Research workbench
AlphaFold monomer V2.0 prediction for zinc import ATP-binding protein znuc (Q5PIA5)
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
- Q5PIA5
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9C5cB57d1eDa7581935cB65276f4b016326De568
- Molecule
- Zinc import ATP-binding protein znuc
- UniProt
- Q5PIA5
- Pockets
- 4 · best druggability 0.40
Structure
1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc import ATP-binding protein znuc | protein | 251 | 36% helix, 25% strand | Q5PIA5 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.40 | 0.75 | 17 | empty |
| 2 | 79 | 0.33 | 0.74 | 15 | empty |
| 3 | 61 | 0.31 | 0.75 | 12 | empty |
| 4 | 51 | 0.29 | 0.75 | 11 | 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 Q5PIA5
- Elsewhere: UniProt Q5PIA5 · AlphaFold DB Q5PIA5
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