4E2F
Crystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate state
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | I, K, G, C, A... | Aspartate carbamoyltransferase catalytic chain | polymer | 310 | 34337.1 | 6 | UniProt (P0A786) Pfam (PF02729) Pfam (PF00185) In PDB | Escherichia coli | Aspartate transcarbamylase, ATCase |
2 | D, B, J, L, H... | Aspartate carbamoyltransferase regulatory chain | polymer | 153 | 17143.6 | 6 | UniProt (P0A7F3) Pfam (PF01948) Pfam (PF02748) In PDB | Escherichia coli | |
3 | D, B, J, L, H... | ZINC ION | non-polymer | 65.4 | 6 | Chemie (ZN) | |||
4 | water | water | 18.0 | 506 | Chemie (HOH) |
Sequence modifications
I, K, G, C, A, E: 1 - 310 (UniProt: P0A786)
PDB | External Database | Details |
---|---|---|
Glu 164 | Lys 165 | engineered mutation |
Lys 239 | Glu 240 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 12 |
Total formula weight | 308884.4 | |
Non-Polymers* | Number of molecules | 6 |
Total formula weight | 392.5 | |
All* | Total formula weight | 309276.8 |