Research workbench

Macrolactone inhibitor bound to HSP90 N-term

Analyse Macrolactone inhibitor bound to HSP90 N-term in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XX5
Type: protein
Length: 211 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent molecular chaperone HSP82
UniProt: P02829
Ligands: 13N
Pockets: 1 · best druggability 0.64

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	211	42% helix, 22% strand	P02829

Ligands and binding sites

13N · (5E,10R)-N-benzyl-13-chloro-14,16-dihydroxy-1,11-dioxo-1,2,3,4,7,8,9,10,11,12-decahydro-2-benzazacyclotetradecine-10-carboxamide · ligand · chains A
GOL · Glycerol · additive · 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	299	0.64	0.80	28	13N

Compared structures

2XX5 · Macrolactone Inhibitor bound to HSP90 N-term · 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 0.82

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 2XX5 · PDBe 2XX5 · UniProt P02829

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.