Research workbench
AlphaFold monomer V2.0 prediction for beta-(1-->2)GLUCAN export ATP- BINDING/PERMEASE protein ndva (Q1QH37)
Analyse AlphaFold monomer V2.0 prediction for beta-(1-->2)GLUCAN export ATP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1QH37
- Type
- protein
- Length
- 593 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- Beta-(1-->2)GLUCAN export ATP-BINDING/PERMEASE protein ndva
- UniProt
- Q1QH37
- Pockets
- 6 · best druggability 0.55
Structure
1 distinct chain · 66% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-(1-->2)GLUCAN export ATP-BINDING/PERMEASE protein ndva | protein | 593 | 66% helix, 10% strand | Q1QH37 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 303 | 0.55 | 0.75 | 32 | empty |
| 2 | 80 | 0.53 | 0.85 | 19 | empty |
| 3 | 164 | 0.46 | 0.75 | 25 | empty |
| 4 | 153 | 0.43 | 0.74 | 21 | empty |
| 5 | 90 | 0.38 | 0.77 | 18 | 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 Q1QH37
- Elsewhere: UniProt Q1QH37 · AlphaFold DB Q1QH37
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