Research workbench
AlphaFold monomer V2.0 prediction for zinc import ATP-binding protein znuc (Q92P76)
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
- Q92P76
- Type
- protein
- Length
- 302 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7E60B954e5d9c3fdcf523d6f27d5Ced1637C0C0D
- Molecule
- Zinc import ATP-binding protein znuc
- UniProt
- Q92P76
- Pockets
- 3 · best druggability 0.43
Structure
1 distinct chain · 28% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc import ATP-binding protein znuc | protein | 302 | 28% helix, 22% strand | Q92P76 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.43 | 0.78 | 14 | empty |
| 2 | 62 | 0.38 | 0.79 | 14 | empty |
| 3 | 82 | 0.35 | 0.75 | 17 | empty |
Modifications
Observed in the structure: 2 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 Q92P76
- Elsewhere: UniProt Q92P76 · AlphaFold DB Q92P76
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