› 1byq

X-ray diffraction
1.5Å resolution

HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG

Released:
DOI: 10.2210/pdb1byq/pdb
PDB entry 1byq coloured by chain, front view.
PDB entry 1byq coloured by chain, side view.
PDB entry 1byq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.
Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU
J Cell Biol 143 901-10 (1998)
PMID: 9817749

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chain: A
Molecule details ›
Chain: A
Length: 228 amino acids
Theoretical weight: 25.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07900 (Residues: 9-236; Coverage: 31%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA
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 MG 1 x MG
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21
Unit cell:
a: 53.14Å b: 42.5Å c: 53.96Å
α: 90° β: 115.53° γ: 90°
R-values:
R R work R free
0.189 0.189 0.247
Expression system: Escherichia coli

Quick links

Citations

63 review citations

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.
Pratt et al. (2003)
62 more

31 mentions without citation

Proposal of Dual Inhibitor Targeting ATPase Domains of Topoisomerase II and Heat Shock Protein 90.
Jun et al. (2016)
30 more