Research workbench
Crystal structure of 16S rRNA methyltranferase
Analyse Crystal structure of 16S rRNA methyltranferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MTE
- Type
- protein
- Length
- 438 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 16S rRNA methylase
- UniProt
- A8C927
- Ligands
- SAM
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 16S rRNA methylase | protein | 219 | 40% helix, 28% strand | A8C927 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 400 | 0.66 | 0.79 | 42 | empty |
| 2 | 405 | 0.63 | 0.77 | 58 | SAM |
| 3 | 170 | 0.60 | 0.82 | 27 | SAM |
| 4 | 112 | 0.45 | 0.78 | 18 | empty |
| 5 | 70 | 0.40 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 521 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 A8C927
- Elsewhere: RCSB PDB 3MTE · PDBe 3MTE · UniProt A8C927
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