› 1g5b

X-ray diffraction
2.15Å resolution

BACTERIOPHAGE LAMBDA SER/THR PROTEIN PHOSPHATASE

Released:
DOI: 10.2210/pdb1g5b/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1g5b coloured by chain, front view.
PDB entry 1g5b coloured by chain, side view.
PDB entry 1g5b coloured by chain, top view.
Source organism: Escherichia virus Lambda
Primary publication:
Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes.
Voegtli WC, White DJ, Reiter NJ, Rusnak F, Rosenzweig AC
Biochemistry 39 15365-74 (2000)
PMID: 11112522

Function and Biology Details

Reaction catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-137256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 221 amino acids
Theoretical weight: 25.19 KDa
Source organism: Escherichia virus Lambda
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03772 (Residues: 1-221; Coverage: 100%)
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

3 bound ligands:
Ligand MN 6 x MN
Ligand HG 2 x HG
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2221
Unit cell:
a: 160.4Å b: 177.3Å c: 79.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Nucleases: diversity of structure, function and mechanism.
Yang W. (2011)
4 more

12 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
11 more