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 | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 1 |
Chain | Residue |
A | HOH107 |
A | HIS118 |
A | ASP120 |
A | HIS196 |
A | HIS263 |
A | ZN308 |
A | ZN309 |
A | HOH334 |
A | HOH474 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 2 |
Chain | Residue |
A | HIS176 |
A | ASP177 |
A | HOH465 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 3 |
Chain | Residue |
A | ALA237 |
A | ASP238 |
A | VAL239 |
A | LYS240 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 4 |
Chain | Residue |
A | SER104 |
A | LYS106 |
A | HOH348 |
A | HOH466 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CO3 A 5 |
Chain | Residue |
A | LEU249 |
A | LYS250 |
A | LYS253 |
A | LEU254 |
A | ILE256 |
A | HOH365 |
A | HOH421 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO3 A 6 |
Chain | Residue |
A | ARG158 |
A | ASP166 |
A | HOH449 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 7 |
Chain | Residue |
A | HOH19 |
A | ASN116 |
A | ASN220 |
A | CYS221 |
A | ILE222 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 9 |
Chain | Residue |
A | GLN47 |
A | HOH393 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 10 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 11 |
Chain | Residue |
A | CL10 |
A | HIS289 |
A | LEU293 |
A | ZN310 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 12 |
Chain | Residue |
A | HIS289 |
A | GLY290 |
A | ZN310 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 308 |
Chain | Residue |
A | SO41 |
A | ASP120 |
A | CYS221 |
A | HIS263 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 309 |
Chain | Residue |
A | SO41 |
A | HIS118 |
A | HIS196 |
A | HOH474 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 310 |
Chain | Residue |
A | CL10 |
A | CL11 |
A | CL12 |
A | HIS289 |
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. PdeqVLyGnCILK |
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 | |