› 2w5x

X-ray diffraction
1.99Å resolution

Structure of TAB5 alkaline phosphatase mutant His 135 Glu with Mg bound in the M3 site.

Released:
DOI: 10.2210/pdb2w5x/pdb
PDB entry 2w5x coloured by chain, front view.
PDB entry 2w5x coloured by chain, side view.
PDB entry 2w5x coloured by chain, top view.
Source organism: Antarctic bacterium TAB5
Primary publication:
Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatases.
Koutsioulis D, Lyskowski A, Mäki S, Guthrie E, Feller G, Bouriotis V, Heikinheimo P
Protein Sci 19 75-84 (2010)
PMID: 19916164

Function and Biology Details

Reaction catalysed: 
A phosphate monoester + H(2)O = an alcohol + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkaline phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 375 amino acids
Theoretical weight: 40.48 KDa
Source organism: Antarctic bacterium TAB5
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KWY4 (Residues: 1-375; Coverage: 100%)
Gene name: phoA
Sequence domains: Alkaline phosphatase
Structure domains: Alkaline Phosphatase, subunit A

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand MG 4 x MG
1 modified residue:
Ligand SEP 2 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 70.42Å b: 173.19Å c: 55.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.161 0.204
Expression system: Escherichia coli

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Citations

2 review citations

One is enough: insights into the two-metal ion nuclease mechanism from global analysis and computational studies.
Dupureur CM. (2010)
1 more

1 mention without citation

Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatases.
Koutsioulis et al. (2010)