Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue QFP A 401 |
Chain | Residue |
A | SER90 |
A | TYR177 |
A | TYR249 |
A | LYS342 |
A | THR343 |
A | GLY344 |
A | SER345 |
A | HOH592 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CL A 402 |
Chain | Residue |
A | PHE147 |
A | ASN179 |
A | GLN146 |
Functional Information from PROSITE/UniProt
site_id | PS00336 |
Number of Residues | 8 |
Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSVSK |
Chain | Residue | Details |
A | PHE86-LYS93 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER90 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | TYR177 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS342 | |