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 |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0042597 | cellular_component | periplasmic space |
B | 0046677 | biological_process | response to antibiotic |
B | 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 301 |
Chain | Residue |
A | HIS77 |
A | HIS79 |
A | HIS139 |
A | 8YF311 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | ASP81 |
A | CYS158 |
A | HIS197 |
A | 8YF311 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | PRO135 |
A | GLY136 |
A | ILE182 |
A | HOH439 |
B | TRP28 |
B | 8YF307 |
A | TYR134 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | VAL64 |
A | GLU69 |
A | ILE70 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | TRP147 |
A | PRO149 |
A | LYS152 |
A | EDO306 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO A 306 |
Chain | Residue |
A | EDO305 |
A | HOH409 |
A | HOH443 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | GLY15 |
A | LEU39 |
A | LEU148 |
A | GLU150 |
A | SER151 |
A | HOH436 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO A 308 |
Chain | Residue |
A | ASN103 |
A | GLN113 |
A | ALA114 |
A | LYS115 |
A | SER117 |
A | HOH403 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue EDO A 309 |
Chain | Residue |
A | GLN141 |
A | ASP170 |
A | ALA171 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 310 |
Chain | Residue |
A | LEU7 |
A | LYS58 |
A | TRP62 |
A | HOH421 |
site_id | AD2 |
Number of Residues | 14 |
Details | binding site for residue 8YF A 311 |
Chain | Residue |
A | HIS77 |
A | HIS79 |
A | SER80 |
A | ASP81 |
A | HIS139 |
A | CYS158 |
A | LYS161 |
A | LEU165 |
A | GLY166 |
A | ASN167 |
A | HIS197 |
A | ZN301 |
A | ZN302 |
A | HOH497 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | HIS77 |
B | HIS79 |
B | HIS139 |
B | 8YF307 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 302 |
Chain | Residue |
B | ASP81 |
B | CYS158 |
B | HIS197 |
B | 8YF307 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
A | TRP28 |
B | VAL121 |
B | PHE133 |
B | TYR134 |
B | PRO135 |
B | GLY136 |
B | HOH414 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
A | SER99 |
A | HOH418 |
B | VAL30 |
B | THR32 |
B | HOH443 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | TYR116 |
B | SER117 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO B 306 |
Chain | Residue |
B | HIS34 |
B | GLU199 |
B | LYS200 |
site_id | AD9 |
Number of Residues | 23 |
Details | binding site for residue 8YF B 307 |
Chain | Residue |
B | GLY166 |
B | ASN167 |
B | HIS197 |
B | ZN301 |
B | ZN302 |
B | HOH407 |
B | HOH423 |
A | VAL121 |
A | EDO303 |
A | HOH402 |
B | VAL25 |
B | TRP28 |
B | VAL30 |
B | VAL31 |
B | THR32 |
B | HIS77 |
B | HIS79 |
B | SER80 |
B | ASP81 |
B | HIS139 |
B | CYS158 |
B | LYS161 |
B | LEU165 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IsSHfHSDstGGiewlnsq.S |
Chain | Residue | Details |
A | ILE74-SER93 | |
site_id | PS00744 |
Number of Residues | 13 |
Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PeskILfGgCFIK |
Chain | Residue | Details |
A | PRO149-LYS161 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS77 | |
B | HIS139 | |
B | CYS158 | |
B | HIS197 | |
A | HIS79 | |
A | ASP81 | |
A | HIS139 | |
A | CYS158 | |
A | HIS197 | |
B | HIS77 | |
B | HIS79 | |
B | ASP81 | |
Chain | Residue | Details |
A | LYS161 | |
B | LYS161 | |
Chain | Residue | Details |
A | ASN167 | |
B | ASN167 | |