Research workbench
AlphaFold monomer V2.0 prediction for zinc import ATP-binding protein znuc (A0LCH8)
Analyse AlphaFold monomer V2.0 prediction for zinc import ATP-binding protein znuc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0LCH8
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71351b1FB9B1B80D8d60E1f869F762a9c785B183
- Molecule
- Zinc import ATP-binding protein znuc
- UniProt
- A0LCH8
- Pockets
- 2 · best druggability 0.39
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc import ATP-binding protein znuc | protein | 260 | 38% helix, 24% strand | A0LCH8 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.39 | 0.80 | 12 | empty |
| 2 | 76 | 0.33 | 0.74 | 12 | 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 A0LCH8
- Elsewhere: UniProt A0LCH8 · AlphaFold DB A0LCH8
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