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3SYI

Crystal structure of sulfide:quinone oxidoreductase Ser126Ala variant from Acidithiobacillus ferrooxidans using 7.0 keV diffraction data

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 Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
ALEU7
AVAL42
ASER77
AALA78
AALA104
ATHR105
AGLY106
APRO163
AVAL267
AGLY301
AILE302
AGLY8
ALYS320
ATHR321
AGLY322
AILE325
AVAL355
APHE357
ALYS391
AHOH509
AHOH510
AHOH536
AALA9
AHOH557
AHOH564
AHOH575
AGLY10
ATHR11
AGLY12
ASER34
AALA35
AASN36

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LMT A 501
ChainResidue
AMET169
AGLY205
AASP206
AILE210
AGLU217
ACYS356
AALA358
AMET360
AALA365
APHE367
ATYR383
AHOH538
AHOH547
AHOH569

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE H2S A 502
ChainResidue
ALEU109
AALA126
ACYS128
ATHR129
AHIS132

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE H2S A 503
ChainResidue
ALYS374
APRO375
AARG376

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
AMET-2
AHIS3
AHIS97
AASP99

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE H2S A 506
ChainResidue
ACYS160
AH2S507

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE H2S A 507
ChainResidue
AGLY162
AH2S506
AHOH580

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

218853

PDB entries from 2024-04-24

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