› 1kh9

X-ray diffraction
2.5Å resolution

E. COLI ALKALINE PHOSPHATASE MUTANT (D153GD330N) COMPLEX WITH PHOSPHATE

Released:
DOI: 10.2210/pdb1kh9/pdb
PDB entry 1kh9 coloured by chain, front view.
PDB entry 1kh9 coloured by chain, side view.
PDB entry 1kh9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase.
Le Du MH, Lamoure C, Muller BH, Bulgakov OV, Lajeunesse E, Ménez A, Boulain JC
J Mol Biol 316 941-53 (2002)
PMID: 11884134

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 1 x MG
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P6322
Unit cell:
a: 164.01Å b: 164.01Å c: 138.878Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.25
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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