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3SZ0

Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans in complex with sodium selenide

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 Residues42
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
ALEU7
APRO43
ASER77
AALA78
AALA104
ATHR105
AGLY106
APRO107
AILE127
ACYS128
ACYS160
AGLY8
APRO163
AVAL267
AGLY301
AILE302
ATHR321
AGLY322
AILE325
AVAL355
APHE357
ALYS391
AALA9
A6SE503
ASE504
AHOH620
AHOH621
AHOH639
AHOH643
AHOH652
AHOH654
AHOH668
AHOH677
AGLY10
AHOH713
AHOH726
AHOH824
ATHR11
AGLY12
ASER34
AALA35
AVAL42

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LMT A 501
ChainResidue
AMET169
AGLY205
AASP206
ALEU211
AGLU217
ACYS356
AALA358
AMET360
AALA365
APHE367
ATYR383
AHOH648
AHOH672
AHOH796

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AMET-2
AHIS3
AHIS97
AHOH719

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 6SE A 503
ChainResidue
ACYS160
ACYS356
AFAD500

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SE A 504
ChainResidue
ATHR321
AVAL355
ACYS356
AFAD500

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SE A 505
ChainResidue
AGLY162
ACYS356
AHOH817

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

223790

PDB entries from 2024-08-14

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