MolNFT v1 · #423579 · protein
AlphaFold monomer V2.0 prediction for protein translocase subunit seca 2 (Q183M9)
Q183M9: “AlphaFold monomer V2.0 prediction for protein translocase subunit seca 2 (Q183M9)”. 9 pockets (best druggability 0.78). MolNFT v1 #423579 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q183M9
- Type
- protein
- Length
- 781 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9bF5F84C75690a56a78965Df98E262fC9c087f0C
- Molecule
- Protein translocase subunit seca 2
- UniProt
- Q183M9
- Pockets
- 9 · best druggability 0.78
Structure
1 distinct chain · 59% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca 2 | protein | 781 | 59% helix, 12% strand | Q183M9 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1190 | 0.78 | 0.80 | 95 | empty |
| 2 | 369 | 0.58 | 0.76 | 41 | empty |
| 3 | 311 | 0.57 | 0.77 | 44 | empty |
| 4 | 216 | 0.56 | 0.79 | 43 | empty |
| 5 | 146 | 0.55 | 0.81 | 18 | empty |
Compared structures
- 6T4H · Crystal structure of the accessory translocation ATPase, SECA2, from clostridium… · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 6T4H · Crystal structure of the accessory translocation ATPase, SecA2, from Clostridium… · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 6SXH · Crystal structure of the accessory translocation ATPase, SECA2, from clostridium difficile · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 6SXH · Crystal structure of the accessory translocation ATPase, SecA2, from Clostridium difficile · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 Q183M9
- Elsewhere: UniProt Q183M9 · AlphaFold DB Q183M9
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