1ZA2
Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, C (A, C) | Aspartate carbamoyltransferase catalytic chain | polymer | 310 | 34337.1 | 2 | UniProt (P00479) Pfam (PF02729) Pfam (PF00185) UniProt (by SIFTS) (P0A786) | Escherichia coli | Aspartate transcarbamylase, ATCase |
| 2 | B, D (B, D) | Aspartate carbamoyltransferase regulatory chain | polymer | 153 | 17143.6 | 2 | UniProt (P00478) Pfam (PF01948) Pfam (PF02748) UniProt (by SIFTS) (P0A7F3) | Escherichia coli | |
| 3 | E (A) | SODIUM ION | non-polymer | 23.0 | 1 | Chemie (NA) | |||
| 4 | F, G, J, K (A, C) | PHOSPHORIC ACID MONO(FORMAMIDE)ESTER | non-polymer | 141.0 | 4 | Chemie (CP) | |||
| 5 | H, L (B, D) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 6 | I, M (B, D) | CYTIDINE-5'-TRIPHOSPHATE | non-polymer | 483.2 | 2 | Chemie (CTP) | |||
| 7 | N, O, P, Q (A, B, C, D) | water | water | 18.0 | 381 | Chemie (HOH) |
Sequence modifications
B, D: 2 - 153 (UniProt: P00478)
| PDB | External Database | Details |
|---|---|---|
| Met 1 | - | initiating methionine |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 102961.5 | |
| Non-Polymers* | Number of molecules | 9 |
| Total formula weight | 1684.2 | |
| All* | Total formula weight | 104645.7 |
