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AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MMAR_1068 (B2HCV2)
Analyse AlphaFold monomer V2.0 prediction for putative S-adenosyl-L… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2HCV2
- Type
- protein
- Length
- 302 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7025bA95cbd795796733105284DD3E7B741Ab901
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1068
- UniProt
- B2HCV2
- Pockets
- 3 · best druggability 0.86
Structure
1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1068 | protein | 302 | 46% helix, 14% strand | B2HCV2 |
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 | 344 | 0.86 | 0.96 | 62 | empty |
| 2 | 110 | 0.45 | 0.79 | 20 | empty |
| 3 | 54 | 0.27 | 0.74 | 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 B2HCV2
- Elsewhere: UniProt B2HCV2 · AlphaFold DB B2HCV2
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