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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | HIS77 |
A | HIS79 |
A | HIS139 |
A | CSD158 |
A | ACY401 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 302 |
Chain | Residue |
B | ACY402 |
B | HIS77 |
B | HIS79 |
B | HIS139 |
B | CSD158 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 303 |
Chain | Residue |
C | HIS77 |
C | HIS79 |
C | HIS139 |
C | CSD158 |
C | ACY403 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 304 |
Chain | Residue |
D | HIS77 |
D | HIS79 |
D | HIS139 |
D | CSD158 |
D | ACY404 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACY A 401 |
Chain | Residue |
A | HIS77 |
A | HIS79 |
A | ALA81 |
A | HIS139 |
A | CSD158 |
A | ZN301 |
A | HOH438 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY B 402 |
Chain | Residue |
B | HIS79 |
B | HIS139 |
B | CSD158 |
B | ZN302 |
B | HOH413 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACY C 403 |
Chain | Residue |
C | HIS77 |
C | HIS79 |
C | HIS139 |
C | CSD158 |
C | ZN303 |
C | HOH404 |
C | HOH445 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACY D 404 |
Chain | Residue |
D | HIS77 |
D | HIS79 |
D | ALA81 |
D | HIS139 |
D | CSD158 |
D | ZN304 |
D | HOH405 |
D | HOH406 |
Functional Information from PROSITE/UniProt
site_id | PS00744 |
Number of Residues | 13 |
Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PerkILfGgCFIK |
Chain | Residue | Details |
A | PRO149-LYS161 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS77 | |
B | ALA81 | |
B | HIS139 | |
B | CSD158 | |
B | LYS161 | |
B | HIS197 | |
C | HIS77 | |
C | HIS79 | |
C | ALA81 | |
C | HIS139 | |
C | CSD158 | |
A | HIS79 | |
C | LYS161 | |
C | HIS197 | |
D | HIS77 | |
D | HIS79 | |
D | ALA81 | |
D | HIS139 | |
D | CSD158 | |
D | LYS161 | |
D | HIS197 | |
A | ALA81 | |
A | HIS139 | |
A | CSD158 | |
A | LYS161 | |
A | HIS197 | |
B | HIS77 | |
B | HIS79 | |
Chain | Residue | Details |
A | ASN167 | |
B | ASN167 | |
C | ASN167 | |
D | ASN167 | |