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The 2.55 a crystal structure of the apo catalytic domain of coactivator-associated arginine methyl transferase I(CARM1:28-507, residues 28-146 and 479-507 not ordered)
Analyse The 2.55 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
- 3B3J
- Type
- protein
- Length
- 332 residues
- Chains
- 1
- 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
- Ligands
- BEN
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-arginine methyltransferase CARM1 (EC 2.1.1.125, 2.1.1.-) | protein | 332 | 27% helix, 37% strand | Q4AE70 |
Ligands and binding sites
- BEN · Benzamidine · ligand · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.79 | 0.98 | 17 | BEN |
| 2 | 304 | 0.65 | 0.81 | 32 | BEN |
| 3 | 108 | 0.48 | 0.80 | 20 | empty |
| 4 | 151 | 0.46 | 0.76 | 25 | empty |
Compared structures
- 3B3J · The 2.55 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 0.89
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 Q4AE70
- Elsewhere: RCSB PDB 3B3J · PDBe 3B3J · UniProt Q4AE70
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