Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 1 |
Chain | Residue |
A | HIS99 |
A | HIS101 |
A | HIS162 |
A | HOH250 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD A 2 |
Chain | Residue |
A | ASP103 |
A | CYS181 |
A | HIS223 |
A | HOH250 |
A | HOH251 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 3 |
Chain | Residue |
A | ASN55 |
A | ASP69 |
A | ASP103 |
A | HOH255 |
A | HOH261 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 1 |
Chain | Residue |
B | HIS99 |
B | HIS101 |
B | HIS162 |
B | HOH250 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD B 2 |
Chain | Residue |
B | ASP103 |
B | CYS181 |
B | HIS223 |
B | HOH250 |
B | HOH251 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 3 |
Chain | Residue |
B | ASN55 |
B | ASP69 |
B | ASP103 |
B | HOH267 |
B | HOH300 |
site_id | CD1 |
Number of Residues | 4 |
Details | THE CADMIUM IS LOCATED IN THE SAME POSITION AS THE ZINC IN THE NATIVE STRUCTURE. |
Chain | Residue |
A | HIS99 |
A | HIS101 |
A | HIS162 |
A | HOH250 |
site_id | CD2 |
Number of Residues | 5 |
Details | THE CADMIUM IS LOCATED IN THE SAME POSITION AS THE ZINC IN THE NATIVE STRUCTURE. |
Chain | Residue |
A | ASP103 |
A | CYS181 |
A | HIS223 |
A | HOH250 |
A | HOH251 |
site_id | NA |
Number of Residues | 5 |
Details | DEDUCED FROM THE COORDINATION. SODIUM WAS PRESENT IN THE CRYSTALLIZATION SOLUTION. |
Chain | Residue |
A | ASN55 |
A | ASP69 |
A | ASP103 |
A | HOH255 |
A | HOH261 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IpNHwHGDciGGlgylqkk.G |
Chain | Residue | Details |
A | ILE96-GLY115 | |
site_id | PS00744 |
Number of Residues | 13 |
Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PtenILfGgCMLK |
Chain | Residue | Details |
A | PRO172-LYS184 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS99 | |
A | HIS101 | |
A | HIS162 | |
B | HIS99 | |
B | HIS101 | |
B | HIS162 | |
Chain | Residue | Details |
A | ASP103 | |
A | CYS181 | |
A | HIS223 | |
B | ASP103 | |
B | CYS181 | |
B | HIS223 | |
Chain | Residue | Details |
A | LYS184 | |
B | LYS184 | |
Chain | Residue | Details |
A | ASN193 | |
B | ASN193 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP103 | |
A | ASN193 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
B | ASP103 | |
B | ASN193 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP103 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
B | ASP103 | |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 15 |
Chain | Residue | Details |
A | HIS99 | metal ligand |
A | HIS101 | metal ligand |
A | ASP103 | metal ligand |
A | HIS162 | metal ligand |
A | CYS181 | metal ligand |
A | LYS184 | electrostatic stabiliser, steric role |
A | ASN193 | electrostatic stabiliser, hydrogen bond donor |
A | HIS223 | metal ligand |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 15 |
Chain | Residue | Details |
B | HIS99 | metal ligand |
B | HIS101 | metal ligand |
B | ASP103 | metal ligand |
B | HIS162 | metal ligand |
B | CYS181 | metal ligand |
B | LYS184 | electrostatic stabiliser, steric role |
B | ASN193 | electrostatic stabiliser, hydrogen bond donor |
B | HIS223 | metal ligand |