Research workbench
Cryo-EM structure of the full-length disease type human huntingtin
Analyse Cryo-EM structure of the full-length disease type human huntingtin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YEJ
- Type
- protein
- Length
- 2,046 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Huntingtin
- UniProt
- P42858
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 47% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Huntingtin | protein | 2046 | 47% helix, 0% strand | P42858 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1156 | 0.80 | 0.81 | 113 | empty |
| 2 | 983 | 0.79 | 0.80 | 87 | empty |
| 3 | 135 | 0.78 | 0.96 | 43 | empty |
| 4 | 112 | 0.76 | 0.95 | 24 | empty |
| 5 | 856 | 0.76 | 0.79 | 63 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6YEJ · Cryo-EM structure of the Full-length disease type human Huntingtin · 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 P42858
- Elsewhere: RCSB PDB 6YEJ · PDBe 6YEJ · UniProt P42858
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