› 6d28

X-ray diffraction
1.75Å resolution

Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with the specific ligand NECA

Released:
DOI: 10.2210/pdb6d28/pdb
PDB entry 6d28 coloured by chain, front view.
PDB entry 6d28 coloured by chain, side view.
PDB entry 6d28 coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.
Soldano KL, Jivan A, Nicchitta CV, Gewirth DT
J Biol Chem 278 48330-8 (2003)
PMID: 12970348

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154244 (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, HSPC4, TRA1
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

2 bound ligands:
Ligand NEC 1 x NEC
Ligand M2M 1 x M2M
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2221
Unit cell:
a: 89.2Å b: 99.18Å c: 63.071Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

30 review citations

Structure and mechanism of the Hsp90 molecular chaperone machinery.
Pearl et al. (2006)
29 more

2 mentions without citation

Expanding the repertoire of methanocarba nucleosides from purinergic signaling to diverse targets.
Jacobson et al. (2021)
1 more