Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein CTHE_0113 (A3DBM5)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein CTHE_0113… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3DBM5
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3E00F62D3140A99ec52E6a60794edd4CcC68D67b
- Molecule
- Nucleotide-binding protein CTHE_0113
- UniProt
- A3DBM5
- Pockets
- 3 · best druggability 0.51
Structure
1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein CTHE_0113 | protein | 291 | 45% helix, 18% strand | A3DBM5 |
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 | 204 | 0.51 | 0.77 | 30 | empty |
| 2 | 97 | 0.32 | 0.73 | 19 | empty |
| 3 | 70 | 0.32 | 0.75 | 13 | 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 A3DBM5
- Elsewhere: UniProt A3DBM5 · AlphaFold DB A3DBM5
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