Research workbench
Delta-N METTL16 mtase domain
Analyse Delta-N 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
- 6GFK
- Type
- protein
- Length
- 668 residues
- Chains
- 3
- 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, SO4
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 22% 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 | 230 | 42% helix, 21% strand | Q86W50 |
| B | U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase (EC 2.1.1.346, 2.1.1.62) | protein | 220 | 39% helix, 22% strand | Q86W50 |
| C | U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase (EC 2.1.1.346, 2.1.1.62) | protein | 218 | 39% helix, 22% strand | Q86W50 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 3 copies · chains A, B, C
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 858 | 0.74 | 0.78 | 84 | empty |
| 2 | 323 | 0.66 | 0.81 | 41 | SAH, SO4 |
| 3 | 52 | 0.65 | 0.95 | 17 | empty |
| 4 | 281 | 0.62 | 0.80 | 38 | SAH, SO4 |
| 5 | 272 | 0.60 | 0.79 | 40 | SAH, SO4 |
Interfaces
3 interfaces between chains.
- A–C · 919 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 423 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 303 Ų buried · 3 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 Q86W50
- Elsewhere: RCSB PDB 6GFK · PDBe 6GFK · UniProt Q86W50
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