Research workbench
NMR solution structure of a thermophilic lysine methyl transferase from sulfolobus islandicus
Analyse NMR solution structure of a thermophilic lysine methyl transferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JWJ
- Type
- protein
- Length
- 162 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-lysine N-methyltransferase
- EC
- 2.1.1.-
- UniProt
- F0NBH8
- Pockets
- 2 · best druggability 0.69
Structure
solution nmr · 1 distinct chain · 25% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-lysine N-methyltransferase (EC 2.1.1.-) | protein | 162 | 25% helix, 21% strand | F0NBH8 |
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 | 393 | 0.69 | 0.81 | 45 | empty |
| 2 | 53 | 0.38 | 0.80 | 13 | empty |
Compared structures
- 5JWJ · NMR solution structure of a thermophilic lysine methyl transferase from Sulfolobus… · the same entry in another collection · chain A against A, TM-score 1.00
- F0NBH8 · AlphaFold monomer V2.0 prediction for protein-lysine N-methyltransferase (F0NBH8) · a predicted model 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: RCSB PDB 5JWJ · PDBe 5JWJ · UniProt F0NBH8
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