4gyf

X-ray diffraction
1.65Å resolution

Crystal structure of histidinol phosphate phosphatase (HISK) from Lactococcus lactis subsp. lactis Il1403 complexed with ZN, L-histidinol and phosphate

Released:
Entry authors: Fedorov AA, Fedorov EV, Ghodge S, Raushel FM, Almo SC

Function and Biology Details

Reaction catalysed:
L-histidinol phosphate + H(2)O = L-histidinol + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphatase Chain: A
Molecule details ›
Chain: A
Length: 284 amino acids
Theoretical weight: 33.24 KDa
Source organism: Lactococcus lactis subsp. lactis Il1403
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02150 (Residues: 2-269; Coverage: 100%)
Gene names: L37351, LL1216, hisK
Sequence domains: PHP domain
Structure domains: Metal-dependent hydrolases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21212
Unit cell:
a: 85.661Å b: 86.679Å c: 45.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.186
Expression system: Escherichia coli