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Identification of novel HSP90/ISOFORM selective inhibitors using structure-based drug design. demonstration of potential utility in treating cns disorders such as HUNTINGTON'S disease

Analyse Identification of novel HSP90/ISOFORM selective inhibitors using… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4O05
Type: protein
Length: 209 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock protein HSP 90-alpha
UniProt: P07900
Ligands: 2Q9
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein HSP 90-alpha	protein	209	44% helix, 23% strand	P07900

Ligands and binding sites

2Q9 · 2,7,7-trimethyl-9-[1-oxo-8-(propan-2-ylamino)-1,2,3,4-tetrahydroisoquinolin-6-yl]-1,2,3,4,6,7,8,9-octahydro-5H-beta-carbolin-5-one · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	326	0.71	0.84	41	2Q9

Compared structures

4O05 · Identification of novel HSP90/isoform selective inhibitors using structure-based drug… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P07900
Elsewhere: RCSB PDB 4O05 · PDBe 4O05 · UniProt P07900

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