9RT3
Structure of Choline O-acetyltransferase in complex with (E)-4-(2-((2-acetamidoethyl)thio)-2-(naphthalen-1-yl)vinyl)-1-methylpyridin-1-ium
This is a non-PDB format compatible entry.
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Choline O-acetyltransferase | polymer | 612 | 68113.4 | 1 | UniProt (P28329) Pfam (PF00755) | Homo sapiens (human) | Choline acetylase |
| 2 | B (A) | ~{N}-[2-[(~{E})-2-(1-methylpyridin-4-yl)-1-naphthalen-1-yl-ethenyl]sulfanylethyl]ethanamide | non-polymer | 363.5 | 1 | Chemie (A1JJI) | |||
| 3 | C, D (A) | 1,2-ETHANEDIOL | non-polymer | 62.1 | 2 | Chemie (EDO) | |||
| 4 | E (A) | DI(HYDROXYETHYL)ETHER | non-polymer | 106.1 | 1 | Chemie (PEG) PubChem (8117) | |||
| 5 | F (A) | SODIUM ION | non-polymer | 23.0 | 1 | Chemie (NA) PubChem (923) | |||
| 6 | G (A) | water | water | 18.0 | 462 | Chemie (HOH) |
Sequence modifications
A: 2 - 615 (UniProt: P28329)
| PDB | External Database | Details |
|---|---|---|
| Ala 1 | - | expression tag |
| Ala 225 | Glu 343 | engineered mutation |
| Ala 226 | Asp 344 | engineered mutation |
| Ala 227 | Glu 345 | engineered mutation |
| Met 343 | Val 461 | conflict |
| Pro 346 | Ser 464 | conflict |
| - | Ser 465 | deletion |
| - | Arg 466 | deletion |
| Glu 349 | Lys 467 | conflict |
| Val 351 | Ile 469 | conflict |
| Ser 353 | Ala 471 | conflict |
| Pro 354 | Asp 472 | conflict |
| Met 355 | Ser 473 | conflict |
| Pro 357 | Ser 475 | conflict |
| - | Glu 476 | deletion |
| Ala 518 | Lys 636 | engineered mutation |
| Ala 519 | Glu 637 | engineered mutation |
| Ala 582 | Lys 700 | engineered mutation |
| Ala 583 | Glu 701 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 68113.4 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 616.7 | |
| All* | Total formula weight | 68730.1 |
