Research workbench
AlphaFold monomer V2.0 prediction for snake venom metalloproteinase atrolysin-C (Q90392)
Analyse AlphaFold monomer V2.0 prediction for snake venom metalloproteinase atrolysin-C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q90392
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x66fcE48dCDE99F905F9F830Ddeb84bE60d9C1089
- Molecule
- Snake venom metalloproteinase atrolysin-C
- UniProt
- Q90392
- Pockets
- 7 · best druggability 0.58
Structure
1 distinct chain · 20% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Snake venom metalloproteinase atrolysin-C | protein | 414 | 20% helix, 27% strand | Q90392 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.58 | 0.81 | 21 | empty |
| 2 | 167 | 0.57 | 0.81 | 30 | empty |
| 3 | 159 | 0.53 | 0.80 | 26 | empty |
| 4 | 141 | 0.49 | 0.78 | 25 | empty |
| 5 | 112 | 0.40 | 0.76 | 18 | 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 Q90392
- Elsewhere: UniProt Q90392 · AlphaFold DB Q90392
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