› 1z12

X-ray diffraction
2.2Å resolution

Crystal Structure of Bovine Low Molecular Weight PTPase Complexed with Vanadate

Released:
DOI: 10.2210/pdb1z12/pdb
PDB entry 1z12 coloured by chain, front view.
PDB entry 1z12 coloured by chain, side view.
PDB entry 1z12 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate.
Zhang M, Zhou M, Van Etten RL, Stauffacher CV
Biochemistry 36 15-23 (1997)
PMID: 8993313

Function and Biology Details

Reactions catalysed: 
A phosphate monoester + H(2)O = an alcohol + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-536327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Low molecular weight phosphotyrosine protein phosphatase Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 17.95 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P11064 (Residues: 2-158; Coverage: 99%)
Gene name: ACP1
Sequence domains: Low molecular weight phosphotyrosine protein phosphatase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand VO4 1 x VO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 95.3Å b: 43.4Å c: 41.2Å
α: 90° β: 113.4° γ: 90°
R-values:
R R work R free
0.173 not available not available
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Vanadium in cancer treatment.
Evangelou AM. (2002)
24 more

2 mentions without citation

Probing the origins of catalytic discrimination between phosphate and sulfate monoester hydrolysis: comparative analysis of alkaline phosphatase and protein tyrosine phosphatases.
Andrews et al. (2014)
1 more