Cupriavidus pinatubonensis JMP134
Expression system: Escherichia coli
UniProt:
  • Canonical: Q46WL3 (Residues: 1-366; Coverage: 100%)
Gene names: Reut_A3110, hisC2
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 76.579Å b: 93.433Å c: 111.341Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.237
Expression system: Escherichia coli