› 6y2v

X-ray diffraction
2Å resolution

Crystal structure of the double mutant L13R I16K of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP)

Released:
DOI: 10.2210/pdb6y2v/pdb
Model geometry
Fit model/data
PDB entry 6y2v coloured by chain, front view.
PDB entry 6y2v coloured by chain, side view.
PDB entry 6y2v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Computational and structure-guided design of phosphoinositide substrate specificity into the tyrosine specific LMW-PTP enzyme.
Egbe E, Levy CW, Tabernero L
OpenAccess logo PLoS One 15 e0235133 (2020)
PMID: 32584877

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: 158 amino acids
Theoretical weight: 18.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P24666 (Residues: 1-158; Coverage: 100%)
  • Best match: P24666-2 (Residues: 1-158)
Gene name: ACP1
Sequence domains: Low molecular weight phosphotyrosine protein phosphatase

Ligands and Environments

2 bound ligands:
Ligand PGE 1 x PGE
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 56.625Å b: 41.287Å c: 56.898Å
α: 90° β: 91.809° γ: 90°
R-values:
R R work R free
0.185 0.183 0.231
Expression system: Escherichia coli BL21(DE3)

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