Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
A | 0046677 | biological_process | response to antibiotic |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE 2UL A 301 |
Chain | Residue |
A | MET68 |
A | LYS233 |
A | SER234 |
A | GLY235 |
A | ALA236 |
A | SER237 |
A | GLU238 |
A | ARG242 |
A | HOH524 |
A | HOH602 |
A | HOH670 |
A | SER69 |
A | GLU103 |
A | TYR104 |
A | SER129 |
A | ASN131 |
A | HIS157 |
A | GLU165 |
A | ASN169 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 302 |
Chain | Residue |
A | GLU36 |
A | GLU36 |
A | HOH404 |
A | HOH404 |
A | HOH405 |
A | HOH405 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 303 |
Chain | Residue |
A | ALA85 |
A | LYS110 |
A | HIS111 |
A | LEU112 |
A | THR113 |
A | ASP114 |
A | HOH681 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | ASP100 |
A | ASN135 |
A | LEU136 |
A | THR139 |
A | HOH418 |
A | HOH610 |
Functional Information from PROSITE/UniProt
site_id | PS00146 |
Number of Residues | 16 |
Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL |
Chain | Residue | Details |
A | PHE65-LEU80 | |