Research workbench
Crystal structure of mouse CARM1 in complex with histone H3_13-22 K18 acetylated
Analyse Crystal structure of mouse CARM1 in complex with histone H3_13-22 K18 acetylated in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OKP
- Type
- protein
- Length
- 1,453 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9WVG6, P84243
- Ligands
- ACE, QVR
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 363 | — | Q9WVG6 |
| B, D | — | protein | 344 | — | Q9WVG6 |
| C | — | protein | 362 | — | Q9WVG6 |
| E, F, G, H | — | protein | 10 | — | P84243 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 4 copies · chains A, E, B, F, C, G, D, H
- 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
- MLI · Malonate ion · additive · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7OKP · Crystal structure of mouse CARM1 in complex with histone H3_13-22 K18 acetylated · 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 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
- Every structure of UniProt P84243
- Elsewhere: RCSB PDB 7OKP · PDBe 7OKP · UniProt Q9WVG6 · UniProt P84243
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