› 1qye

X-ray diffraction
2.1Å resolution

Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine

Released:
DOI: 10.2210/pdb1qye/pdb
PDB entry 1qye coloured by chain, front view.
PDB entry 1qye coloured by chain, side view.
PDB entry 1qye coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.
Soldano KL, Jivan A, Nicchitta CV, Gewirth DT
J Biol Chem 278 48330-8 (2003)
PMID: 12970348

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmin Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 30.64 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41148 (Residues: 69-337; Coverage: 34%)
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

2 bound ligands:
Ligand CDY 1 x CDY
Ligand M2M 1 x M2M
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: C2221
Unit cell:
a: 87.008Å b: 98.974Å c: 63.254Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.272
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

31 review citations

Structure and mechanism of the Hsp90 molecular chaperone machinery.
Pearl et al. (2006)
30 more

2 mentions without citation

Analysis of HSP90-related folds with MED-SuMo classification approach.
Doppelt-Azeroual et al. (2009)
1 more