› 5pnt

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF A HUMAN LOW MOLECULAR WEIGHT PHOSPHOTYROSYL PHOSPHATASE. IMPLICATIONS FOR SUBSTRATE SPECIFICITY

Released:
DOI: 10.2210/pdb5pnt/pdb
PDB entry 5pnt coloured by chain, front view.
PDB entry 5pnt coloured by chain, side view.
PDB entry 5pnt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity.
Zhang M, Stauffacher CV, Lin D, Van Etten RL
J Biol Chem 273 21714-20 (1998)
PMID: 9705307

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-150269 (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: 17.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P24666 (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 MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 34.1Å b: 56.6Å c: 97.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.248
Expression system: Escherichia coli BL21

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Citations

5 review citations

Protein tyrosine phosphatases as potential therapeutic targets.
He et al. (2014)
4 more

16 mentions without citation

Therapeutic Targeting of Protein Tyrosine Phosphatases from Mycobacterium tuberculosis.
Ruddraraju et al. (2020)
15 more