2AIR
T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme
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, G) | Aspartate carbamoyltransferase catalytic chain | polymer | 310 | 34337.1 | 2 | UniProt (P0A786) Pfam (PF02729) Pfam (PF00185) | Escherichia coli | Aspartate transcarbamylase, ATCase |
| 2 | B, D (B, H) | Aspartate carbamoyltransferase regulatory chain | polymer | 153 | 17143.6 | 2 | UniProt (P0A7F3) Pfam (PF01948) Pfam (PF02748) | Escherichia coli | |
| 3 | E, H (A, G) | PHOSPHORIC ACID MONO(FORMAMIDE)ESTER | non-polymer | 141.0 | 2 | Chemie (CP) | |||
| 4 | F, I (A, G) | 3-[HYDROXY(NITROSO)AMINO]-L-ALANINE | non-polymer | 149.1 | 2 | Chemie (AL0) | |||
| 5 | G, J (B, H) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 6 | K, L, M, N (A, B, G, H) | water | water | 18.0 | 606 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 102961.5 | |
| Non-Polymers* | Number of molecules | 6 |
| Total formula weight | 711.1 | |
| All* | Total formula weight | 103672.5 |
