MolNFT v1 · #17371 · protein

Structure of the predominant protein arginine methyltransferase PRMT1

1ORI · Protein arginine N-methyltransferase 1: “Structure of the predominant protein arginine methyltransferase PRMT1”. X-ray diffraction, 2 ligands (UNL, SAH), 1 pocket (best druggability 0.67). MolNFT v1 #17371 on GenesisL1: 3D…

PDB: 1ORI
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein arginine N-methyltransferase 1
EC: 2.1.1.125
UniProt: Q63009
Ligands: UNL, SAH
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein arginine N-methyltransferase 1 (EC 2.1.1.125)	protein	316	26% helix, 40% strand	Q63009

Ligands and binding sites

UNL · Unknown ligand · ligand · 2 copies · chains A
SAH · S-adenosyl-L-homocysteine · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	375	0.67	0.80	48	SAH, UNL

Compared structures

1ORI · Structure of the predominant protein arginine methyltransferase PRMT1 · the same entry in another collection · chain A against A, TM-score 1.00
Q63009 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 1 (Q63009) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q63009
Elsewhere: RCSB PDB 1ORI · PDBe 1ORI · UniProt Q63009

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