PDBe 4nh9

X-ray diffraction
2.77Å resolution

Correlation between chemotype-dependent binding conformations of HSP90 alpha/beta and isoform selectivity

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmin Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 31.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14625 (Residues: 69-337; Coverage: 34%)
Gene names: GRP94, HSP90B1, TRA1
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2221
Unit cell:
a: 91.102Å b: 101.194Å c: 63.497Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.245 0.277
Expression system: Escherichia coli