Research workbench
Crystal structure of human protein arginine N-methyltransferase 6 (PRMT6) in complex with SGC6870 inhibitor
Analyse Crystal structure of human protein arginine N-methyltransferase 6 (PRMT6) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W6D
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein arginine N-methyltransferase 6
- EC
- 2.1.1.319
- UniProt
- Q96LA8
- Ligands
- SAH, T9A
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arginine N-methyltransferase 6 (EC 2.1.1.319) | protein | 328 | 30% helix, 34% strand | Q96LA8 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- T9A · (5R)-4-(5-bromothiophene-2-carbonyl)-5-(3,5-dimethylphenyl)-7-methyl-1,3,4,5-tetrahydro-2H-1,4-benzodiazepin-2-one · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 294 | 0.83 | 0.93 | 35 | T9A |
| 2 | 370 | 0.62 | 0.78 | 39 | SAH |
Compared structures
- 6W6D · Crystal Structure of Human Protein arginine N-methyltransferase 6 (PRMT6) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q96LA8 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 6 (Q96LA8) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q96LA8
- Elsewhere: RCSB PDB 6W6D · PDBe 6W6D · UniProt Q96LA8
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