› 3o2f

X-ray diffraction
2Å resolution

Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54

Released:
DOI: 10.2210/pdb3o2f/pdb
PDB entry 3o2f coloured by chain, front view.
PDB entry 3o2f coloured by chain, side view.
PDB entry 3o2f coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2.
Patel PD, Yan P, Seidler PM, Patel HJ, Sun W, Yang C, Que NS, Taldone T, Finotti P, Stephani RA, Gewirth DT, Chiosis G
Nat Chem Biol 9 677-84 (2013)
PMID: 23995768

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154246 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmin Chains: A, B
Molecule details ›
Chains: A, B
Length: 236 amino acids
Theoretical weight: 26.51 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41148 (Residues: 69-286, 328-337; Coverage: 29%)
Gene names: GRP94, HSP90B1, HSPC4, TRA1
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

3 bound ligands:
Ligand P54 2 x P54
Ligand IPA 4 x IPA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 60.96Å b: 65.686Å c: 85.453Å
α: 90° β: 98.13° γ: 90°
R-values:
R R work R free
0.236 0.234 0.269
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

36 review citations

Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential.
Lee AS. (2014)
35 more

12 mentions without citation

Selective targeting of the stress chaperome as a therapeutic strategy.
Taldone et al. (2014)
11 more