MolNFT v1 · #6141 · protein
Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
1F3L: “Crystal structure of the conserved core of protein arginine methyltransferase PRMT3”. X-ray diffraction, 1 ligand (SAH), 3 pockets (best druggability 0.81). MolNFT v1 #6141 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1F3L
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein arginine methyltransferase PRMT3
- UniProt
- O70467
- Ligands
- SAH
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arginine methyltransferase PRMT3 | protein | 321 | 26% helix, 37% strand | O70467 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.81 | 0.97 | 32 | SAH |
| 2 | 51 | 0.61 | 0.93 | 17 | empty |
| 3 | 99 | 0.41 | 0.77 | 18 | empty |
Compared structures
- 1F3L · Crystal structure of the conserved core of protein arginine methyltransferase PRMT3 · the same entry in another collection · chain A against A, TM-score 1.00
- O70467 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 3 (O70467) · 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 O70467
- Elsewhere: RCSB PDB 1F3L · PDBe 1F3L · UniProt O70467
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