Research workbench
AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MMAR_1057 (B2HCU3)
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
- B2HCU3
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79C8eac7b0A7F48c5Dc63A746EA9A516335a21cf
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1057
- UniProt
- B2HCU3
- Pockets
- 2 · best druggability 0.86
Structure
1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1057 | protein | 304 | 45% helix, 14% strand | B2HCU3 |
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 | 763 | 0.86 | 0.89 | 92 | empty |
| 2 | 62 | 0.29 | 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 B2HCU3
- Elsewhere: UniProt B2HCU3 · AlphaFold DB B2HCU3
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