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AlphaFold monomer V2.0 prediction for nucleotide-binding protein BMA10229_A1510 (A2S6C3)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein BMA10229_A1510… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2S6C3
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Nucleotide-binding protein BMA10229_A1510
- UniProt
- A2S6C3
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein BMA10229_A1510 | protein | 297 | 44% helix, 20% strand | A2S6C3 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.52 | 0.78 | 33 | empty |
| 2 | 199 | 0.49 | 0.76 | 24 | empty |
| 3 | 69 | 0.36 | 0.77 | 14 | empty |
| 4 | 76 | 0.30 | 0.73 | 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 A2S6C3
- Elsewhere: UniProt A2S6C3 · AlphaFold DB A2S6C3
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