Research workbench

Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

Analyse Crystal structure of the conserved core of protein arginine methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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.

Pocket	Volume (Å³)	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

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.