2FY4
Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
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) | CHOACTase, Choline acetylase, ChAT |
| 2 | B (A) | COENZYME A | non-polymer | 767.5 | 1 | Chemie (COA) | |||
| 3 | C (A) | water | water | 18.0 | 447 | Chemie (HOH) |
Sequence modifications
A: 2 - 615 (UniProt: P28329)
| PDB | External Database | Details |
|---|---|---|
| Ala 1 | - | cloning artifact |
| Ala 225 | Glu 343 | engineered mutation |
| Ala 226 | Asp 344 | engineered mutation |
| Ala 227 | Glu 345 | engineered mutation |
| - | Ser 464 | SEE REMARK 999 |
| - | Ser 465 | SEE REMARK 999 |
| Pro 346 | Arg 466 | SEE REMARK 999 |
| Glu 349 | Lys 467 | SEE REMARK 999 |
| Val 351 | Ile 469 | SEE REMARK 999 |
| Ser 353 | Ala 471 | SEE REMARK 999 |
| Pro 354 | Asp 472 | SEE REMARK 999 |
| Met 355 | Ser 473 | SEE REMARK 999 |
| - | Ser 475 | SEE REMARK 999 |
| Pro 357 | Glu 476 | SEE REMARK 999 |
| 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 | 1 |
| Total formula weight | 767.5 | |
| All* | Total formula weight | 68880.9 |
