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3T2Y

Crystal structure of sulfide:quinone oxidoreductase His132Ala variant from Acidithiobacillus ferrooxidans with bound disulfide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0019646biological_processaerobic electron transport chain
A0048038molecular_functionquinone binding
A0070224molecular_functionsulfide:quinone oxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
ALEU7
APRO43
ASER77
AALA78
AALA104
ATHR105
AGLY106
APRO107
ACYS160
APRO163
AGLY301
AGLY8
AILE302
ALYS320
ATHR321
AGLY322
AILE325
AVAL355
APHE357
AHOH520
AHOH522
AHOH525
AALA9
AGLY10
ATHR11
AGLY12
ASER34
AALA35
AVAL42

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE LMT A 501
ChainResidue
AMET169
AGLY205
AASP206
AILE210
ALEU211
ACYS356
AALA358
AALA365
ATYR383
AHOH539
AHOH548

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE H2S A 504
ChainResidue
ACYS160
AS2H505

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE S2H A 505
ChainResidue
AGLY162
ACYS356
AH2S504

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"20303979","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22542586","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20303979","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22542586","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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