› 4gc3

X-ray diffraction
1.32Å resolution

Crystal structure of L-HISTIDINOL PHOSPHATE PHOSPHATASE (HISK) from Lactococcus lactis subsp. lactis Il1403 complexed with ZN and sulfate

Released:
DOI: 10.2210/pdb4gc3/pdb
PDB entry 4gc3 coloured by chain, front view.
PDB entry 4gc3 coloured by chain, side view.
PDB entry 4gc3 coloured by chain, top view.
Source organism: Lactococcus lactis subsp. lactis Il1403
Primary publication:
Structural and mechanistic characterization of L-histidinol phosphate phosphatase from the polymerase and histidinol phosphatase family of proteins.
Ghodge SV, Fedorov AA, Fedorov EV, Hillerich B, Seidel R, Almo SC, Raushel FM
Biochemistry 52 1101-12 (2013)
PMID: 23327428

Function and Biology Details

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

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

2 bound ligands:
Ligand ZN 3 x ZN
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 51.48Å b: 76.495Å c: 78.057Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.152 0.162
Expression system: Escherichia coli

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Citations

1 review citation

Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks.
Gerlt et al. (2015)
13 other articles

1 mention without citation

Structural and mechanistic characterization of L-histidinol phosphate phosphatase from the polymerase and histidinol phosphatase family of proteins.
Ghodge et al. (2013)