1RAE
CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, C | Aspartate carbamoyltransferase catalytic chain | polymer | 310 | 34337.1 | 2 | UniProt (P0A786) Pfam (PF02729) Pfam (PF00185) In PDB | Escherichia coli | Aspartate transcarbamylase, ATCase |
| 2 | B, D | Aspartate carbamoyltransferase regulatory chain | polymer | 153 | 17143.6 | 2 | UniProt (P0A7F3) Pfam (PF01948) Pfam (PF02748) In PDB | Escherichia coli | |
| 3 | B, D | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 4 | B, D | CYTIDINE-5'-TRIPHOSPHATE | non-polymer | 483.2 | 2 | Chemie (CTP) | |||
| 5 | water | water | 18.0 | 93 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 102961.5 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 1097.1 | |
| All* | Total formula weight | 104058.6 |
