Research workbench
Crystal structure of mouse protein arginine methyltransferase 7 in complex with sah
Analyse Crystal structure of mouse protein arginine methyltransferase 7 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C4A
- Type
- protein
- Length
- 641 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein arginine N-methyltransferase 7
- EC
- 2.1.1.-, 2.1.1.125, 2.1.1.126
- UniProt
- Q922X9
- Ligands
- SAH, DMX, ZN
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arginine N-methyltransferase 7 (EC 2.1.1.-, 2.1.1.125, 2.1.1.126) | protein | 641 | 27% helix, 34% strand | Q922X9 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- DMX · 3-[benzyl(dimethyl)ammonio]propane-1-sulfonate · ligand · chains A
- ZN · Zinc ion · metal · chains A
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 865 | 0.76 | 0.80 | 109 | SAH |
| 2 | 126 | 0.65 | 0.88 | 29 | empty |
| 3 | 61 | 0.52 | 0.87 | 22 | empty |
| 4 | 60 | 0.36 | 0.78 | 13 | empty |
| 5 | 78 | 0.33 | 0.75 | 17 | DMX |
Compared structures
- 4C4A · Crystal structure of mouse protein arginine methyltransferase 7 in complex with SAH · the same entry in another collection · chain A against A, TM-score 1.00
- Q922X9 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 7 (Q922X9) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q922X9
- Elsewhere: RCSB PDB 4C4A · PDBe 4C4A · UniProt Q922X9
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