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 |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0042597 | cellular_component | periplasmic space |
B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 0NB A 401 |
Chain | Residue |
A | SER64 |
A | HOH788 |
A | TYR150 |
A | ASN152 |
A | VAL211 |
A | SER212 |
A | ALA318 |
A | GLY320 |
A | HOH785 |
A | HOH787 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 402 |
Chain | Residue |
A | PHE41 |
A | THR42 |
A | HOH577 |
A | HOH601 |
A | HOH759 |
A | HOH813 |
B | GLY116 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 403 |
Chain | Residue |
A | THR262 |
A | GLY263 |
A | PRO297 |
A | HOH606 |
B | TYR45 |
B | LYS51 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 404 |
Chain | Residue |
A | TRP93 |
A | LEU157 |
A | LYS164 |
A | HOH616 |
A | HOH682 |
A | HOH768 |
A | HOH797 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 405 |
Chain | Residue |
A | PRO140 |
A | ALA141 |
A | TRP142 |
A | ALA143 |
A | HOH771 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 0NB B 401 |
Chain | Residue |
A | LEU85 |
A | GLN250 |
A | LEU254 |
A | SER257 |
A | TYR259 |
A | PRO304 |
A | HOH534 |
B | GLN250 |
B | GLN253 |
B | LEU254 |
B | SER257 |
B | PRO303 |
B | PRO304 |
B | PRO306 |
B | HOH628 |
B | HOH641 |
B | HOH758 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 0NB B 402 |
Chain | Residue |
B | SER64 |
B | GLN120 |
B | TYR150 |
B | ASN152 |
B | VAL211 |
B | SER212 |
B | GLY317 |
B | ALA318 |
B | GLY320 |
B | HOH739 |
B | HOH741 |
B | HOH747 |
B | HOH755 |
B | HOH774 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 403 |
Chain | Residue |
A | ARG133 |
A | HIS186 |
A | HOH711 |
A | HOH743 |
A | HOH748 |
B | LYS290 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 B 404 |
Chain | Residue |
B | ARG80 |
B | HOH567 |
Functional Information from PROSITE/UniProt
site_id | PS00336 |
Number of Residues | 8 |
Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK |
Chain | Residue | Details |
A | PHE60-LYS67 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER64 | |
B | SER64 | |
Chain | Residue | Details |
A | SER64 | |
B | SER64 | |
Chain | Residue | Details |
A | GLN120 | |
B | GLN120 | |
Chain | Residue | Details |
A | TYR150 | |
B | TYR150 | |
Chain | Residue | Details |
A | ASN152 | |
A | ALA318 | |
B | ASN152 | |
B | ALA318 | |
Chain | Residue | Details |
A | ASN343 | |
B | ASN343 | |