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 | 2 |
Details | BINDING SITE FOR RESIDUE AZI A1293 |
Chain | Residue |
A | ASN215 |
A | ASN255 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE AZI A1295 |
Chain | Residue |
A | LYS186 |
A | GLN210 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A1296 |
Chain | Residue |
A | HIS116 |
A | HIS118 |
A | HIS196 |
A | CSD221 |
A | HOH2110 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A1297 |
Chain | Residue |
A | LYS102 |
A | LYS280 |
B | LYS251 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A1298 |
Chain | Residue |
A | SER225 |
A | THR226 |
A | SER227 |
A | GLY264 |
A | GLU265 |
A | HOH2030 |
A | HOH2112 |
A | HOH2113 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A1299 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE AZI A1300 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B1293 |
Chain | Residue |
B | HIS116 |
B | HIS118 |
B | HIS196 |
B | CSD221 |
B | HOH2101 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B1294 |
Chain | Residue |
B | LYS181 |
B | LYS186 |
B | ARG252 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B1295 |
Chain | Residue |
B | SER225 |
B | THR226 |
B | SER227 |
B | GLU265 |
B | HOH2102 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A1294 |
Chain | Residue |
B | GLU97 |
B | ARG107 |
B | ARG131 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B1301 |
Chain | Residue |
B | GLU247 |
B | LEU287 |
B | HOH2103 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADciGGiktlker.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. PqynILvGgCLVK |
Chain | Residue | Details |
A | PRO209-LYS224 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS116 | |
A | HIS118 | |
A | HIS196 | |
B | HIS116 | |
B | HIS118 | |
B | HIS196 | |
Chain | Residue | Details |
A | ASP120 | |
A | CSD221 | |
A | HIS263 | |
B | ASP120 | |
B | CSD221 | |
B | HIS263 | |
Chain | Residue | Details |
A | LYS224 | |
B | LYS224 | |
Chain | Residue | Details |
A | ASN233 | |
B | 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 | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
B | ASP120 | |
B | ASN233 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP120 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
B | ASP120 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 16 |
Chain | Residue | Details |
A | HIS116 | metal ligand |
A | HIS118 | metal ligand |
A | ASP120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | HIS196 | metal ligand |
A | ASN233 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 16 |
Chain | Residue | Details |
B | HIS116 | metal ligand |
B | HIS118 | metal ligand |
B | ASP120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | HIS196 | metal ligand |
B | ASN233 | electrostatic stabiliser, hydrogen bond donor |