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Structure of HSP90 with small molecule inhibitor bound

Analyse Structure of HSP90 with small molecule inhibitor bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XJJ
Type: protein
Length: 414 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock protein HSP 90-alpha
UniProt: P07900
Ligands: L81
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Heat shock protein HSP 90-alpha	protein	207	43% helix, 23% strand	P07900

Ligands and binding sites

L81 · 1,3-dihydroisoindol-2-yl-(6-hydroxy-3,3-dimethyl-1,2-dihydroindol-5-yl)methanone · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	246	0.61	0.81	27	GOL, L81
2	261	0.61	0.80	27	GOL, L81
3	54	0.25	0.72	13	empty

Interfaces

1 interface between chains.

A–B · 268 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2XJJ · Structure of HSP90 with small molecule inhibitor bound · 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 2XJJ · PDBe 2XJJ · UniProt P07900

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