Research workbench
Structure of the 16S rRNA methylase rmtb, P21
Analyse Structure of the 16S rRNA methylase rmtb, P21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FRH
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 16S rRNA methylase
- EC
- 2.1.1.-
- UniProt
- Q763K9
- Ligands
- SAH
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 16S rRNA methylase (EC 2.1.1.-) | protein | 241 | 47% helix, 21% strand | Q763K9 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 259 | 0.72 | 0.87 | 41 | SAH |
| 2 | 74 | 0.44 | 0.81 | 17 | empty |
| 3 | 62 | 0.35 | 0.78 | 17 | empty |
Compared structures
- 3FRH · Structure of the 16S rRNA methylase RmtB, P21 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q763K9
- Elsewhere: RCSB PDB 3FRH · PDBe 3FRH · UniProt Q763K9
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