Research workbench
AlphaFold monomer V2.0 prediction for hemolysin (P09545)
Analyse AlphaFold monomer V2.0 prediction for hemolysin (P09545) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P09545
- Type
- protein
- Length
- 741 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661E995327D4c9b99E17Cca11ea8072ed8a218Dd
- Molecule
- Hemolysin
- UniProt
- P09545
- Pockets
- 5 · best druggability 0.79
Structure
1 distinct chain · 11% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemolysin | protein | 741 | 11% helix, 44% strand | P09545 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1021 | 0.79 | 0.81 | 96 | empty |
| 2 | 199 | 0.63 | 0.83 | 33 | empty |
| 3 | 169 | 0.52 | 0.79 | 22 | empty |
| 4 | 105 | 0.39 | 0.76 | 21 | empty |
| 5 | 72 | 0.28 | 0.73 | 19 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1XEZ · Crystal Structure Of The Vibrio Cholerae Cytolysin (HlyA) Pro-Toxin With Octylglucoside… · an experimental structure of the same protein · chain A against A, TM-score 0.89
- 1XEZ · Crystal structure of the vibrio cholerae cytolysin (hlya) pro-toxin with octylglucoside… · an experimental structure of the same protein · chain A against A, TM-score 0.89
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 P09545
- Elsewhere: UniProt P09545 · AlphaFold DB P09545
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.