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 PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 21 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG |
Chain | Residue | Details |
A | LEU81-GLY101 | |
B | LEU81-GLY101 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | HIS84 | |
B | HIS86 | |
B | ASP88 | |
B | HIS89 | |
B | HIS160 | |
Chain | Residue | Details |
B | ASP184 | |
Chain | Residue | Details |
B | HIS225 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
B | HIS84 | metal ligand |
B | HIS86 | metal ligand |
B | ASP88 | metal ligand |
B | HIS89 | metal ligand |
B | HIS160 | metal ligand |
B | TYR191 | electrostatic stabiliser, hydrogen bond donor |
B | HIS225 | metal ligand |