1T3M
Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, C | Putative L-asparaginase | polymer | 177 | 18882.6 | 2 | UniProt (P37595) Pfam (PF01112) In PDB | Escherichia coli | L-asparagine amidohydrolase |
| 2 | B, D | Putative L-asparaginase | polymer | 147 | 14895.6 | 2 | UniProt (P37595) Pfam (PF01112) In PDB | Escherichia coli | L-asparagine amidohydrolase |
| 3 | A, C | SODIUM ION | non-polymer | 23.0 | 2 | Chemie (NA) | |||
| 4 | A, B, C | NITRATE ION | non-polymer | 62.0 | 3 | Chemie (NO3) | |||
| 5 | water | water | 18.0 | 681 | Chemie (HOH) |
Sequence modifications
B, D: 178 - 320 (UniProt: P37595)
| PDB | External Database | Details |
|---|---|---|
| His 321 | - | cloning artifact |
| Ser 322 | - | cloning artifact |
| Ile 323 | - | cloning artifact |
| Glu 324 | - | cloning artifact |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 67556.4 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 232.0 | |
| All* | Total formula weight | 67788.4 |
