3F2H
Crystal structure of the mercury-bound form of MerB mutant C160S, the Organomercurial Lyase involved in a bacterial mercury resistance system
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016829 | molecular_function | lyase activity |
A | 0018836 | molecular_function | alkylmercury lyase activity |
A | 0046689 | biological_process | response to mercury ion |
B | 0016829 | molecular_function | lyase activity |
B | 0018836 | molecular_function | alkylmercury lyase activity |
B | 0046689 | biological_process | response to mercury ion |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE HG A 221 |
Chain | Residue |
A | CYS96 |
A | ASP99 |
A | CYS159 |
A | HOH252 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE HG B 221 |
Chain | Residue |
B | CYS96 |
B | ASP99 |
B | PHE158 |
B | CYS159 |
B | HOH358 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 297 |
Chain | Residue | Details |
A | CYS96 | activator, covalently attached, hydrogen bond donor, nucleophile, proton donor |
A | ASP99 | activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
A | CYS159 | activator, covalently attached, nucleophile, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 297 |
Chain | Residue | Details |
B | CYS96 | activator, covalently attached, hydrogen bond donor, nucleophile, proton donor |
B | ASP99 | activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
B | CYS159 | activator, covalently attached, nucleophile, proton donor |