Research workbench
AlphaFold monomer V2.0 prediction for putative ABC transporter ATP- binding protein SSO1893 (Q97X60)
Analyse AlphaFold monomer V2.0 prediction for putative ABC transporter ATP- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q97X60
- Type
- protein
- Length
- 530 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd2B806f92bedc80F03610Bf62FF190193655f360
- Molecule
- Putative ABC transporter ATP-binding protein SSO1893
- UniProt
- Q97X60
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ABC transporter ATP-binding protein SSO1893 | protein | 530 | 39% helix, 25% strand | Q97X60 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 766 | 0.77 | 0.81 | 100 | empty |
| 2 | 267 | 0.56 | 0.77 | 24 | empty |
| 3 | 201 | 0.54 | 0.78 | 24 | empty |
| 4 | 55 | 0.35 | 0.78 | 12 | 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 Q97X60
- Elsewhere: UniProt Q97X60 · AlphaFold DB Q97X60
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