Research workbench
METTL16 mtase domain
Analyse METTL16 mtase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GFN
- Type
- protein
- Length
- 254 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase
- EC
- 2.1.1.346, 2.1.1.62
- UniProt
- Q86W50
- Ligands
- SAH
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase (EC 2.1.1.346, 2.1.1.62) | protein | 254 | 41% helix, 20% strand | Q86W50 |
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 | 264 | 0.61 | 0.80 | 42 | SAH |
| 2 | 83 | 0.37 | 0.76 | 20 | empty |
| 3 | 59 | 0.31 | 0.76 | 13 | empty |
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 Q86W50
- Elsewhere: RCSB PDB 6GFN · PDBe 6GFN · UniProt Q86W50
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