Research workbench

Yeast HSP82 in complex with the novel HSP90 inhibitor radester amine

Analyse Yeast HSP82 in complex with the novel HSP90 inhibitor radester amine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZWH
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent molecular chaperone HSP82
UniProt: P02829
Ligands: RDE
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent molecular chaperone HSP82	protein	213	42% helix, 22% strand	P02829

Ligands and binding sites

RDE · 2-(3-amino-2,5,6-trimethoxyphenyl)ethyl 5-chloro-2,4-dihydroxybenzoate · 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	222	0.57	0.79	24	RDE

Compared structures

1ZWH · Yeast Hsp82 in complex with the novel Hsp90 inhibitor Radester amine · the same entry in another collection · chain A against A, TM-score 1.00
P02829 · AlphaFold monomer V2.0 prediction for ATP-dependent molecular chaperone HSP82 (P02829) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 P02829
Elsewhere: RCSB PDB 1ZWH · PDBe 1ZWH · UniProt P02829

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