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

X-ray diffraction
3.25Å resolution
PDB entry 1yt2 coloured by chain, front view.
PDB entry 1yt2 coloured by chain, side view.
PDB entry 1yt2 coloured by chain, top view.
Source organism: Canis lupus familiaris
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Endoplasmin
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Multimeric state: monomeric
Accessible surface area: 11203.05 Å2
Buried surface area: 1327.72 Å2
Dissociation area: 177.34 Å2
Dissociation energy (ΔGdiss): -4.69 kcal/mol
Dissociation entropy (TΔSdiss): 1.37 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-154244

Macromolecules

Endoplasmin
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, HSPC4, TRA1
Pfam: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
InterPro:
CATH: Histidine kinase-like ATPase, C-terminal domain
SCOP: Heat shock protein 90, HSP90, N-terminal domain
Endoplasmin in PDB entry 1yt2, assembly 1, front view.
Endoplasmin in PDB entry 1yt2, assembly 1, side view.
Endoplasmin in PDB entry 1yt2, assembly 1, top view.
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