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 | 8 |
Details | BINDING SITE FOR RESIDUE NZ9 A 401 |
Chain | Residue |
A | LEU254 |
A | SER257 |
A | PRO306 |
A | HOH686 |
B | GLN250 |
B | GLN253 |
B | LEU254 |
B | SER257 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NZ9 A 402 |
Chain | Residue |
A | PRO26 |
A | ILE48 |
A | TYR203 |
A | LYS342 |
A | HOH689 |
A | HOH830 |
A | LYS24 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE NZ9 A 403 |
Chain | Residue |
A | GLN261 |
A | THR262 |
A | GLY263 |
A | PRO297 |
A | VAL298 |
A | HOH733 |
A | HOH758 |
B | LYS50 |
B | LYS51 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NZ9 A 404 |
Chain | Residue |
A | SER64 |
A | GLN120 |
A | ASN152 |
A | LEU293 |
A | GLY317 |
A | ALA318 |
A | THR319 |
A | NZ9405 |
A | HOH675 |
A | HOH688 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NZ9 A 405 |
Chain | Residue |
A | GLN120 |
A | VAL211 |
A | SER212 |
A | GLY320 |
A | NZ9404 |
A | HOH552 |
A | HOH586 |
A | HOH698 |
A | HOH725 |
A | HOH880 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 406 |
Chain | Residue |
A | HIS13 |
A | PHE41 |
A | THR42 |
A | HOH655 |
A | HOH731 |
B | GLY116 |
B | HOH558 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NZ9 B 401 |
Chain | Residue |
B | SER64 |
B | LEU119 |
B | GLN120 |
B | ASN152 |
B | TYR221 |
B | LEU293 |
B | GLY317 |
B | ALA318 |
B | THR319 |
B | NZ9403 |
B | HOH669 |
B | HOH670 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE NZ9 B 402 |
Chain | Residue |
A | GLN250 |
A | HOH874 |
B | PRO240 |
B | LEU241 |
B | GLN253 |
B | GLN256 |
B | PRO306 |
B | ALA307 |
B | ARG309 |
B | PRO330 |
B | HOH681 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE NZ9 B 403 |
Chain | Residue |
B | VAL211 |
B | SER212 |
B | THR319 |
B | GLY320 |
B | NZ9401 |
B | HOH689 |
B | HOH699 |
B | HOH792 |
B | HOH812 |
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 | |