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AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MMAR_1058 (B2HCU4)
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
- B2HCU4
- Type
- protein
- Length
- 300 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1058
- UniProt
- B2HCU4
- Pockets
- 2 · 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_1058 | protein | 300 | 46% helix, 14% strand | B2HCU4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 600 | 0.86 | 0.91 | 86 | empty |
| 2 | 78 | 0.33 | 0.75 | 20 | 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 B2HCU4
- Elsewhere: UniProt B2HCU4 · AlphaFold DB B2HCU4
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