› 1alk

X-ray diffraction
2Å resolution

REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS

Released:
DOI: 10.2210/pdb1alk/pdb
PDB entry 1alk coloured by chain, front view.
PDB entry 1alk coloured by chain, side view.
PDB entry 1alk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis.
Kim EE, Wyckoff HW
J Mol Biol 218 449-64 (1991)
PMID: 2010919

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: 47.09 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
Spacegroup: I222
Unit cell:
a: 195.3Å b: 167.4Å c: 76.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 not available
Expression system: Escherichia coli

Quick links

Citations

43 review citations

Calcineurin: form and function.
Rusnak et al. (2000)
42 more

31 mentions without citation

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy et al. (2008)
30 more