MolNFT v1 · #499066 · protein
AlphaFold monomer V2.0 prediction for actin-interacting protein 1 (Q11176)
Q11176: “AlphaFold monomer V2.0 prediction for actin-interacting protein 1 (Q11176)”. 8 pockets (best druggability 0.78). MolNFT v1 #499066 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q11176
- Type
- protein
- Length
- 611 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA55fA446aDFd185F1deb3281162E4D0d9a8056F7
- Molecule
- Actin-interacting protein 1
- UniProt
- Q11176
- Pockets
- 8 · best druggability 0.78
Structure
1 distinct chain · 1% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin-interacting protein 1 | protein | 611 | 1% helix, 51% strand | Q11176 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.78 | 0.86 | 44 | empty |
| 2 | 797 | 0.77 | 0.81 | 64 | empty |
| 3 | 149 | 0.57 | 0.82 | 22 | empty |
| 4 | 104 | 0.37 | 0.74 | 21 | empty |
| 5 | 66 | 0.36 | 0.77 | 16 | empty |
Compared structures
- 1NR0 · Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 1NR0 · Two seven-bladed beta-propeller domains revealed by the structure of a C. elegans… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 1PEV · Crystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 1PEV · Crystal structure of the actin interacting protein from caenorhabditis elegans · an experimental structure of the same protein · chain A against A, TM-score 0.99
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 Q11176
- Elsewhere: UniProt Q11176 · AlphaFold DB Q11176
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