MolNFT v1 · #54697 · protein

Macrolactone inhibitor bound to HSP90 N-term

2XX2 · ATP-dependent molecular chaperone HSP82: “Macrolactone inhibitor bound to HSP90 N-term”. X-ray diffraction, 1 ligand (13C), 6 pockets (best druggability 0.77). MolNFT v1 #54697 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 2XX2
Type: protein
Length: 856 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent molecular chaperone HSP82
UniProt: P02829
Ligands: 13C
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	ATP-dependent molecular chaperone HSP82	protein	214	42% helix, 24% strand	P02829

Ligands and binding sites

13C · (5E)-13-chloro-14,16-dihydroxy-3,4,7,8,9,10-hexahydro-2-benzazacyclotetradecine-1,11(2H,12H)-dione · ligand · 4 copies · chains A, B, C, D
GOL · Glycerol · additive · 4 copies · chains A, B, D, C

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

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1158	0.77	0.79	114	13C, GOL
2	537	0.72	0.81	70	GOL
3	559	0.72	0.80	58	GOL
4	244	0.61	0.80	27	13C
5	256	0.61	0.80	24	13C

Interfaces

3 interfaces between chains.

B–C · 1196 Å² buried · 29 hydrogen bonds · protein-protein
A–D · 1101 Å² buried · 24 hydrogen bonds · protein-protein
A–B · 587 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2XX2 · 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 0.81

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 2XX2 · PDBe 2XX2 · UniProt P02829

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