Research workbench
AlphaFold monomer V2.0 prediction for unconventional myosin-ixb (Q13459)
Analyse AlphaFold monomer V2.0 prediction for unconventional myosin-ixb (Q13459) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q13459
- Type
- protein
- Length
- 2,157 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Unconventional myosin-ixb
- UniProt
- Q13459
- Pockets
- 18 · best druggability 0.82
Structure
1 distinct chain · 39% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Unconventional myosin-ixb | protein | 2157 | 39% helix, 8% strand | Q13459 |
Pockets
18 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1023 | 0.82 | 0.83 | 107 | empty |
| 2 | 532 | 0.71 | 0.80 | 67 | empty |
| 3 | 795 | 0.71 | 0.77 | 61 | empty |
| 4 | 1175 | 0.69 | 0.74 | 74 | empty |
| 5 | 402 | 0.64 | 0.78 | 53 | empty |
Compared structures
- 5C5S · Crystal Structure of human Myosin 9b RhoGAP domain at 2.2 angstrom · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 5C5S · Crystal structure of human myosin 9B rhogap domain at 2.2 ångström · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 5HPY · Crystal structure of RHOA.GDP.MGF3-in complex with human myosin 9B rhogap domain · an experimental structure of the same protein · chain A against A, TM-score 0.09
- 5HPY · Crystal Structure of RhoA.GDP.MgF3-in complex with human Myosin 9b RhoGAP domain · an experimental structure of the same protein · chain A against A, TM-score 0.09
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 Q13459
- Elsewhere: UniProt Q13459 · AlphaFold DB Q13459
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