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5C0U

Crystal structure of the copper-bound form of MerB mutant D99S

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 CU A 301
ChainResidue
ACYS96
ASER99
ACYS159
AHOH439

site_idAC2
Number of Residues3
Detailsbinding site for residue BR A 302
ChainResidue
ALYS2
APRO5
BPRO5

site_idAC3
Number of Residues4
Detailsbinding site for residue CU B 301
ChainResidue
BCYS159
BHOH524
BCYS96
BSER99

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 297
ChainResidueDetails
ACYS96activator, covalently attached, hydrogen bond donor, nucleophile, proton donor
ASER99activator, 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
BSER99activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
BCYS159activator, covalently attached, nucleophile, proton donor

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PDB entries from 2025-06-18

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