› 5wmt

X-ray diffraction
2.75Å resolution

Structure of GRP94 N-terminal Domain bound to resorcinylic inhibitor BnIm.

Released:
DOI: 10.2210/pdb5wmt/pdb
PDB entry 5wmt coloured by chain, front view.
PDB entry 5wmt coloured by chain, side view.
PDB entry 5wmt coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding.
Que NLS, Crowley VM, Duerfeldt AS, Zhao J, Kent CN, Blagg BSJ, Gewirth DT
J Med Chem 61 2793-2805 (2018)
PMID: 29528635

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-154244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 236 amino acids
Theoretical weight: 26.51 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli
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 EDO 15 x EDO
Ligand 9QY 4 x 9QY
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 94.412Å b: 94.73Å c: 179.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.236
Expression system: Escherichia coli

Quick links

Citations

3 review citations

A Chemical Biology Approach to the Chaperome in Cancer-HSP90 and Beyond.
Taldone et al. (2020)
2 more

2 mentions without citation

Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding.
Que et al. (2018)
1 more