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 | 0030655 | biological_process | beta-lactam 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 | 0030655 | biological_process | beta-lactam 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 | 0030655 | biological_process | beta-lactam 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 | 0030655 | biological_process | beta-lactam 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 | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 2001 |
Chain | Residue |
A | HIS121 |
A | HIS263 |
A | ZN2002 |
A | HOH2095 |
A | HOH2096 |
A | HOH2108 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 2002 |
Chain | Residue |
A | ZN2001 |
A | HOH2095 |
A | HIS116 |
A | HIS118 |
A | HIS196 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 2001 |
Chain | Residue |
B | HIS121 |
B | HIS263 |
B | HOH2084 |
B | HOH2085 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 2002 |
Chain | Residue |
B | HIS116 |
B | HIS118 |
B | HIS196 |
B | HOH2084 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 2001 |
Chain | Residue |
C | HIS121 |
C | HIS263 |
C | HOH2069 |
C | HOH2070 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 2002 |
Chain | Residue |
C | HIS116 |
C | HIS118 |
C | HIS196 |
C | HOH2069 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN D 2001 |
Chain | Residue |
D | HIS121 |
D | HIS263 |
D | HOH2093 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN D 2002 |
Chain | Residue |
D | HIS116 |
D | HIS118 |
D | HIS196 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS116 | |
B | HIS196 | |
C | HIS116 | |
C | HIS118 | |
C | ASN120 | |
C | HIS121 | |
C | HIS196 | |
D | HIS116 | |
D | HIS118 | |
D | ASN120 | |
D | HIS121 | |
A | HIS118 | |
D | HIS196 | |
A | ASN120 | |
A | HIS121 | |
A | HIS196 | |
B | HIS116 | |
B | HIS118 | |
B | ASN120 | |
B | HIS121 | |
Chain | Residue | Details |
A | ASP220 | |
B | ASP220 | |
C | ASP220 | |
D | ASP220 | |
Chain | Residue | Details |
A | HIS263 | |
B | HIS263 | |
C | HIS263 | |
D | HIS263 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
A | ASN120 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
B | ASN120 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
C | ASN120 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
D | ASN120 | |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
A | HIS116 | metal ligand |
A | HIS118 | metal ligand |
A | ASN120 | metal ligand |
A | HIS121 | metal ligand |
A | HIS196 | metal ligand |
A | TYR228 | electrostatic stabiliser, hydrogen bond donor |
A | HIS263 | metal ligand |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
B | HIS116 | metal ligand |
B | HIS118 | metal ligand |
B | ASN120 | metal ligand |
B | HIS121 | metal ligand |
B | HIS196 | metal ligand |
B | TYR228 | electrostatic stabiliser, hydrogen bond donor |
B | HIS263 | metal ligand |
site_id | MCSA3 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
C | HIS116 | metal ligand |
C | HIS118 | metal ligand |
C | ASN120 | metal ligand |
C | HIS121 | metal ligand |
C | HIS196 | metal ligand |
C | TYR228 | electrostatic stabiliser, hydrogen bond donor |
C | HIS263 | metal ligand |
site_id | MCSA4 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
D | HIS116 | metal ligand |
D | HIS118 | metal ligand |
D | ASN120 | metal ligand |
D | HIS121 | metal ligand |
D | HIS196 | metal ligand |
D | TYR228 | electrostatic stabiliser, hydrogen bond donor |
D | HIS263 | metal ligand |