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Crystal structure of C.elegans PRMT7 in complex with SAH (P43212)

Analyse Crystal structure of C.elegans PRMT7 in complex with SAH (P43212) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3X0D
Type
protein
Length
624 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.15
Source
Caenorhabditis elegans
Molecule
Protein arginine N-methyltransferase 7
EC
2.1.1.-
UniProt
Q9XW42
Ligands
SAH, ZN
Pockets
7 · best druggability 0.75

Structure

x-ray diffraction · resolution 2.15 · 1 distinct chain · 27% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 7 (EC 2.1.1.-)protein62427% helix, 30% strandQ9XW42

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · chains A
  • ZN · Zinc ion · metal · chains A

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18480.750.7989SAH
21720.660.8624empty
3670.650.9328empty
41340.570.8322empty
5770.500.8315empty

Compared structures

  • 3X0D · Crystal structure of C.ELEGANS PRMT7 in complex with sah (P43212) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9XW42 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 7 (Q9XW42) · a predicted model of the same protein · chain A against A, TM-score 0.99

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