Research workbench
The structure of the complex between AHA1 and HSP90
Analyse The structure of the complex between AHA1 and HSP90 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1USV
- Type
- protein
- Length
- 1,568 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein HSP82; AHA1
- UniProt
- P02829, Q12449
- Pockets
- 20 · best druggability 0.69
Structure
x-ray diffraction · 8 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein HSP82 | protein | 251 | 37% helix, 22% strand | P02829 |
| B | AHA1 | protein | 143 | 27% helix, 36% strand | Q12449 |
| C | Heat shock protein HSP82 | protein | 247 | 38% helix, 22% strand | P02829 |
| D | AHA1 | protein | 142 | 26% helix, 36% strand | Q12449 |
| E | Heat shock protein HSP82 | protein | 251 | 36% helix, 20% strand | P02829 |
| F | AHA1 | protein | 145 | 26% helix, 33% strand | Q12449 |
| G | Heat shock protein HSP82 | protein | 248 | 38% helix, 23% strand | P02829 |
| H | AHA1 | protein | 141 | 32% helix, 38% strand | Q12449 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 779 | 0.69 | 0.76 | 81 | empty |
| 2 | 357 | 0.64 | 0.79 | 47 | empty |
| 3 | 355 | 0.62 | 0.78 | 50 | empty |
| 4 | 203 | 0.56 | 0.79 | 29 | empty |
| 5 | 358 | 0.54 | 0.73 | 39 | empty |
Interfaces
10 interfaces between chains.
- C–D · 844 Ų buried · 12 hydrogen bonds · protein-protein
- G–H · 824 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 791 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 789 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 322 Ų buried · 3 hydrogen bonds · protein-protein
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 P02829
- Every structure of UniProt Q12449
- Elsewhere: RCSB PDB 1USV · PDBe 1USV · UniProt P02829 · UniProt Q12449
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