Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein MRA_1430 (A5U2C3)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein MRA_1430… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5U2C3
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1e766cf26De71e382B3A4fab285Ff5E14E07c319
- Molecule
- Nucleotide-binding protein MRA_1430
- UniProt
- A5U2C3
- Pockets
- 4 · best druggability 0.51
Structure
1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein MRA_1430 | protein | 301 | 41% helix, 18% strand | A5U2C3 |
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 | 57 | 0.51 | 0.87 | 22 | empty |
| 2 | 197 | 0.47 | 0.75 | 26 | empty |
| 3 | 111 | 0.44 | 0.78 | 27 | empty |
| 4 | 82 | 0.41 | 0.79 | 24 | 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 A5U2C3
- Elsewhere: UniProt A5U2C3 · AlphaFold DB A5U2C3
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