Research workbench
Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), unliganded
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
- 2V7E
- Type
- protein
- Length
- 644 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-arginine methyltransferase CARM1
- EC
- 2.1.1.-
- UniProt
- Q9WVG6
- Ligands
- HG
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Histone-arginine methyltransferase CARM1 (EC 2.1.1.-) | protein | 322 | 26% helix, 37% strand | Q9WVG6 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 3 copies · chains A, B
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 | 391 | 0.64 | 0.78 | 46 | HG |
| 2 | 305 | 0.62 | 0.79 | 55 | empty |
Interfaces
1 interface between chains.
- A–B · 1688 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 2V7E · Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WVG6 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q9WVG6) · a predicted model of the same protein · chain B 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 Q9WVG6
- Elsewhere: RCSB PDB 2V7E · PDBe 2V7E · UniProt Q9WVG6
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