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3T2K

Crystal structure of sulfide:quinone oxidoreductase Cys128Ala variant from Acidithiobacillus ferrooxidans with bound trisulfane

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
AALA78
AALA104
ATHR105
AGLY106
APRO107
AILE127
ACYS160
APRO163
AVAL267
AGLY301
AGLY8
AILE302
ATHR321
AGLY322
AILE325
AVAL355
APHE357
ALYS391
AS3H503
AHOH504
AHOH512
AGLY10
AHOH556
AHOH560
AHOH593
AHOH605
AHOH634
AHOH662
AHOH664
ATHR11
AGLY12
ASER34
AALA35
AVAL42
ASER77

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE LMT A 501
ChainResidue
AGLY205
AASP206
AILE210
AGLU217
ACYS356
AALA358
AALA365
ATYR383
AHOH523
AHOH600

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AMET-2
AHIS3
AHIS97
AHOH583

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE S3H A 503
ChainResidue
ACYS160
ACYS356
AFAD500

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

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PDB entries from 2024-10-16

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