PDBe 1hjk

X-ray diffraction
2.3Å resolution

ALKALINE PHOSPHATASE MUTANT H331Q

Released:
Source organism: Escherichia coli
Primary publication:
Trapping and visualization of a covalent enzyme-phosphate intermediate.
Nat. Struct. Biol. 4 618-22 (1997)
PMID: 9253408

Function and Biology Details

Reaction catalysed:
A phosphate monoester + H(2)O = an alcohol + phosphate
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkaline phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 449 amino acids
Theoretical weight: 47.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00634 (Residues: 23-471; Coverage: 100%)
Gene names: JW0374, b0383, phoA
Sequence domains: Alkaline phosphatase
Structure domains: Alkaline Phosphatase, subunit A

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I222
Unit cell:
a: 195.52Å b: 167.86Å c: 77.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.2
Expression system: Escherichia coli