PDBe 1tc0

X-ray diffraction
2.2Å resolution

Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo 12-mer
homo tetramer
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: 69-337; Coverage: 30%)
Gene names: GRP94, HSP90B1, 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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: R32
Unit cell:
a: 159.013Å b: 159.013Å c: 109.472Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.226 0.267
Expression system: Escherichia coli BL21(DE3)