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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 251 |
Chain | Residue |
A | HIS82 |
A | HIS84 |
A | HIS145 |
A | ZN252 |
A | HOH256 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 252 |
Chain | Residue |
A | HOH256 |
A | HOH257 |
A | ASP86 |
A | CYS164 |
A | HIS206 |
A | ZN251 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 255 |
Chain | Residue |
A | ASN38 |
A | ASP52 |
A | ASP86 |
A | HOH258 |
A | HOH266 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 251 |
Chain | Residue |
B | HIS82 |
B | HIS84 |
B | HIS145 |
B | ZN252 |
B | HOH256 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 252 |
Chain | Residue |
B | ASP86 |
B | CYS164 |
B | HIS206 |
B | ZN251 |
B | HOH256 |
B | HOH257 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 255 |
Chain | Residue |
B | ASN38 |
B | ASP52 |
B | ASP86 |
B | HOH259 |
B | HOH263 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MES A 250 |
Chain | Residue |
A | TRP32 |
A | ASP86 |
A | HIS145 |
A | GLY175 |
A | ASN176 |
A | HIS206 |
A | HOH257 |
A | HOH329 |
B | ARG200 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MES B 250 |
Chain | Residue |
B | TRP32 |
B | ASP86 |
B | HIS145 |
B | GLY175 |
B | ASN176 |
B | HOH257 |
B | HOH282 |
B | HOH342 |
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 | ILE79-GLY98 | |
site_id | PS00744 |
Number of Residues | 13 |
Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PtenILfGgCMLK |
Chain | Residue | Details |
A | PRO155-LYS167 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS82 | |
A | HIS84 | |
A | HIS145 | |
B | HIS82 | |
B | HIS84 | |
B | HIS145 | |
Chain | Residue | Details |
A | ASP86 | |
A | CYS164 | |
A | HIS206 | |
B | ASP86 | |
B | CYS164 | |
B | HIS206 | |
Chain | Residue | Details |
A | LYS167 | |
B | LYS167 | |
Chain | Residue | Details |
A | ASN176 | |
B | ASN176 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP86 | |
A | ASN176 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
B | ASP86 | |
B | ASN176 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP86 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
B | ASP86 | |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 15 |
Chain | Residue | Details |
A | HIS82 | metal ligand |
A | HIS84 | metal ligand |
A | ASP86 | metal ligand |
A | HIS145 | metal ligand |
A | CYS164 | metal ligand |
A | LYS167 | electrostatic stabiliser, steric role |
A | ASN176 | electrostatic stabiliser, hydrogen bond donor |
A | HIS206 | metal ligand |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 15 |
Chain | Residue | Details |
B | HIS82 | metal ligand |
B | HIS84 | metal ligand |
B | ASP86 | metal ligand |
B | HIS145 | metal ligand |
B | CYS164 | metal ligand |
B | LYS167 | electrostatic stabiliser, steric role |
B | ASN176 | electrostatic stabiliser, hydrogen bond donor |
B | HIS206 | metal ligand |