› 3ffh

X-ray diffraction
2.31Å resolution

The crystal structure of histidinol-phosphate aminotransferase from Listeria innocua Clip11262.

Released:
DOI: 10.2210/pdb3ffh/pdb
PDB entry 3ffh coloured by chain, front view.
PDB entry 3ffh coloured by chain, side view.
PDB entry 3ffh coloured by chain, top view.
Source organism: Listeria innocua
Entry authors: Tan K, Gu M, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187840 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 363 amino acids
Theoretical weight: 40.56 KDa
Source organism: Listeria innocua
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92A83 (Residues: 1-360; Coverage: 100%)
Gene names: hisC, lin2039
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 9 x SO4
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 78.456Å b: 83.671Å c: 122.773Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.252
Expression system: Escherichia coli

Quick links