Research workbench
AlphaFold monomer V2.0 prediction for RAS-related protein rab-9A (P24408)
Analyse AlphaFold monomer V2.0 prediction for RAS-related protein rab-9A (P24408) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P24408
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- RAS-related protein rab-9A
- UniProt
- P24408
- Pockets
- 2 · best druggability 0.48
Structure
1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related protein rab-9A | protein | 201 | 36% helix, 22% strand | P24408 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.48 | 0.80 | 28 | empty |
| 2 | 89 | 0.35 | 0.75 | 19 | empty |
Compared structures
- 1S8F · Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of… · an experimental structure of the same protein · chain A against A, TM-score 0.80
- 1S8F · Crystal structure of RAB9 complexed to GDP reveals a dimer with an active conformation of… · an experimental structure of the same protein · chain A against A, TM-score 0.80
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 P24408
- Elsewhere: UniProt P24408 · AlphaFold DB P24408
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