Research workbench
HSP90 complexed with A56322
Analyse HSP90 complexed with A56322 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QF6
- Type
- protein
- Length
- 828 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein HSP 90-alpha
- UniProt
- P07900
- Ligands
- A56
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Heat shock protein HSP 90-alpha | protein | 207 | 43% helix, 23% strand | P07900 |
Ligands and binding sites
- A56 · 6-(3-bromo-2-naphthyl)-1,3,5-triazine-2,4-diamine · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.66 | 0.83 | 29 | A56 |
| 2 | 217 | 0.64 | 0.83 | 25 | A56 |
| 3 | 216 | 0.64 | 0.83 | 22 | A56 |
| 4 | 234 | 0.64 | 0.82 | 24 | A56 |
Interfaces
1 interface between chains.
- A–C · 78 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2QF6 · HSP90 complexed with A56322 · 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 2QF6 · PDBe 2QF6 · UniProt P07900
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