Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3SZF

Crystal structure of sulfide:quinone oxidoreductase H198A variant from Acidithiobacillus ferrooxidans in complex with bound trisulfide and decylubiquinone

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
ASER77
AALA78
AALA104
ATHR105
AGLY106
APRO107
AILE127
ACYS160
APRO163
AVAL267
AGLY8
AGLY301
AILE302
ALYS320
ATHR321
AGLY322
AILE325
AVAL355
APHE357
ADCQ502
AH2S503
AALA9
AS3H504
AH2S506
AHOH622
AHOH623
AHOH644
AHOH648
AHOH657
AHOH659
AHOH673
AHOH682
AGLY10
AHOH724
AHOH727
AHOH740
ATHR11
AGLY12
ASER34
AALA35
AVAL42

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE LMT A 501
ChainResidue
AASP206
AILE210
ALEU211
ACYS356
APHE357
AALA358
AALA365
APHE367
ATYR383
AHOH653
AHOH661
AHOH677
AHOH717
AHOH723
AHOH788
AHOH828
AHOH865

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE DCQ A 502
ChainResidue
APHE41
APRO43
AGLY322
ATYR323
AVAL355
APHE357
APHE394
ATYR411
ALYS417
AFAD500
AHOH761

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE H2S A 503
ChainResidue
ATHR321
AVAL355
ACYS356
AFAD500

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE S3H A 504
ChainResidue
ACYS160
APRO319
ACYS356
AFAD500
AH2S505

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE H2S A 505
ChainResidue
AGLY162
ACYS356
AS3H504
AHOH877

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE H2S A 506
ChainResidue
ACYS160
AFAD500
AHOH701

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 508
ChainResidue
AMET-2
AHIS3
AHIS97
AHOH734

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

PDB statisticsPDBj update infoContact PDBjnumon