› 4z9b

X-ray diffraction
2.41Å resolution

Crystal structure of Low Molecular Weight Protein Tyrosine Phosphatase isoform A complexed with benzylphosphonic acid

Released:
DOI: 10.2210/pdb4z9b/pdb
PDB entry 4z9b coloured by chain, front view.
PDB entry 4z9b coloured by chain, side view.
PDB entry 4z9b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the apo form and a complex of human LMW-PTP with a phosphonic acid provide new evidence of a secondary site potentially related to the anchorage of natural substrates.
Fonseca EMB, Trivella DBB, Scorsato V, Dias MP, Bazzo NL, Mandapati KR, de Oliveira FL, Ferreira-Halder CV, Pilli RA, Miranda PCML, Aparicio R
Bioorg Med Chem 23 4462-4471 (2015)
PMID: 26117648

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 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: 164 amino acids
Theoretical weight: 18.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P24666 (Residues: 1-158; Coverage: 100%)
Gene name: ACP1
Sequence domains: Low molecular weight phosphotyrosine protein phosphatase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand B85 1 x B85
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 32.088Å b: 54.287Å c: 97.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.215 0.301
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Phosphonic acid: preparation and applications.
Sevrain et al. (2017)
1 more