Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein BMA3112 (Q62FD0)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein BMA3112… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q62FD0
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Nucleotide-binding protein BMA3112
- UniProt
- Q62FD0
- Pockets
- 4 · best druggability 0.53
Structure
1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein BMA3112 | protein | 297 | 43% helix, 20% strand | Q62FD0 |
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 | 209 | 0.53 | 0.78 | 32 | empty |
| 2 | 189 | 0.50 | 0.77 | 24 | empty |
| 3 | 81 | 0.42 | 0.80 | 18 | empty |
| 4 | 97 | 0.36 | 0.74 | 15 | 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 Q62FD0
- Elsewhere: UniProt Q62FD0 · AlphaFold DB Q62FD0
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