2f8j

X-ray diffraction
2.4Å resolution

Crystal structure of Histidinol-phosphate aminotransferase (EC 2.6.1.9) (Imidazole acetol-phosphate transferase) (tm1040) from Thermotoga maritima at 2.40 A resolution

Released:
Source organism: Thermotoga maritima
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-194697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 347 amino acids
Theoretical weight: 40.81 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0D0 (Residues: 1-335; Coverage: 100%)
Gene names: TM_1040, hisC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 4 x PMP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21212
Unit cell:
a: 145.156Å b: 187.453Å c: 54.316Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.238
Expression system: Escherichia coli