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

6OIC

Crystal structure of human Sulfide Quinone Oxidoreductase in complex with coenzyme Q (sulfite soaked)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
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
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 Residues36
Detailsbinding site for residue FAD A 501
ChainResidue
AGLY50
AVAL118
AALA144
ALEU145
AGLY146
AASN169
ATYR170
ACYS201
ALYS207
AVAL303
AGLY335
AGLY52
AASP336
ALYS344
ATHR345
AALA346
AALA347
AVAL349
APRO380
ALYS418
AUQ1503
AH2S505
ASER53
AHOH602
AHOH603
AHOH610
AHOH620
AHOH624
AHOH629
AHOH649
AGLY54
AGLU75
APRO76
AGLN83
APRO84
AARG117

site_idAC2
Number of Residues6
Detailsbinding site for residue UQ1 A 502
ChainResidue
AGLN247
AGLN251
ALEU255
ATHR256
AVAL257
ATYR259

site_idAC3
Number of Residues13
Detailsbinding site for residue UQ1 A 503
ChainResidue
ATYR82
AALA346
AALA347
ATYR376
ASER378
ALEU390
AGLU392
ATHR402
AMET422
AMET430
ATRP435
APRO438
AFAD501

site_idAC4
Number of Residues6
Detailsbinding site for residue UQ1 A 504
ChainResidue
ALYS371
ATYR434
ATRP435
AGLY436
AGLY437
APHE440

site_idAC5
Number of Residues4
Detailsbinding site for residue H2S A 505
ChainResidue
ACYS201
ATHR345
ACYS379
AFAD501

site_idAC6
Number of Residues32
Detailsbinding site for residue FAD B 501
ChainResidue
BGLY50
BGLY52
BSER53
BGLY54
BGLU75
BPRO76
BGLN83
BPRO84
BTHR87
BARG117
BVAL118
BALA144
BLEU145
BGLY146
BASN169
BTYR170
BCYS201
BLYS207
BVAL303
BGLY335
BASP336
BLYS344
BTHR345
BALA346
BALA347
BPRO380
BLYS418
BUQ1502
BH2S503
BHOH609
BHOH611
BHOH612

site_idAC7
Number of Residues14
Detailsbinding site for residue UQ1 B 502
ChainResidue
BALA347
BTYR376
BSER378
BPRO380
BLEU390
BGLU392
BTHR402
BMET422
BMET430
BTRP435
BPRO438
BFAD501
BTYR82
BALA346

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Cysteine persulfide intermediate => ECO:0000269|PubMed:30905673, ECO:0000303|PubMed:22852582
ChainResidueDetails
ACYS201
ACYS379
BCYS201
BCYS379

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:30905673
ChainResidueDetails
AASP336
ALYS344
BSER53
BGLU75
BGLN83
BVAL118
BASP336
BLYS344
ASER53
AGLU75
AGLN83
AVAL118

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9R112
ChainResidueDetails
ALYS173
BLYS173

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9R112
ChainResidueDetails
ASER343
BSER343

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon