Research workbench
High resolution cryoem structure of huntingtin in complex with HAP40
Analyse High resolution cryoem structure of huntingtin in complex with HAP40 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X9O
- Type
- protein
- Length
- 2,669 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Huntingtin; 40-kda huntingtin-associated protein
- UniProt
- P42858, P23610
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Huntingtin | protein | 2425 | 65% helix, 0% strand | P42858 |
| B | 40-kda huntingtin-associated protein | protein | 244 | 74% helix, 0% strand | P23610 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 524 | 0.87 | 0.93 | 93 | empty |
| 2 | 381 | 0.83 | 0.92 | 67 | empty |
| 3 | 695 | 0.79 | 0.83 | 57 | empty |
| 4 | 299 | 0.78 | 0.90 | 43 | empty |
| 5 | 889 | 0.77 | 0.80 | 79 | empty |
Interfaces
1 interface between chains.
- A–B · 4921 Ų buried · 40 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6X9O · High resolution cryoEM structure of huntingtin in complex with HAP40 · the same entry in another collection · chain A against A, TM-score 1.00
- P23610 · AlphaFold monomer V2.0 prediction for 40-kda huntingtin-associated protein (P23610) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P42858
- Every structure of UniProt P23610
- Elsewhere: RCSB PDB 6X9O · PDBe 6X9O · UniProt P42858 · UniProt P23610
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