› 1bvh

Solution NMR

SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE

Released:
DOI: 10.2210/pdb1bvh/pdb
PDB entry 1bvh coloured by chain, ensemble of 15 models, front view.
PDB entry 1bvh coloured by chain, ensemble of 15 models, side view.
PDB entry 1bvh coloured by chain, ensemble of 15 models, top view.
Source organism: Bos taurus
Primary publication:
Solution structure of a low molecular weight protein tyrosine phosphatase.
Logan TM, Zhou MM, Nettesheim DG, Meadows RP, Van Etten RL, Fesik SW
Biochemistry 33 11087-96 (1994)
PMID: 7727361

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-145642 (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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis.
Zhang ZY. (1998)
3 more

3 mentions without citation

Systematic comparison of crystal and NMR protein structures deposited in the protein data bank.
Sikic et al. (2010)
2 more