Research workbench
AlphaFold monomer V2.0 prediction for protein-lysine N-methyltransferase (F0NBH8)
Analyse AlphaFold monomer V2.0 prediction for protein-lysine N-methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F0NBH8
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x01e98F6aA2b8835b76ABa5D63df70C33997ED954
- UniProt
- F0NBH8
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 161 | — | F0NBH8 |
Compared structures
- 5JWJ · NMR solution structure of a thermophilic lysine methyl transferase from sulfolobus… · an experimental structure of the same protein · chain A against A, TM-score 0.86
- 5JWJ · NMR solution structure of a thermophilic lysine methyl transferase from Sulfolobus… · an experimental structure of the same protein · chain A against A, TM-score 0.86
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 F0NBH8
- Elsewhere: UniProt F0NBH8 · AlphaFold DB F0NBH8
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