› 5jnv

X-ray diffraction
1.6Å resolution

Crystal structure of bovine low molecular weight protein tyrosine phosphatase (LMPTP) mutant (W49Y N50E) complexed with HEPES

Released:
DOI: 10.2210/pdb5jnv/pdb
PDB entry 5jnv coloured by chain, front view.
PDB entry 5jnv coloured by chain, side view.
PDB entry 5jnv coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Diabetes reversal by inhibition of the low-molecular-weight tyrosine phosphatase.
Stanford SM, Aleshin AE, Zhang V, Ardecky RJ, Hedrick MP, Zou J, Ganji SR, Bliss MR, Yamamoto F, Bobkov AA, Kiselar J, Liu Y, Cadwell GW, Khare S, Yu J, Barquilla A, Chung TDY, Mustelin T, Schenk S, Bankston LA, Liddington RC, Pinkerton AB, Bottini N
Nat Chem Biol 13 624-632 (2017)
PMID: 28346406

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-145642 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Low molecular weight phosphotyrosine protein phosphatase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.08 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:
Ligand EPE 1 x EPE
Ligand DMS 3 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 59.944Å b: 122.939Å c: 44.888Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.154 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Targeting Tyrosine Phosphatases: Time to End the Stigma.
Stanford et al. (2017)
10 more

2 mentions without citation

Diabetes reversal by inhibition of the low-molecular-weight tyrosine phosphatase.
Stanford et al. (2017)
1 more