Research workbench
Hsp90-beta bound to PU-11-trans
Analyse Hsp90-beta bound to PU-11-trans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N8Y
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.55391
- Source
- Homo sapiens
- Molecule
- Heat shock protein HSP 90-beta
- UniProt
- P08238
- Ligands
- KFY
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · resolution 1.55391 · 1 distinct chain · 45% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein HSP 90-beta | protein | 210 | 45% helix, 22% strand | P08238 |
Ligands and binding sites
- KFY · 9-[(2E)-but-2-en-1-yl]-8-[(3,4,5-trimethoxyphenyl) methyl]-9H-purin-6-amine · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.71 | 0.83 | 43 | KFY |
Compared structures
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 P08238
- Elsewhere: RCSB PDB 6N8Y · PDBe 6N8Y · UniProt P08238
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