Research workbench
AlphaFold monomer V2.0 prediction for pleiotropic ABC efflux transporter of multiple drugs (P33302)
Analyse AlphaFold monomer V2.0 prediction for pleiotropic ABC efflux transporter of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P33302
- Type
- protein
- Length
- 1,511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC416EAe88162fE5e5FCc9C720A60b7eb703e7AfD
- Molecule
- Pleiotropic ABC efflux transporter of multiple drugs
- UniProt
- P33302
- Pockets
- 20 · best druggability 0.84
Structure
1 distinct chain · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pleiotropic ABC efflux transporter of multiple drugs | protein | 1511 | 52% helix, 11% strand | P33302 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 562 | 0.84 | 0.89 | 48 | empty |
| 2 | 360 | 0.80 | 0.90 | 52 | empty |
| 3 | 398 | 0.80 | 0.89 | 46 | empty |
| 4 | 307 | 0.79 | 0.90 | 61 | empty |
| 5 | 852 | 0.77 | 0.80 | 62 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7P06 · Cryo-EM structure of PDR5 from saccharomyces cerevisiae in outward- facing conformation… · an experimental structure of the same protein · chain A against A, TM-score 0.87
- 7P06 · Cryo-EM structure of Pdr5 from Saccharomyces cerevisiae in outward-facing conformation… · an experimental structure of the same protein · chain A against A, TM-score 0.87
- 7P04 · Cryo-EM structure of PDR5 from saccharomyces cerevisiae in inward- facing conformation… · an experimental structure of the same protein · chain A against A, TM-score 0.84
- 7P04 · Cryo-EM structure of Pdr5 from Saccharomyces cerevisiae in inward-facing conformation… · an experimental structure of the same protein · chain A against A, TM-score 0.84
- 7P05 · Cryo-EM structure of Pdr5 from Saccharomyces cerevisiae in inward-facing conformation… · an experimental structure of the same protein · chain A against A, TM-score 0.83
- 7P05 · Cryo-EM structure of PDR5 from saccharomyces cerevisiae in inward- facing conformation… · an experimental structure of the same protein · chain A against A, TM-score 0.83
- 7P03 · Cryo-EM structure of PDR5 from saccharomyces cerevisiae in inward- facing conformation… · an experimental structure of the same protein · chain A against A, TM-score 0.82
- 7P03 · Cryo-EM structure of Pdr5 from Saccharomyces cerevisiae in inward-facing conformation… · an experimental structure of the same protein · chain A against A, TM-score 0.82
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 P33302
- Elsewhere: UniProt P33302 · AlphaFold DB P33302
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