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 | 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 | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue GOL A 401 |
Chain | Residue |
A | TRP93 |
A | LEU157 |
A | SER160 |
A | LYS164 |
A | HOH513 |
A | HOH563 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 402 |
Chain | Residue |
A | ALA308 |
A | GLU329 |
A | PRO305 |
A | VAL306 |
A | LYS307 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | GLN120 |
A | ASN152 |
A | TYR221 |
A | SER316 |
A | THR317 |
A | GLY318 |
A | SO4406 |
A | HOH556 |
A | HOH576 |
A | HOH671 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | GLN136 |
A | SER137 |
A | GLU241 |
A | THR242 |
A | GLN331 |
A | HOH509 |
A | HOH729 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue SO4 A 405 |
Chain | Residue |
A | SER64 |
A | TYR150 |
A | ASN289 |
A | LYS313 |
A | THR314 |
A | ASN344 |
A | HOH510 |
A | HOH533 |
A | HOH603 |
A | HOH662 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 406 |
Chain | Residue |
A | VAL211 |
A | SER212 |
A | THR317 |
A | GLY318 |
A | GOL403 |
A | HOH508 |
A | HOH587 |
A | HOH767 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 407 |
Chain | Residue |
A | SER4 |
A | GLU5 |
A | PRO122 |
A | ASP123 |
A | HOH519 |
A | HOH535 |
A | HOH666 |
A | HOH748 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 408 |
Chain | Residue |
A | PHE43 |
A | GLY44 |
A | HOH530 |
A | HOH633 |
A | HOH716 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 409 |
Chain | Residue |
A | LYS141 |
A | ALA292 |
A | LEU293 |
A | HOH503 |
A | HOH614 |
A | HOH657 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue GOL B 401 |
Chain | Residue |
A | ASP285 |
A | GLU349 |
B | GLN23 |
B | LYS340 |
B | PRO343 |
B | HOH612 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | TRP93 |
B | LEU131 |
B | SER160 |
B | LYS164 |
B | HOH509 |
B | HOH555 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | THR17 |
B | MET20 |
B | GLY44 |
B | SO4404 |
B | HOH569 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 404 |
Chain | Residue |
B | PHE43 |
B | GLY44 |
B | GOL403 |
B | HOH566 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 405 |
Chain | Residue |
B | ARG204 |
B | VAL211 |
B | SER212 |
B | THR317 |
B | GLY318 |
B | HOH502 |
B | HOH587 |
B | HOH675 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 406 |
Chain | Residue |
B | ASN185 |
B | HIS186 |
B | HOH539 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 407 |
Chain | Residue |
B | HIS193 |
B | HOH503 |
site_id | AD8 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 408 |
Chain | Residue |
B | SER4 |
B | GLU5 |
B | ASP123 |
B | HOH501 |
B | HOH514 |
B | HOH629 |
B | HOH646 |
B | HOH665 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue DIO B 409 |
Chain | Residue |
B | ASN237 |
B | PRO240 |
B | GLN256 |
B | LYS307 |
B | PRO328 |
B | HOH744 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue DIO B 410 |
Chain | Residue |
B | GLN250 |
B | PRO304 |
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 | |