1uyl

X-ray diffraction
1.4Å resolution

Structure-Activity Relationships in purine-based inhibitor binding to HSP90 isoforms

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 236 amino acids
Theoretical weight: 26.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07900 (Residues: 1-236; Coverage: 32%)
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I222
Unit cell:
a: 65.127Å b: 88.769Å c: 99.944Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.227
Expression system: Escherichia coli BL21(DE3)