› 5ggz

X-ray diffraction
2.02Å resolution

Crystal structure of novel inhibitor bound with Hsp90

Released:
DOI: 10.2210/pdb5ggz/pdb
PDB entry 5ggz coloured by chain, front view.
PDB entry 5ggz coloured by chain, side view.
PDB entry 5ggz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel Tetrahydropyrido[4,3-d]pyrimidines as Potent Inhibitors of Chaperone Heat Shock Protein 90.
Jiang F, Wang HJ, Jin YH, Zhang Q, Wang ZH, Jia JM, Liu F, Wang L, Bao QC, Li DD, You QD, Xu XL
J Med Chem 59 10498-10519 (2016)
PMID: 27933959

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139824 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 210 amino acids
Theoretical weight: 23.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07900 (Residues: 16-225; Coverage: 29%)
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

1 bound ligand:
Ligand 6TN 4 x 6TN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 66.841Å b: 88.581Å c: 99.382Å
α: 90° β: 90.08° γ: 90°
R-values:
R R work R free
0.209 0.208 0.265
Expression system: Escherichia coli

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Citations

2 review citations

Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery.
Wang et al. (2020)
1 more