› 1elz

X-ray diffraction
2.8Å resolution

E. COLI ALKALINE PHOSPHATASE MUTANT (S102G)

Released:
DOI: 10.2210/pdb1elz/pdb
PDB entry 1elz coloured by chain, front view.
PDB entry 1elz coloured by chain, side view.
PDB entry 1elz coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102.
Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER
J Mol Biol 277 647-62 (1998)
PMID: 9533886

Function and Biology Details

Reaction catalysed: 
A phosphate monoester + H(2)O = an alcohol + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132772 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkaline phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 449 amino acids
Theoretical weight: 47.06 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:
Ligand ZN 4 x ZN
Ligand MG 2 x MG
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6322
Unit cell:
a: 164.57Å b: 164.5Å c: 138.59Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.138 0.138 0.173
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cellular function and molecular structure of ecto-nucleotidases.
Zimmermann et al. (2012)
1 more

2 mentions without citation

Prediction of functional sites by analysis of sequence and structure conservation.
Panchenko et al. (2004)
1 more