PDBe 1uu1

X-ray diffraction
2.38Å resolution

Complex of Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (Apo-form)

Released:

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 335 amino acids
Theoretical weight: 39.35 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW 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: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 53.61Å b: 136.519Å c: 92.815Å
α: 90° β: 95.19° γ: 90°
R-values:
R R work R free
0.206 0.206 0.268
Expression system: Escherichia coli BL21(DE3)