1ACM
ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY
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 | 34251.0 | 2 | UniProt (P0A786) Pfam (PF02729) Pfam (PF00185) | ||
| 2 | B, D (B, D) | ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN | polymer | 153 | 17072.5 | 2 | UniProt (P0A7F3) Pfam (PF01948) Pfam (PF02748) | ||
| 3 | E, G (A, C) | N-(PHOSPHONACETYL)-L-ASPARTIC ACID | non-polymer | 255.1 | 2 | Chemie (PAL) | |||
| 4 | F, H (B, D) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 5 | I, J (A, C) | water | water | 18.0 | 15 | Chemie (HOH) |
Sequence modifications
A, C: 1 - 310 (UniProt: P0A786)
B, D: 2 - 153 (UniProt: P0A7F3)
| PDB | External Database | Details |
|---|---|---|
| Ala 54 | Arg 54 | conflict |
| Gln 60 | Glu 60 | conflict |
| Gln 147 | Glu 147 | conflict |
| Glu 149 | Gln 149 | conflict |
| Glu 196 | Gln 196 | conflict |
| PDB | External Database | Details |
|---|---|---|
| Gly 8 | Gln 7 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 102647.1 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 641.1 | |
| All* | Total formula weight | 103288.1 |
