Rattus norvegicus
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | BENZAMIDINE × 6 water × 1 | Consistent with protein count |
| UniProt name | CARM1_RAT |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–480； UniProt 28–507 |
The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.
| Entry ID entry_id | 3b3j |
| Deposition date deposition_date | 2007-10-22 |
| Structure title title | The 2.55 A crystal structure of the apo catalytic domain of coactivator-associated arginine methyl transferase I(CARM1:28-507, residues 28-146 and 479-507 not ordered) |
| Keywords keywords | ;PROTEIN ARGININE METHYLTRANSFERASE 4, apo CATALYTIC DOMAIN, Chromatin regulator, mRNA processing, mRNA splicing, Nucleus, S-adenosyl-L-methionine, Transcription, Transcription regulation, TRANSFERASE ;; TRANSFERASE |
| Experimental Method method | X-RAY DIFFRACTION |
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
| Rg（Guinier） | 23.39 Å |
| Rg (electron density) | 22.45 Å |
| Total Rg | 23.34 Å |
| Atom count | 2718 |
| Residues | 332 |
| Excluded volume | 48697 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | 3b3jA01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 50 — Rossmann fold |
| Homologous superfamily homologous superfamily | 150 — Vaccinia Virus protein VP39 |
| Domain ID domain_id | 3b3jA02 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 70 — Distorted Sandwich |
| Topology topology | 160 — Hnrnp arginine n-methyltransferase1 |
| Homologous superfamily homologous superfamily | 11 — Hnrnp arginine n-methyltransferase1 |