Research workbench
AlphaFold monomer V2.0 prediction for zinc metalloproteinase (P23224)
Analyse AlphaFold monomer V2.0 prediction for zinc metalloproteinase (P23224) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23224
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA722eA6E71d03bAe87Bd6148797813D88FAe94D0
- Molecule
- Zinc metalloproteinase
- UniProt
- P23224
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 31% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc metalloproteinase | protein | 510 | 31% helix, 24% strand | P23224 |
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 | 513 | 0.70 | 0.80 | 55 | empty |
| 2 | 456 | 0.65 | 0.78 | 49 | empty |
| 3 | 131 | 0.53 | 0.81 | 32 | empty |
| 4 | 85 | 0.44 | 0.80 | 12 | empty |
| 5 | 102 | 0.37 | 0.75 | 24 | 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 P23224
- Elsewhere: UniProt P23224 · AlphaFold DB P23224
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