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6OIB

Crystal structure of human Sulfide Quinone Oxidoreductase in complex with coenzyme Q

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006790biological_processsulfur compound metabolic process
A0016491molecular_functionoxidoreductase activity
A0048038molecular_functionquinone binding
A0070221biological_processsulfide oxidation, using sulfide:quinone oxidoreductase
A0070224molecular_functionsulfide:quinone oxidoreductase activity
A0071949molecular_functionFAD binding
A0106436molecular_functionglutathione-dependent sulfide quinone oxidoreductase activity
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006790biological_processsulfur compound metabolic process
B0016491molecular_functionoxidoreductase activity
B0048038molecular_functionquinone binding
B0070221biological_processsulfide oxidation, using sulfide:quinone oxidoreductase
B0070224molecular_functionsulfide:quinone oxidoreductase activity
B0071949molecular_functionFAD binding
B0106436molecular_functionglutathione-dependent sulfide quinone oxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue GOL A 501
ChainResidue
AARG411
ALEU412
ASER413

site_idAC2
Number of Residues33
Detailsbinding site for residue FAD A 502
ChainResidue
APRO84
AARG117
AVAL118
AALA144
ALEU145
AGLY146
AASN169
ATYR170
ACYS201
ALYS207
AGLY335
AASP336
ALYS344
ATHR345
AALA346
AALA347
APRO380
ALYS418
AUQ1504
AH2S505
AHOH604
AHOH605
AHOH630
AHOH642
AHOH653
AHOH674
AHOH681
AGLY52
ASER53
AGLY54
AGLU75
APRO76
AGLN83

site_idAC3
Number of Residues5
Detailsbinding site for residue UQ1 A 503
ChainResidue
AGLN247
AGLN251
ALEU255
ATHR256
AVAL257

site_idAC4
Number of Residues10
Detailsbinding site for residue UQ1 A 504
ChainResidue
ATYR82
AALA347
ATYR376
ASER378
ALEU390
AGLU392
AMET422
AMET430
ATRP435
AFAD502

site_idAC5
Number of Residues4
Detailsbinding site for residue H2S A 505
ChainResidue
ACYS201
ALYS207
AFAD502
AH2S506

site_idAC6
Number of Residues3
Detailsbinding site for residue H2S A 506
ChainResidue
AGLY203
ACYS379
AH2S505

site_idAC7
Number of Residues12
Detailsbinding site for residue UQ1 B 501
ChainResidue
BTYR82
BALA346
BALA347
BTYR376
BSER378
BPRO380
BGLU392
BMET422
BMET430
BTRP435
BPRO438
BFAD502

site_idAC8
Number of Residues33
Detailsbinding site for residue FAD B 502
ChainResidue
BHOH615
BHOH624
BHOH628
BHOH647
BGLY50
BGLY52
BSER53
BGLY54
BGLU75
BPRO76
BGLN83
BPRO84
BTHR87
BARG117
BVAL118
BALA144
BLEU145
BGLY146
BASN169
BTYR170
BCYS201
BLYS207
BGLY335
BASP336
BLYS344
BTHR345
BALA346
BALA347
BPRO380
BLYS418
BUQ1501
BH2S503
BHOH612

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"30905673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22852582","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30905673","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9R112","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9R112","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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