› 1y4s

X-ray diffraction
2.9Å resolution

Conformation rearrangement of heat shock protein 90 upon ADP binding

Released:
DOI: 10.2210/pdb1y4s/pdb
PDB entry 1y4s coloured by chain, front view.
PDB entry 1y4s coloured by chain, side view.
PDB entry 1y4s coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding.
Huai Q, Wang H, Liu Y, Kim HY, Toft D, Ke H
Structure 13 579-90 (2005)
PMID: 15837196

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141496 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein HtpG Chains: A, B
Molecule details ›
Chains: A, B
Length: 559 amino acids
Theoretical weight: 63.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A6Z3 (Residues: 1-559; Coverage: 90%)
Gene names: JW0462, b0473, htpG
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21212
Unit cell:
a: 72.5Å b: 84.18Å c: 212.886Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.269 0.269 0.314
Expression system: Escherichia coli BL21

Quick links

Citations

17 review citations

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

2 mentions without citation

A History of Molecular Chaperone Structures in the Protein Data Bank.
Bascos et al. (2019)
1 more