Research workbench
Apo-form of T. thermophilus 16S rRNA A1518 and A1519 methyltransferase (ksga) in space group P43212
Analyse Apo-form of T. thermophilus 16S rRNA A1518 and A1519 methyltransferase (ksga)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FUV
- Type
- protein
- Length
- 768 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dimethyladenosine transferase
- EC
- 2.1.1.-
- UniProt
- Q5SM60
- Pockets
- 14 · best druggability 0.60
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dimethyladenosine transferase (EC 2.1.1.-) | protein | 260 | 44% helix, 19% strand | Q5SM60 |
| B | Dimethyladenosine transferase (EC 2.1.1.-) | protein | 256 | 44% helix, 18% strand | Q5SM60 |
| C | Dimethyladenosine transferase (EC 2.1.1.-) | protein | 252 | 44% helix, 19% strand | Q5SM60 |
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 386 | 0.60 | 0.76 | 31 | empty |
| 2 | 167 | 0.59 | 0.82 | 32 | empty |
| 3 | 358 | 0.58 | 0.76 | 31 | empty |
| 4 | 257 | 0.56 | 0.77 | 33 | empty |
| 5 | 143 | 0.56 | 0.82 | 37 | empty |
Interfaces
2 interfaces between chains.
- A–C · 641 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 624 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3FUV · Apo-form of T. thermophilus 16S rRNA A1518 and A1519 methyltransferase (KsgA) in space… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5SM60 · AlphaFold monomer V2.0 prediction for ribosomal RNA small subunit methyltransferase a… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q5SM60
- Elsewhere: RCSB PDB 3FUV · PDBe 3FUV · UniProt Q5SM60
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