Research workbench
AlphaFold monomer V2.0 prediction for ABC transporter ATP-binding protein rama (O88039)
Analyse AlphaFold monomer V2.0 prediction for ABC transporter ATP-binding protein rama… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O88039
- Type
- protein
- Length
- 636 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8BCf7F9aD1d31a7dae90D9C5756CAF8f8aCfA15B
- Molecule
- ABC transporter ATP-binding protein rama
- UniProt
- O88039
- Pockets
- 7 · best druggability 0.70
Structure
1 distinct chain · 56% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC transporter ATP-binding protein rama | protein | 636 | 56% helix, 10% strand | O88039 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.70 | 0.98 | 17 | empty |
| 2 | 240 | 0.54 | 0.77 | 29 | empty |
| 3 | 161 | 0.43 | 0.75 | 29 | empty |
| 4 | 57 | 0.36 | 0.79 | 17 | empty |
| 5 | 73 | 0.34 | 0.75 | 16 | 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 O88039
- Elsewhere: UniProt O88039 · AlphaFold DB O88039
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