MolNFT v1 · #504071 · protein
AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MMAR_1069 (B2HCV3)
B2HCV3 · Putative S-adenosyl-L-methionine-dependent…: “AlphaFold monomer V2.0 prediction for putative S-adenosyl-L- methionine-dependent methyltransferase MMAR_1069…”. 3 pockets (best druggability 0.86). MolNFT v1 #504071 on GenesisL1: 3D…
- Accession
- B2HCV3
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x51B7636bc80cc968e87D857214f08A0195D96382
- Molecule
- Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1069
- UniProt
- B2HCV3
- Pockets
- 3 · best druggability 0.86
Structure
1 distinct chain · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_1069 | protein | 316 | 45% helix, 13% strand | B2HCV3 |
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 | 484 | 0.86 | 0.92 | 81 | empty |
| 2 | 71 | 0.46 | 0.82 | 19 | empty |
| 3 | 105 | 0.40 | 0.76 | 22 | 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 B2HCV3
- Elsewhere: UniProt B2HCV3 · AlphaFold DB B2HCV3
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