Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | SER70 |
| A | TYR105 |
| A | SER130 |
| A | HOH672 |
| A | HOH692 |
| A | HOH749 |
| A | HOH910 |
| A | HOH931 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1 |
| Chain | Residue |
| B | SER70 |
| B | SER130 |
| B | ASN132 |
| B | HOH698 |
| B | HOH711 |
| B | HOH960 |
| site_id | CTA |
| Number of Residues | 6 |
| Details | THE CATALYTIC SITE IS CENTERED AROUND SER 70 AT THE N-TERMINUS OF HELIX A2 AND IS PRESENTED HERE. STRAND 5 OF SHEET *S1* CONTAINS IMPORTANT RESIDUES LYS 234 AND THR 235. INVARIANT GLUTAMIC ACID 166 IS INVOLVED IN DEACYLATION (SEE ALSO THE E166A MUTANT STRUCTURE PRESENTED IN PROTEIN DATA BANK ENTRY 1MBL) |
| Chain | Residue |
| A | SER70 |
| A | LYS73 |
| A | SER130 |
| A | GLU166 |
| A | LYS234 |
| A | THR235 |
| site_id | CTB |
| Number of Residues | 6 |
| Details | THE CATALYTIC SITE IS CENTERED AROUND SER 70 AT THE N-TERMINUS OF HELIX A2 AND IS PRESENTED HERE. STRAND 5 OF SHEET *S1* CONTAINS IMPORTANT RESIDUES LYS 234 AND THR 235. INVARIANT GLUTAMIC ACID 166 IS INVOLVED IN DEACYLATION (SEE ALSO THE E166A MUTANT STRUCTURE PRESENTED IN PROTEIN DATA BANK ENTRY 1MBL) |
| Chain | Residue |
| B | GLU166 |
| B | LYS234 |
| B | THR235 |
| B | SER70 |
| B | LYS73 |
| B | SER130 |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FALDTGTNRTVA |
| Chain | Residue | Details |
| A | PHE47-ALA59 | |
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTiKaltVGVLL |
| Chain | Residue | Details |
| A | PHE66-LEU81 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-ester intermediate"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | GLU166 | |
| A | LYS73 | |
| A | SER130 | |
| A | SER70 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| B | GLU166 | |
| B | LYS73 | |
| B | SER130 | |
| B | SER70 | |
