Research workbench
Crystal structure of SAH bound protein arginine N-methyltransferase 1 (PRMT1) from Naegleria fowleri
Analyse Crystal structure of SAH bound protein arginine N-methyltransferase 1 (PRMT1)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8FT7
- Type
- protein
- Length
- 628 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.15
- Source
- Naegleria fowleri
- Molecule
- PUA domain-containing protein
- UniProt
- A0A6A5BBK9
- Ligands
- SAH
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · resolution 2.15 · 1 distinct chain · 27% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | PUA domain-containing protein | protein | 314 | 27% helix, 39% strand | A0A6A5BBK9 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.60 | 0.78 | 35 | SAH |
| 2 | 256 | 0.59 | 0.79 | 34 | SAH |
| 3 | 125 | 0.50 | 0.80 | 18 | empty |
| 4 | 108 | 0.50 | 0.81 | 19 | empty |
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 A0A6A5BBK9
- Elsewhere: RCSB PDB 8FT7 · PDBe 8FT7 · UniProt A0A6A5BBK9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.