Research workbench
Structure of anti-huntingtin vl domain in complex with huntingtin peptide
Analyse Structure of anti-huntingtin vl domain in complex with huntingtin peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LRH
- Type
- protein
- Length
- 991 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-huntingtin vl domain; Huntingtin
- UniProt
- P42858
- Pockets
- 15 · best druggability 0.81
Structure
x-ray diffraction · 5 distinct chains · 5% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, G, K | Anti-huntingtin vl domain | protein | 109 | 3% helix, 49% strand | — |
| B, D, F, H, J, L, N, P | Huntingtin | protein | 14 | 86% helix, 0% strand | P42858 |
| E | Anti-huntingtin vl domain | protein | 112 | 3% helix, 49% strand | — |
| I, M | Anti-huntingtin vl domain | protein | 110 | 3% helix, 50% strand | — |
| O | Anti-huntingtin vl domain | protein | 111 | 3% helix, 49% strand | — |
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 847 | 0.81 | 0.84 | 99 | empty |
| 2 | 497 | 0.68 | 0.79 | 60 | empty |
| 3 | 51 | 0.60 | 0.92 | 24 | empty |
| 4 | 201 | 0.55 | 0.79 | 34 | empty |
| 5 | 103 | 0.53 | 0.83 | 26 | empty |
Interfaces
31 interfaces between chains.
- I–O · 683 Ų buried · 14 hydrogen bonds · protein-protein
- M–O · 664 Ų buried · 6 hydrogen bonds · protein-protein
- C–E · 646 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 631 Ų buried · 2 hydrogen bonds · protein-protein
- M–N · 618 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3LRH · Structure of anti-huntingtin VL domain in complex with huntingtin peptide · 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 3LRH · PDBe 3LRH · UniProt P42858
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