Research workbench
Crystal structure of 16S rRNA methyltransferase rmtf in complex with S-adenosyl-L-homocysteine
Analyse Crystal structure of 16S rRNA methyltransferase rmtf in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PI9
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 16S rRNA (GUANINE(1405)-N(7))-methyltransferase
- EC
- 2.1.1.179
- UniProt
- I1YZZ5
- Ligands
- SAH
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 16S rRNA (GUANINE(1405)-N(7))-methyltransferase (EC 2.1.1.179) | protein | 260 | 51% helix, 17% strand | I1YZZ5 |
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
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 | 202 | 0.74 | 0.90 | 40 | SAH |
| 2 | 60 | 0.38 | 0.80 | 18 | empty |
Compared structures
- 6PI9 · Crystal structure of 16S rRNA methyltransferase RmtF in complex with… · 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 I1YZZ5
- Elsewhere: RCSB PDB 6PI9 · PDBe 6PI9 · UniProt I1YZZ5
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