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Crystal structure of trypanosoma brucei protein arginine methyltransferase 7 complex with adohcy

Analyse Crystal structure of trypanosoma brucei protein arginine methyltransferase 7… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4M37
Type
protein
Length
337 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein arginine N-methyltransferase 7
EC
2.1.1.-
UniProt
Q582G4
Ligands
SAH
Pockets
2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 7 (EC 2.1.1.-)protein33730% helix, 28% strandQ582G4

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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13410.640.7939SAH
2510.470.8516empty

Compared structures

  • 4M37 · Crystal structure of Trypanosoma brucei protein arginine methyltransferase 7 complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q582G4 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 7 (Q582G4) · a predicted model of the same protein · chain A against A, TM-score 1.00

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