› 3vhd

X-ray diffraction
1.52Å resolution

Hsp90 alpha N-terminal domain in complex with a macrocyclic inhibitor, CH5164840

Released:
DOI: 10.2210/pdb3vhd/pdb
PDB entry 3vhd coloured by chain, front view.
PDB entry 3vhd coloured by chain, side view.
PDB entry 3vhd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and synthesis of novel macrocyclic 2-amino-6-arylpyrimidine Hsp90 inhibitors.
Suda A, Koyano H, Hayase T, Hada K, Kawasaki K, Komiyama S, Hasegawa K, Fukami TA, Sato S, Miura T, Ono N, Yamazaki T, Saitoh R, Shimma N, Shiratori Y, Tsukuda T
Bioorg Med Chem Lett 22 1136-41 (2012)
PMID: 22192591

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 229 amino acids
Theoretical weight: 25.79 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

1 bound ligand:
Ligand VHE 2 x VHE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P1
Unit cell:
a: 40.995Å b: 53.061Å c: 54.178Å
α: 114.6° β: 91.12° γ: 90.17°
R-values:
R R work R free
0.166 0.164 0.196
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Targeting protein-protein interactions as an anticancer strategy.
Ivanov et al. (2013)
4 more

1 mention without citation

Machine learning accelerates MD-based binding pose prediction between ligands and proteins.
Terayama et al. (2018)