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
- 1USU
- Type
- protein
- Length
- 378 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein HSP82; AHA1
- UniProt
- P02829, Q12449
- Pockets
- 9 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein HSP82 | protein | 246 | 39% helix, 23% strand | P02829 |
| B | AHA1 | protein | 132 | 33% helix, 31% strand | Q12449 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.57 | 0.80 | 23 | empty |
| 2 | 140 | 0.42 | 0.75 | 19 | empty |
| 3 | 76 | 0.40 | 0.79 | 15 | empty |
| 4 | 113 | 0.37 | 0.74 | 22 | empty |
| 5 | 101 | 0.36 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 794 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 1USU · The Structure of the complex between Aha1 and HSP90 · the same entry in another collection · chain A against A, TM-score 1.00
- Q12449 · AlphaFold monomer V2.0 prediction for HSP90 co-chaperone AHA1 (Q12449) · a predicted model of the same protein · chain B against A, TM-score 0.98
- 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 0.96
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 1USU · PDBe 1USU · UniProt P02829 · UniProt Q12449
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