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 ZN A 301 |
Chain | Residue |
A | HIS99 |
A | HIS101 |
A | HIS162 |
A | ZN302 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 302 |
Chain | Residue |
A | ASP103 |
A | CYS181 |
A | HIS223 |
A | ZN301 |
A | 113602 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | HIS99 |
B | HIS101 |
B | HIS162 |
B | 113601 |
B | HOH616 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | ASP103 |
B | CYS181 |
B | HIS223 |
B | 113601 |
B | HOH616 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 501 |
Chain | Residue |
A | TYR40 |
A | ASN55 |
A | ASP69 |
A | THR70 |
A | ASP103 |
A | HOH616 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 502 |
Chain | Residue |
B | SER54 |
B | ASN55 |
B | THR70 |
B | ASP103 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 113 B 601 |
Chain | Residue |
B | HIS162 |
B | CYS181 |
B | LYS184 |
B | SER190 |
B | ASN193 |
B | HIS223 |
B | ZN401 |
B | ZN402 |
B | HOH616 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 113 A 602 |
Chain | Residue |
A | ILE46 |
A | HIS162 |
A | CYS181 |
A | LYS184 |
A | ASN193 |
A | HIS223 |
A | ZN302 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IpNHwHGDciGGlgylqrk.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 |