Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0042597 | cellular_component | periplasmic space |
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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | CO32 |
A | ASP120 |
A | ARG121 |
A | CYS221 |
A | HIS263 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CO3 A 2 |
Chain | Residue |
A | HIS263 |
A | ZN401 |
A | HOH403 |
A | HOH404 |
A | HOH410 |
A | ASP120 |
A | HIS196 |
A | CYS221 |
A | LYS224 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 3 |
Chain | Residue |
A | ARG143 |
A | ARG143 |
A | LYS147 |
A | LYS147 |
A | HOH560 |
A | HOH561 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 4 |
Chain | Residue |
A | ARG140 |
A | ARG140 |
A | HOH496 |
A | HOH601 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 5 |
Chain | Residue |
A | LYS97 |
A | ARG102 |
A | LYS257 |
A | HOH446 |
A | HOH451 |
A | HOH637 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 6 |
Chain | Residue |
A | HIS176 |
A | ASP177 |
A | GLY178 |
A | ASP179 |
A | HOH642 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 7 |
Chain | Residue |
A | LEU267 |
A | HIS289 |
A | GLY290 |
A | GLU292 |
A | HOH566 |
A | HOH645 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. InTNyHTDraGGnaywksi.G |
Chain | Residue | Details |
A | ILE113-GLY133 | |
site_id | PS00744 |
Number of Residues | 13 |
Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PdeqVLyGgCILK |
Chain | Residue | Details |
A | PRO209-LYS224 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP120 | |
A | CYS221 | |
A | HIS263 | |
Chain | Residue | Details |
A | THR157 | |
Chain | Residue | Details |
A | HIS196 | |
Chain | Residue | Details |
A | LYS224 | |
Chain | Residue | Details |
A | ASN233 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP120 | |
A | ASN233 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP120 | |