Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein xcc-B100_1354 (B0RQG9)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein xcc-B100_1354… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0RQG9
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Nucleotide-binding protein xcc-B100_1354
- UniProt
- B0RQG9
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein xcc-B100_1354 | protein | 282 | 48% helix, 16% strand | B0RQG9 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.56 | 0.79 | 26 | empty |
| 2 | 157 | 0.46 | 0.77 | 23 | empty |
| 3 | 54 | 0.32 | 0.77 | 14 | 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 B0RQG9
- Elsewhere: UniProt B0RQG9 · AlphaFold DB B0RQG9
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