1GHM
Structures of the acyl-enzyme complex of the staphylococcus aureus beta-lactamase mutant GLU166ASP:ASN170GLN with degraded cephaloridine
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | BETA-LACTAMASE | polymer | 258 | 28974.4 | 1 | UniProt (P00807) Pfam (PF00144) Pfam (PF13354) In PDB | Staphylococcus aureus | PENICILLINASE |
2 | A | SULFATE ION | non-polymer | 96.1 | 5 | Chemie (SO4) | |||
3 | A | CARBONATE ION | non-polymer | 60.0 | 1 | Chemie (CO3) | |||
4 | A | 5-METHYL-2-[2-OXO-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-ETHYL]-3,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID | non-polymer | 340.4 | 1 | Chemie (CED) | |||
5 | water | water | 18.0 | 326 | Chemie (HOH) |
Sequence modifications
A: 31 - 290 (UniProt: P00807)
PDB | External Database | Details |
---|---|---|
Met 30 | - | SEE REMARK 999 |
Asp 166 | Glu 157 | engineered mutation |
Gln 170 | Asn 161 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 28974.4 | |
Non-Polymers* | Number of molecules | 7 |
Total formula weight | 880.7 | |
All* | Total formula weight | 29855.2 |