2HSE
Structure of D236A E. coli Aspartate Transcarbamoylase in the presence of phosphonoacetamide and l-Aspartate at 2.60 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 | Aspartate carbamoyltransferase catalytic chain | polymer | 310 | 34293.1 | 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 | A | PHOSPHATE ION | non-polymer | 95.0 | 1 | Chemie (PO4) | |||
| 4 | A, C | PHOSPHONOACETAMIDE | non-polymer | 139.0 | 2 | Chemie (PCT) | |||
| 5 | A, C | ASPARTIC ACID | non-polymer | 133.1 | 3 | Chemie (ASP) | |||
| 6 | B, D | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 7 | water | water | 18.0 | 349 | Chemie (HOH) |
Sequence modifications
A, C: 1 - 310 (UniProt: P0A786)
B, D: 2 - 153 (UniProt: P0A7F3)
| PDB | External Database | Details |
|---|---|---|
| Ala 236 | Asp 236 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Met 1 | - | initiating methionine |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 102873.4 | |
| Non-Polymers* | Number of molecules | 8 |
| Total formula weight | 903.2 | |
| All* | Total formula weight | 103776.6 |
