Research workbench
AlphaFold monomer V2.0 prediction for ZINC/CADMIUM resistance protein (P20107)
Analyse AlphaFold monomer V2.0 prediction for ZINC/CADMIUM resistance protein (P20107) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P20107
- Type
- protein
- Length
- 442 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- ZINC/CADMIUM resistance protein
- UniProt
- P20107
- Pockets
- 5 · best druggability 0.75
Structure
1 distinct chain · 51% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ZINC/CADMIUM resistance protein | protein | 442 | 51% helix, 6% strand | P20107 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1187 | 0.75 | 0.78 | 78 | empty |
| 2 | 100 | 0.38 | 0.76 | 17 | empty |
| 3 | 100 | 0.34 | 0.73 | 15 | empty |
| 4 | 56 | 0.29 | 0.75 | 12 | empty |
| 5 | 50 | 0.26 | 0.73 | 11 | empty |
Modifications
Observed in the structure: 1 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 P20107
- Elsewhere: UniProt P20107 · AlphaFold DB P20107
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