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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 300 |
Chain | Residue |
A | HIS120 |
A | HIS122 |
A | HIS189 |
A | HOH401 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | CYS208 |
A | HIS250 |
A | HOH401 |
A | HOH410 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 300 |
Chain | Residue |
B | HIS122 |
B | HIS189 |
B | HOH401 |
B | HOH539 |
B | HIS120 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 301 |
Chain | Residue |
B | CYS208 |
B | HIS250 |
B | HOH401 |
B | HOH468 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 300 |
Chain | Residue |
C | HIS120 |
C | HIS122 |
C | HIS189 |
C | HOH401 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 301 |
Chain | Residue |
C | ASN124 |
C | CYS208 |
C | HIS250 |
C | HOH401 |
C | HOH518 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 300 |
Chain | Residue |
D | HIS120 |
D | HIS122 |
D | HIS189 |
D | HOH483 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 301 |
Chain | Residue |
D | CYS208 |
D | HIS250 |
D | HOH426 |
D | HOH483 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS120 | |
B | HIS189 | |
B | CYS208 | |
B | HIS250 | |
C | HIS120 | |
C | HIS122 | |
C | ASN124 | |
C | HIS189 | |
C | CYS208 | |
C | HIS250 | |
D | HIS120 | |
A | HIS122 | |
D | HIS122 | |
D | ASN124 | |
D | HIS189 | |
D | CYS208 | |
D | HIS250 | |
A | ASN124 | |
A | HIS189 | |
A | CYS208 | |
A | HIS250 | |
B | HIS120 | |
B | HIS122 | |
B | ASN124 | |
Chain | Residue | Details |
A | LYS211 | |
A | ASN220 | |
B | LYS211 | |
B | ASN220 | |
C | LYS211 | |
C | ASN220 | |
D | LYS211 | |
D | ASN220 | |