Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent permease PDR12 (Q02785)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent permease PDR12 (Q02785) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q02785
- Type
- protein
- Length
- 1,511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF435Cc7528760B6B8D880Df3befF1C3095f62B98
- Molecule
- ATP-dependent permease PDR12
- UniProt
- Q02785
- Pockets
- 17 · best druggability 0.86
Structure
1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent permease PDR12 | protein | 1511 | 54% helix, 12% strand | Q02785 |
Pockets
17 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 955 | 0.86 | 0.87 | 114 | empty |
| 2 | 568 | 0.85 | 0.90 | 79 | empty |
| 3 | 269 | 0.78 | 0.90 | 35 | empty |
| 4 | 658 | 0.76 | 0.82 | 61 | empty |
| 5 | 130 | 0.76 | 0.94 | 25 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 Q02785
- Elsewhere: UniProt Q02785 · AlphaFold DB Q02785
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