Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein AMB4396 (Q2VYX5)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein AMB4396… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2VYX5
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79C8eac7b0A7F48c5Dc63A746EA9A516335a21cf
- Molecule
- Nucleotide-binding protein AMB4396
- UniProt
- Q2VYX5
- Pockets
- 3 · best druggability 0.49
Structure
1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein AMB4396 | protein | 306 | 41% helix, 17% strand | Q2VYX5 |
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 | 162 | 0.49 | 0.77 | 27 | empty |
| 2 | 85 | 0.33 | 0.74 | 25 | empty |
| 3 | 62 | 0.32 | 0.76 | 17 | 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 Q2VYX5
- Elsewhere: UniProt Q2VYX5 · AlphaFold DB Q2VYX5
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