› 1ajc

X-ray diffraction
2.5Å resolution

THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY

Released:
DOI: 10.2210/pdb1ajc/pdb
PDB entry 1ajc coloured by chain, front view.
PDB entry 1ajc coloured by chain, side view.
PDB entry 1ajc coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase.
Dealwis CG, Brennan C, Christianson K, Mandecki W, Abad-Zapatero C
Biochemistry 34 13967-73 (1995)
PMID: 7577993

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: 47.04 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

2 bound ligands:
Ligand ZN 4 x ZN
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 195.02Å b: 166.93Å c: 76.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.162 not available
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Structural studies of human placental alkaline phosphatase in complex with functional ligands.
Llinas et al. (2005)
10 more

1 mention without citation

Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site.
Sunden et al. (2015)