1I5Q
CRYSTAL STRUCTURE OF THE E. COLI AMPC BETA-LACTAMASE MUTANT N152A COVALENTLY ACYLATED WITH THE INHIBITORY BETA-LACTAM, MOXALACTAM
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | BETA-LACTAMASE | polymer | 358 | 39544.9 | 2 | UniProt (P00811) Pfam (PF00144) In PDB | Escherichia coli | CEPHALOSPORINASE |
2 | A, B | (2R)-2-[(1R)-1-{[(2S)-2-carboxy-2-(4-hydroxyphenyl)acetyl]amino}-1-methoxy-2-oxoethyl]-5-methylidene-5,6-dihydro-2H-1,3-oxazine-4-carboxylic acid | non-polymer | 406.3 | 2 | Chemie (MOX) | |||
3 | water | water | 18.0 | 394 | Chemie (HOH) |
Sequence modifications
A, B: 4 - 361 (UniProt: P00811)
PDB | External Database | Details |
---|---|---|
Ala 152 | Asn 168 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 79089.8 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 812.7 | |
All* | Total formula weight | 79902.5 |