Research workbench
AlphaFold monomer V2.0 prediction for proteases secretion ATP-binding protein prtd (P23596)
Analyse AlphaFold monomer V2.0 prediction for proteases secretion ATP-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23596
- Type
- protein
- Length
- 575 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Proteases secretion ATP-binding protein prtd
- UniProt
- P23596
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 66% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteases secretion ATP-binding protein prtd | protein | 575 | 66% helix, 11% strand | P23596 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 639 | 0.65 | 0.75 | 53 | empty |
| 2 | 168 | 0.49 | 0.76 | 15 | empty |
| 3 | 77 | 0.39 | 0.77 | 16 | empty |
| 4 | 75 | 0.36 | 0.77 | 14 | 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 P23596
- Elsewhere: UniProt P23596 · AlphaFold DB P23596
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