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5U83

Crystal structure of a MerB-trimethytin complex.

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 Residues3
Detailsbinding site for residue ZN8 A 301
ChainResidue
AASP99
APHE158
AHOH638

site_idAC2
Number of Residues7
Detailsbinding site for residue ACT A 302
ChainResidue
BHOH473
ACYS160
AHIS161
AHIS163
ATRP174
AHIS178
AHOH500

site_idAC3
Number of Residues2
Detailsbinding site for residue BR B 301
ChainResidue
ALYS2
BLYS2

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN8 B 302
ChainResidue
BGLY75
BTRP95
BASP99
BPHE158

site_idAC5
Number of Residues7
Detailsbinding site for residue ACT B 303
ChainResidue
BCYS160
BHIS161
BHIS163
BTRP174
BHOH419
BHOH432
BHOH472

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

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PDB entries from 2024-07-24

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