› 7f8g

X-ray diffraction
3.49Å resolution

Structure-activity relationship studies of allosteric inhibitors of EYA2 tyrosine phosphatase

Released:
DOI: 10.2210/pdb7f8g/pdb
PDB entry 7f8g coloured by chain, front view.
PDB entry 7f8g coloured by chain, side view.
PDB entry 7f8g coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-activity relationship studies of allosteric inhibitors of EYA2 tyrosine phosphatase.
Anantharajan J, Baburajendran N, Lin G, Loh YY, Xu W, Ahmad NHB, Liu S, Jansson AE, Kuan JWL, Ng EY, Yeo YK, Hung AW, Joy J, Hill J, Ford HL, Zhao R, Keller TH, Kang C
Protein Sci 31 422-431 (2022)
PMID: 34761455

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-126128 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Eyes absent homolog 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 33.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00167 (Residues: 253-538; Coverage: 53%)
Gene names: EAB1, EYA2
Sequence domains: haloacid dehalogenase-like hydrolase

Ligands and Environments

1 bound ligand:
Ligand 1RI 2 x 1RI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P31
Unit cell:
a: 89.92Å b: 89.92Å c: 96.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.214 0.267
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Glycolytic flux control by drugging phosphoglycolate phosphatase.
Jeanclos et al. (2022)
1 more

1 mention without citation

Structure-activity relationship studies of allosteric inhibitors of EYA2 tyrosine phosphatase.
Anantharajan et al. (2022)