Research workbench
T. thermophilus 16S rRNA N2 G1207 methyltransferase (rsmc) in complex with adomet
Analyse T. thermophilus 16S rRNA N2 G1207 methyltransferase (rsmc) 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
- 3DMF
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable ribosomal RNA small subunit methyltransferase
- EC
- 2.1.1.-
- UniProt
- Q5SKW0
- Ligands
- SAM, SO4
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable ribosomal RNA small subunit methyltransferase (EC 2.1.1.-) | protein | 371 | 31% helix, 31% strand | Q5SKW0 |
Ligands and binding sites
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 | 646 | 0.73 | 0.80 | 63 | SO4, SAM |
| 2 | 56 | 0.38 | 0.79 | 11 | empty |
Compared structures
- 3DMF · T. Thermophilus 16S rRNA N2 G1207 methyltransferase (RsmC) in complex with AdoMet · 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 Q5SKW0
- Elsewhere: RCSB PDB 3DMF · PDBe 3DMF · UniProt Q5SKW0
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