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The 2.2 a crystal structure of the catalytic domain of coactivator- associated arginine methyl transferase I(CARM1,142-478), in complex with S-adenosyl homocysteine
Analyse The 2.2 a crystal structure of the catalytic domain of coactivator- associated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B3F
- Type
- protein
- Length
- 1,348 residues
- Chains
- 4
- 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
- SAH
- Pockets
- 6 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Histone-arginine methyltransferase CARM1 (EC 2.1.1.125, 2.1.1.-) | protein | 337 | 30% helix, 36% strand | Q4AE70 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1106 | 0.80 | 0.81 | 109 | SAH |
| 2 | 560 | 0.78 | 0.85 | 67 | SAH |
| 3 | 384 | 0.78 | 0.87 | 52 | SAH |
| 4 | 258 | 0.71 | 0.86 | 40 | SAH |
| 5 | 75 | 0.32 | 0.74 | 16 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1884 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 1844 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 3B3F · The 2.2 A crystal structure of the catalytic domain of coactivator-associated arginine… · the same entry in another collection · chain D against D, 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
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 3B3F · PDBe 3B3F · UniProt Q4AE70
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