Research workbench
AlphaFold monomer V2.0 prediction for trafficking protein particle complex subunit 11 (Q5ZI89)
Analyse AlphaFold monomer V2.0 prediction for trafficking protein particle complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5ZI89
- Type
- protein
- Length
- 1,132 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Trafficking protein particle complex subunit 11
- UniProt
- Q5ZI89
- Pockets
- 14 · best druggability 0.71
Structure
1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trafficking protein particle complex subunit 11 | protein | 1132 | 34% helix, 28% strand | Q5ZI89 |
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 448 | 0.71 | 0.82 | 31 | empty |
| 2 | 538 | 0.70 | 0.79 | 56 | empty |
| 3 | 61 | 0.58 | 0.90 | 20 | empty |
| 4 | 61 | 0.53 | 0.88 | 18 | empty |
| 5 | 66 | 0.51 | 0.86 | 17 | empty |
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 Q5ZI89
- Elsewhere: UniProt Q5ZI89 · AlphaFold DB Q5ZI89
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