4ECA
ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B, C, D (A, B, C, D) | L-ASPARAGINE AMIDOHYDROLASE | polymer | 326 | 34739.9 | 4 | UniProt (P00805) Pfam (PF00710) Pfam (PF17763) | Escherichia coli | ASPARAGINASE |
2 | E, F, G, H (A, B, C, D) | water | water | 18.0 | 720 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 1 - 326 (UniProt: P00805)
PDB | External Database | Details |
---|---|---|
Aei 12 | Thr 34 | modified residue |
Val 89 | Thr 111 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 4 |
Total formula weight | 138959.7 | |
All* | Total formula weight | 138959.7 |