MolNFT v1 · #47163 · protein
Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)
2OQB · Histone-arginine methyltransferase CARM1: “Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.65). MolNFT v1 #47163 on…
- PDB
- 2OQB
- Type
- protein
- Length
- 214 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
- UniProt
- Q4AE70
- Ligands
- CL
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-arginine methyltransferase CARM1 (EC 2.1.1.125) | protein | 108 | 13% helix, 55% strand | Q4AE70 |
| B | Histone-arginine methyltransferase CARM1 (EC 2.1.1.125) | protein | 106 | 10% helix, 49% strand | Q4AE70 |
Ligands and binding sites
- CL · Chloride ion · ion · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.65 | 0.87 | 22 | empty |
| 2 | 189 | 0.53 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1100 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 2OQB · Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1… · 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 B against A, TM-score 0.92
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 2OQB · PDBe 2OQB · UniProt Q4AE70
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