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3SZC

Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans in complex with gold (I) cyanide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0048038molecular_functionquinone binding
A0070224molecular_functionsulfide:quinone oxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
ALEU7
AVAL42
ASER77
AALA78
AALA104
ATHR105
AGLY106
APRO107
AILE127
APRO163
AVAL267
AGLY8
AGLY301
AILE302
ALYS320
ATHR321
AGLY322
AVAL355
ACYS356
APHE357
ALYS391
ADCQ502
AALA9
AAU503
AH2S508
AHOH510
AHOH514
AHOH523
AHOH527
AHOH529
AGLY10
ATHR11
AGLY12
ASER34
AALA35
AASN36

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE DCQ A 502
ChainResidue
ATHR11
APRO43
AGLY322
ATYR323
APHE357
ALYS391
APHE394
ATYR411
ALYS413
ALYS417
AFAD500

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE AU A 503
ChainResidue
ACYS128
AFAD500

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AU A 504
ChainResidue
ACYS160
ALYS320
AAU505
AH2S509

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AU A 505
ChainResidue
ACYS160
AAU504
AH2S506
AH2S508

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE H2S A 506
ChainResidue
AGLY162
ACYS356
AAU505
AH2S508

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 507
ChainResidue
AMET-2
AHIS3
AHIS97

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE H2S A 508
ChainResidue
ACYS356
AFAD500
AAU505
AH2S506

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE H2S A 509
ChainResidue
ASER159
APHE264
ALYS320
AAU504
AHOH513

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Cysteine persulfide intermediate => ECO:0000269|PubMed:20303979, ECO:0000269|PubMed:22542586
ChainResidueDetails
ACYS160
ACYS356

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20303979, ECO:0000269|PubMed:22542586
ChainResidueDetails
AGLY8
ASER34
ASER77
AILE302
AGLY322
ALYS391

226707

PDB entries from 2024-10-30

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