MolNFT v1 · #123517 · protein

Crystal structure of mus musculus protein arginine methyltransferase 2 with CP3

5JMQ · Protein arginine N-methyltransferase 2: “Crystal structure of mus musculus protein arginine methyltransferase 2 with CP3”. X-ray diffraction, 3 ligands (6LC, CA, CL), 1 pocket (best druggability 0.73). MolNFT v1 #123517 on…

PDB: 5JMQ
Type: protein
Length: 339 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein arginine N-methyltransferase 2
UniProt: Q3UKX1
Ligands: 6LC, CA, CL
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein arginine N-methyltransferase 2	protein	339	26% helix, 36% strand	Q3UKX1

Ligands and binding sites

6LC · 9-[(5E)-7-carbamimidamido-5,6,7-trideoxy-beta-D-ribo-hept-5-enofuranosyl]-9H-purin-6-amine · ligand · chains A
CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 4 copies · chains A
PG4 · Tetraethylene glycol · additive · 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	358	0.73	0.84	44	EDO, 6LC

Compared structures

5JMQ · Crystal Structure of Mus musculus Protein Arginine Methyltransferase 2 with CP3 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q3UKX1
Elsewhere: RCSB PDB 5JMQ · PDBe 5JMQ · UniProt Q3UKX1

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