Research workbench

Crystal structure of HSP90 with fragment 42-C03

Analyse Crystal structure of HSP90 with fragment 42-C03 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HYZ
Type: protein
Length: 413 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: 42C
Pockets: 5 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein HSP 90-alpha	protein	204	42% helix, 23% strand	P07900
B	Heat shock protein HSP 90-alpha	protein	209	42% helix, 23% strand	P07900

Ligands and binding sites

42C · N,N-dimethyl-7H-purin-6-amine · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	320	0.65	0.80	33	42C
2	220	0.64	0.82	23	42C
3	302	0.54	0.76	36	empty
4	72	0.31	0.74	18	empty
5	78	0.31	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 377 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3HYZ · Crystal structure of Hsp90 with fragment 42-C03 · the same entry in another collection · chain B against B, 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 3HYZ · PDBe 3HYZ · UniProt P07900

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