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3FN8

Crystal Structure of MerB complexed with mercury

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0018836molecular_functionalkylmercury lyase activity
A0046689biological_processresponse to mercury ion
B0016829molecular_functionlyase activity
B0018836molecular_functionalkylmercury lyase activity
B0046689biological_processresponse to mercury ion
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 221
ChainResidue
ACYS96
AASP99
ACYS159
AHOH263

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 222
ChainResidue
ATYR74
AGLY75
AASP99
AHOH263

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG B 221
ChainResidue
BASP99
BCYS159
BCYS96

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 222
ChainResidue
BASP99
BHOH389

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 297
ChainResidueDetails
ACYS96activator, covalently attached, hydrogen bond donor, nucleophile, proton donor
AASP99activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
ACYS159activator, covalently attached, nucleophile, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 297
ChainResidueDetails
BCYS96activator, covalently attached, hydrogen bond donor, nucleophile, proton donor
BASP99activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
BCYS159activator, covalently attached, nucleophile, proton donor

226707

PDB entries from 2024-10-30

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