› 2o1t

X-ray diffraction
3.2Å resolution

Structure of Middle plus C-terminal domains (M+C) of GRP94

Released:
DOI: 10.2210/pdb2o1t/pdb
PDB entry 2o1t coloured by chain, front view.
PDB entry 2o1t coloured by chain, side view.
PDB entry 2o1t coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.
Dollins DE, Warren JJ, Immormino RM, Gewirth DT
Mol Cell 28 41-56 (2007)
PMID: 17936703

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, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 450 amino acids
Theoretical weight: 52.48 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41148 (Residues: 336-765; Coverage: 55%)
Gene names: GRP94, HSP90B1, HSPC4, TRA1
Sequence domains: Hsp90 protein
Structure domains: Ribosomal Protein S5; domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 131.3Å b: 129.54Å c: 184.78Å
α: 90° β: 99.91° γ: 90°
R-values:
R R work R free
0.285 0.284 0.294
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

45 review citations

HSP90 at the hub of protein homeostasis: emerging mechanistic insights.
Taipale et al. (2010)
44 more

4 mentions without citation

Corresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulations.
Morra et al. (2012)
3 more