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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | ASP120 |
A | CYS221 |
A | HIS263 |
A | IFS308 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE IFS A 308 |
Chain | Residue |
A | PHE156 |
A | THR157 |
A | LEU161 |
A | HIS196 |
A | ASN233 |
A | HIS263 |
A | HOH333 |
A | HOH435 |
A | ZN1 |
A | VAL67 |
A | THR119 |
A | ASP120 |
A | ILE153 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 309 |
Chain | Residue |
A | SER104 |
A | LYS106 |
A | HOH270 |
A | HOH332 |
A | HOH443 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 2 |
Chain | Residue |
A | ARG143 |
A | ARG143 |
A | LYS147 |
A | LYS147 |
A | HOH508 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 3 |
Chain | Residue |
A | HIS176 |
A | ASP177 |
A | GLY178 |
A | ASP179 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 4 |
Chain | Residue |
A | HIS289 |
A | GLY290 |
A | GLU292 |
A | HOH395 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 5 |
Chain | Residue |
A | LYS129 |
A | VAL170 |
A | LEU171 |
A | LYS302 |
A | HOH403 |
A | HOH432 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 6 |
Chain | Residue |
A | HOH19 |
A | LYS97 |
A | ARG102 |
A | LYS257 |
A | HOH324 |
A | HOH442 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 7 |
Chain | Residue |
A | ALA237 |
A | ASP238 |
A | VAL239 |
A | LYS240 |
A | GLN306 |
A | HOH337 |
A | HOH368 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 8 |
Chain | Residue |
A | LYS226 |
A | LEU231 |
A | GLY232 |
A | HOH400 |
A | HOH413 |
A | HOH500 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 9 |
Chain | Residue |
A | ARG140 |
A | ARG140 |
A | HOH287 |
A | HOH394 |
A | HOH394 |
A | HOH482 |
A | HOH482 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 10 |
Chain | Residue |
A | HOH66 |
A | ARG93 |
A | HOH208 |
A | HOH493 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 310 |
Chain | Residue |
A | THR181 |
A | ARG188 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 311 |
Chain | Residue |
A | HOH37 |
A | HOH61 |
A | LYS78 |
A | LEU182 |
A | GLN183 |
A | GLU184 |
A | HOH286 |
A | HOH357 |
A | HOH484 |
A | HOH505 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 312 |
Chain | Residue |
A | HOH40 |
A | ASP179 |
A | ARG188 |
A | PHE190 |
A | TYR204 |
A | MET252 |
A | HOH276 |
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 | |