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The 2.4 a crystal structure of the apo catalytic domain of coactivator-associated arginine methyl transferase I(CARM1,140-480).

Analyse The 2.4 a crystal structure of the apo catalytic domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3B3G
Type
protein
Length
648 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone-arginine methyltransferase CARM1
EC
2.1.1.125, 2.1.1.-
UniProt
Q4AE70
Pockets
3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHistone-arginine methyltransferase CARM1 (EC 2.1.1.125, 2.1.1.-)protein32427% helix, 38% strandQ4AE70

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12950.550.7635empty
22910.550.7633empty
3600.340.7714empty

Interfaces

1 interface between chains.

  • A–B · 1758 Ų buried · 24 hydrogen bonds · protein-protein

Compared structures

  • 3B3G · The 2.4 A crystal structure of the apo catalytic domain of coactivator-associated… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q4AE70 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q4AE70) · a predicted model of the same protein · chain A against A, TM-score 0.99

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