MolNFT v1 · #125698 · protein
Crystal structure of mouse CARM1 in complex with ligand P2C3U
5LGS · Histone-arginine methyltransferase CARM1: “Crystal structure of mouse CARM1 in complex with ligand P2C3U”. X-ray diffraction, 3 ligands (QVR, DXE, SO4), 12 pockets (best druggability 0.82). MolNFT v1 #125698 on GenesisL1: 3D…
- PDB
- 5LGS
- Type
- protein
- Length
- 1,406 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-arginine methyltransferase CARM1; Polyadenylate-binding protein 1
- EC
- 2.1.1.319
- UniProt
- Q9WVG6, P11940
- Ligands
- QVR, DXE, SO4
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 5 distinct chains · 30% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-arginine methyltransferase CARM1 (EC 2.1.1.319) | protein | 344 | 29% helix, 35% strand | Q9WVG6 |
| B, D | Histone-arginine methyltransferase CARM1 (EC 2.1.1.319) | protein | 343 | 31% helix, 36% strand | Q9WVG6 |
| C | Histone-arginine methyltransferase CARM1 (EC 2.1.1.319) | protein | 343 | 30% helix, 37% strand | Q9WVG6 |
| E, G, H | Polyadenylate-binding protein 1 | protein | 8 | 0% helix, 0% strand | P11940 |
| F | Polyadenylate-binding protein 1 | protein | 9 | 0% helix, 0% strand | P11940 |
Ligands and binding sites
- QVR · (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol · ligand · 4 copies · chains A, E, B, F, C, G, D, H
- DXE · 1,2-dimethoxyethane · ligand · 3 copies · chains A, B, D
- SO4 · Sulfate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains C, B, D
- PEG · Di(hydroxyethyl)ether · additive · chains A
- PG4 · Tetraethylene glycol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.82 | 0.98 | 35 | QVR |
| 2 | 128 | 0.80 | 0.98 | 33 | QVR |
| 3 | 129 | 0.80 | 0.98 | 31 | QVR |
| 4 | 127 | 0.80 | 0.98 | 31 | QVR |
| 5 | 1125 | 0.78 | 0.80 | 77 | empty |
Interfaces
10 interfaces between chains.
- C–D · 1929 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 1923 Ų buried · 26 hydrogen bonds · protein-protein
- B–D · 796 Ų buried · 9 hydrogen bonds · protein-protein
- B–F · 659 Ų buried · 10 hydrogen bonds · protein-protein
- D–H · 658 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent (covalent ligand).
Compared structures
- 5LGS · Crystal structure of mouse CARM1 in complex with ligand P2C3u · the same entry in another collection · chain H against H, TM-score 1.00
- Q9WVG6 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q9WVG6) · a predicted model of the same protein · chain A against A, TM-score 1.00
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
- Every structure of UniProt P11940
- Elsewhere: RCSB PDB 5LGS · PDBe 5LGS · UniProt Q9WVG6 · UniProt P11940
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