Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
A | 0046872 | molecular_function | metal ion binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0042597 | cellular_component | periplasmic space |
B | 0046677 | biological_process | response to antibiotic |
B | 0046872 | molecular_function | metal ion binding |
C | 0008270 | molecular_function | zinc ion binding |
C | 0008800 | molecular_function | beta-lactamase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0017001 | biological_process | antibiotic catabolic process |
C | 0042597 | cellular_component | periplasmic space |
C | 0046677 | biological_process | response to antibiotic |
C | 0046872 | molecular_function | metal ion binding |
D | 0008270 | molecular_function | zinc ion binding |
D | 0008800 | molecular_function | beta-lactamase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0017001 | biological_process | antibiotic catabolic process |
D | 0042597 | cellular_component | periplasmic space |
D | 0046677 | biological_process | response to antibiotic |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | SER99 |
A | GLU100 |
A | LEU101 |
A | SER119 |
A | TYR134 |
A | LEU144 |
A | HOH455 |
A | HOH524 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue BME A 302 |
Chain | Residue |
A | PRO135 |
A | TYR134 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL A 303 |
Chain | Residue |
A | LEU39 |
A | VAL40 |
A | GLU150 |
A | SER151 |
A | HOH483 |
A | HOH512 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GLY A 304 |
Chain | Residue |
A | GLU10 |
A | HIS34 |
A | LYS200 |
A | HOH440 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GLY A 305 |
Chain | Residue |
A | GLU120 |
A | VAL121 |
A | SER122 |
A | HOH469 |
A | HOH516 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue BME A 306 |
Chain | Residue |
A | LYS58 |
A | GLY309 |
A | HOH450 |
D | HOH1218 |
D | HOH1250 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GLY A 307 |
Chain | Residue |
A | GLN141 |
A | ASP170 |
A | ALA171 |
A | HOH421 |
A | HOH447 |
A | HOH490 |
A | HOH547 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GLY A 308 |
Chain | Residue |
A | VAL25 |
A | ASN26 |
A | TRP28 |
A | GLY29 |
A | GLY311 |
D | GLY1104 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue GLY A 309 |
Chain | Residue |
A | TRP62 |
A | ARG66 |
A | BME306 |
A | HOH416 |
A | HOH487 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue BME A 310 |
Chain | Residue |
A | LYS108 |
A | HOH487 |
A | HOH532 |
A | HOH591 |
D | LYS107 |
D | GLY110 |
D | HOH1299 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue GLY A 311 |
Chain | Residue |
A | VAL25 |
A | ASN26 |
A | TRP28 |
A | GLY308 |
A | HOH518 |
A | HOH539 |
D | VAL31 |
D | HIS197 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue ZN A 312 |
Chain | Residue |
A | HIS77 |
A | HIS79 |
A | HIS139 |
A | ZN313 |
A | HOH562 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue ZN A 313 |
Chain | Residue |
A | ASP81 |
A | CYS158 |
A | HIS197 |
A | ZN312 |
A | HOH553 |
A | HOH562 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residue GOL B 301 |
Chain | Residue |
B | SER99 |
B | GLU100 |
B | LEU101 |
B | SER119 |
B | TYR134 |
B | LEU144 |
B | HOH437 |
B | HOH471 |
B | HOH516 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue BME B 302 |
Chain | Residue |
B | PHE133 |
B | TYR134 |
B | PRO135 |
B | HOH415 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue ZN B 303 |
Chain | Residue |
B | HIS77 |
B | HIS79 |
B | HIS139 |
B | ZN304 |
C | HOH493 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue ZN B 304 |
Chain | Residue |
B | ASP81 |
B | CYS158 |
B | HIS197 |
B | ZN303 |
C | ASN26 |
C | HOH493 |
site_id | AD9 |
Number of Residues | 7 |
Details | binding site for residue PO4 B 305 |
Chain | Residue |
