› 6h8r

X-ray diffraction
1.66Å resolution

CRYSTAL STRUCTURE OF THE HUMAN PROTEIN TYROSINE PHOSPHATASE PTPN5 (STEP) IN COMPLEX WITH COMPOUND 2

Released:
DOI: 10.2210/pdb6h8r/pdb
PDB entry 6h8r coloured by chain, front view.
PDB entry 6h8r coloured by chain, side view.
PDB entry 6h8r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Allosteric Activation of Striatal-Enriched Protein Tyrosine Phosphatase (STEP, PTPN5) by a Fragment-like Molecule.
Tautermann CS, Binder F, Büttner FH, Eickmeier C, Fiegen D, Gross U, Grundl MA, Heilker R, Hobson S, Hoerer S, Luippold A, Mack V, Montel F, Peters S, Bhattacharya S, Vaidehi N, Schnapp G, Thamm S, Zeeb M
J Med Chem 62 306-316 (2019)
PMID: 30207464

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-157113 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 5 Chain: A
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 35.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54829 (Residues: 282-563; Coverage: 50%)
Gene name: PTPN5
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand FWB 1 x FWB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 53.095Å b: 64.375Å c: 100.804Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.2 0.239
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins.
Bhattacharya et al. (2019)
6 more

3 mentions without citation

ProxyBind: A compendium of binding sites for proximity-induced pharmacology.
Rovers et al. (2022)
2 more