Research workbench
AlphaFold monomer V2.0 prediction for oligopeptide transport ATP- binding protein oppf (P0CZ32)
Analyse AlphaFold monomer V2.0 prediction for oligopeptide transport ATP- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CZ32
- Type
- protein
- Length
- 307 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc65cB70a906CEEA439D51B5d816F369AA26D074F
- Molecule
- Oligopeptide transport ATP-binding protein oppf
- UniProt
- P0CZ32
- Pockets
- 4 · best druggability 0.48
Structure
1 distinct chain · 42% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oligopeptide transport ATP-binding protein oppf | protein | 307 | 42% helix, 25% strand | P0CZ32 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.48 | 0.76 | 31 | empty |
| 2 | 58 | 0.32 | 0.76 | 10 | empty |
| 3 | 64 | 0.32 | 0.75 | 12 | empty |
| 4 | 58 | 0.32 | 0.75 | 11 | 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 P0CZ32
- Elsewhere: UniProt P0CZ32 · AlphaFold DB P0CZ32
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