B | LEU39 |
B | VAL40 |
B | GLU150 |
B | HOH416 |
B | HOH417 |
B | HOH483 |
B | VAL38 |
site_id | AE1 |
Number of Residues | 9 |
Details | binding site for residue GOL C 301 |
Chain | Residue |
C | SER99 |
C | GLU100 |
C | LEU101 |
C | SER119 |
C | TYR134 |
C | LEU144 |
C | HOH442 |
C | HOH467 |
C | HOH500 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue GLY C 302 |
Chain | Residue |
C | LEU39 |
C | SER151 |
C | HOH430 |
C | HOH443 |
C | HOH537 |
site_id | AE3 |
Number of Residues | 2 |
Details | binding site for residue GLY C 303 |
Chain | Residue |
C | LYS200 |
C | HOH404 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue GLY C 304 |
Chain | Residue |
C | LEU7 |
C | ILE9 |
C | TRP62 |
C | HOH520 |
site_id | AE5 |
Number of Residues | 6 |
Details | binding site for residue GLY C 305 |
Chain | Residue |
B | LYS107 |
C | TRP210 |
C | GLU211 |
C | LEU214 |
C | HOH401 |
C | HOH471 |
site_id | AE6 |
Number of Residues | 10 |
Details | binding site for residue BME C 306 |
Chain | Residue |
B | HOH442 |
C | HIS79 |
C | ASP81 |
C | HIS139 |
C | ASN167 |
C | ZN307 |
C | ZN308 |
C | HOH503 |
C | HOH507 |
C | HOH559 |
site_id | AE7 |
Number of Residues | 6 |
Details | binding site for residue ZN C 307 |
Chain | Residue |
C | HIS77 |
C | HIS79 |
C | HIS139 |
C | BME306 |
C | ZN308 |
C | HOH507 |
site_id | AE8 |
Number of Residues | 6 |
Details | binding site for residue ZN C 308 |
Chain | Residue |
C | ASP81 |
C | CYS158 |
C | HIS197 |
C | BME306 |
C | ZN307 |
C | HOH507 |
site_id | AE9 |
Number of Residues | 8 |
Details | binding site for residue GLY D 1101 |
Chain | Residue |
A | VAL31 |
A | HIS197 |
D | VAL25 |
D | ASN26 |
D | HOH1239 |
D | HOH1249 |
D | HOH1276 |
D | HOH1293 |
site_id | AF1 |
Number of Residues | 8 |
Details | binding site for residue GOL D 1102 |
Chain | Residue |
D | GLU100 |
D | LEU101 |
D | SER119 |
D | TYR134 |
D | LEU144 |
D | HOH1259 |
D | HOH1280 |
D | HOH1314 |
site_id | AF2 |
Number of Residues | 8 |
Details | binding site for residue GOL D 1103 |
Chain | Residue |
D | GLU14 |
D | LEU39 |
D | LEU148 |
D | GLU150 |
D | SER151 |
D | HOH1215 |
D | HOH1282 |
D | HOH1351 |
site_id | AF3 |
Number of Residues | 3 |
Details | binding site for residue GLY D 1104 |
Chain | Residue |
A | VAL30 |
A | GLY308 |
D | VAL30 |
site_id | AF4 |
Number of Residues | 3 |
Details | binding site for residue BME D 1105 |
Chain | Residue |
D | TYR134 |
D | HOH1234 |
D | HOH1424 |
site_id | AF5 |
Number of Residues | 2 |
Details | binding site for residue GLY D 1106 |
Chain | Residue |
D | HOH1279 |
D | HOH1288 |
site_id | AF6 |
Number of Residues | 5 |
Details | binding site for residue ZN D 1107 |
Chain | Residue |
D | HIS77 |
D | HIS79 |
D | HIS139 |
D | ZN1108 |
D | HOH1341 |
site_id | AF7 |
Number of Residues | 6 |
Details | binding site for residue ZN D 1108 |
Chain | Residue |
A | HOH518 |
D | ASP81 |
D | CYS158 |
D | HIS197 |
D | ZN1107 |
D | HOH1341 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IsSHfHSDstGGiewlnsq.S |
Chain | Residue | Details |
A | ILE74-SER93 | |
site_id | PS00744 |
Number of Residues | 13 |
Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PeskILfGgCFIK |
Chain | Residue | Details |
A | PRO149-LYS161 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS77 | |
B | HIS139 | |
B | CYS158 | |
B | HIS197 | |
C | HIS77 | |
C | HIS79 | |
C | ASP81 | |
C | HIS139 | |
C | CYS158 | |
C | HIS197 | |
D | HIS77 | |
A | HIS79 | |
D | HIS79 | |
D | ASP81 | |
D | HIS139 | |
D | CYS158 | |
D | HIS197 | |
A | ASP81 | |
A | HIS139 | |
A | CYS158 | |
A | HIS197 | |
B | HIS77 | |
B | HIS79 | |
B | ASP81 | |
Chain | Residue | Details |
A | LYS161 | |
B | LYS161 | |
C | LYS161 | |
D | LYS161 | |
Chain | Residue | Details |
A | ASN167 | |
B | ASN167 | |
C | ASN167 | |
D | ASN167 | |