› 2o1u

X-ray diffraction
2.4Å resolution

Structure of full length GRP94 with AMP-PNP bound

Released:
DOI: 10.2210/pdb2o1u/pdb
PDB entry 2o1u coloured by chain, front view.
PDB entry 2o1u coloured by chain, side view.
PDB entry 2o1u 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
Molecule details ›
Chains: A, B
Length: 666 amino acids
Theoretical weight: 76.6 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41148 (Residues: 73-754; Coverage: 82%)
Gene names: GRP94, HSP90B1, HSPC4, TRA1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 5 x MG
Ligand ANP 2 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 99.33Å b: 109.26Å c: 148.887Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.243 0.289
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

41 review citations

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

26 mentions without citation

ATP-driven molecular chaperone machines.
Clare et al. (2013)
25 more