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Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), in complex with S-adenosyl-homocysteine

Analyse Crystal structure of coactivator-associated arginine methyltransferase 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2V74
Type
protein
Length
1,329 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
Q9WVG6

Structure

x-ray diffraction · 4 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
B—protein332—Q9WVG6
D—protein333—Q9WVG6
F—protein333—Q9WVG6
H—protein331—Q9WVG6

Compared structures

  • 2V74 · Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), in… · the same entry in another collection · chain D against D, TM-score 1.00
  • Q9WVG6 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q9WVG6) · a predicted model of the same protein · chain D against A, TM-score 0.99

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