› 4nh9

X-ray diffraction
2.77Å resolution

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

Released:
DOI: 10.2210/pdb4nh9/pdb
PDB entry 4nh9 coloured by chain, front view.
PDB entry 4nh9 coloured by chain, side view.
PDB entry 4nh9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Correlation between chemotype-dependent binding conformations of HSP90α/β and isoform selectivity-Implications for the structure-based design of HSP90α/β selective inhibitors for treating neurodegenerative diseases.
Ernst JT, Liu M, Zuccola H, Neubert T, Beaumont K, Turnbull A, Kallel A, Vought B, Stamos D
Bioorg Med Chem Lett 24 204-8 (2014)
PMID: 24332488

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146986 (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, HSPC4, 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:
Ligand 2LC 1 x 2LC
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

Quick links

Citations

6 review citations

Old and New Approaches to Target the Hsp90 Chaperone.
Sanchez et al. (2020)
5 more

3 mentions without citation

Paralog Specific Hsp90 Inhibitors - A Brief History and a Bright Future.
Gewirth DT. (2016)
2 more