› 6pfw

X-ray diffraction
2.34Å resolution

Protein Tyrosine Phosphatase 1B (1-301), T177A mutant, apo state

Released:
DOI: 10.2210/pdb6pfw/pdb
Model geometry
Fit model/data
PDB entry 6pfw coloured by chain, front view.
PDB entry 6pfw coloured by chain, side view.
PDB entry 6pfw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Uncovering the Molecular Interactions in the Catalytic Loop That Modulate the Conformational Dynamics in Protein Tyrosine Phosphatase 1B.
Cui DS, Lipchock JM, Brookner D, Loria JP
J Am Chem Soc 141 12634-12647 (2019)
PMID: 31339043

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 1 Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 34.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18031 (Residues: 2-298; Coverage: 68%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase

Ligands and Environments

2 bound ligands:
Ligand GOL 2 x GOL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P3121
Unit cell:
a: 87.929Å b: 87.929Å c: 102.924Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.209 0.247
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Interaction of Vanadium Complexes with Proteins: Revisiting the Reported Structures in the Protein Data Bank (PDB) since 2015.
Santos et al. (2023)
1 more

1 mention without citation

Native dynamics and allosteric responses in PTP1B probed by high-resolution HDX-MS.
Woods et al. (2023)