› 2akp

X-ray diffraction
1.94Å resolution

Hsp90 Delta24-N210 mutant

Released:
DOI: 10.2210/pdb2akp/pdb
PDB entry 2akp coloured by chain, front view.
PDB entry 2akp coloured by chain, side view.
PDB entry 2akp coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Intrinsic inhibition of the Hsp90 ATPase activity.
Richter K, Moser S, Hagn F, Friedrich R, Hainzl O, Heller M, Schlee S, Kessler H, Reinstein J, Buchner J
J Biol Chem 281 11301-11 (2006)
PMID: 16461354

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-136252 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent molecular chaperone HSP82 Chains: A, B
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 20.96 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 25-210; Coverage: 26%)
Gene names: HSP82, HSP90, YPL240C
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 90.5Å b: 52.95Å c: 84.24Å
α: 90° β: 122.05° γ: 90°
R-values:
R R work R free
0.231 0.231 0.269
Expression system: Escherichia coli

Quick links

Citations

5 review citations

GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.
Marzec et al. (2012)
4 more