PDBe 1yt2

X-ray diffraction
3.25Å resolution

Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N APO CRYSTAL

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmin Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 31.06 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41148 (Residues: 69-337; Coverage: 34%)
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 90.321Å b: 100.257Å c: 64.013Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.252 0.293
Expression system: Escherichia coli BL21(DE3)