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2GMJ

Structure of Porcine Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004174molecular_functionelectron-transferring-flavoprotein dehydrogenase activity
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006979biological_processresponse to oxidative stress
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0022900biological_processelectron transport chain
A0022904biological_processrespiratory electron transport chain
A0046872molecular_functionmetal ion binding
A0048039molecular_functionubiquinone binding
A0050660molecular_functionflavin adenine dinucleotide binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0004174molecular_functionelectron-transferring-flavoprotein dehydrogenase activity
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006979biological_processresponse to oxidative stress
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0022900biological_processelectron transport chain
B0022904biological_processrespiratory electron transport chain
B0046872molecular_functionmetal ion binding
B0048039molecular_functionubiquinone binding
B0050660molecular_functionflavin adenine dinucleotide binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 A 610
ChainResidue
ALEU504
ACYS528
APRO529
ACYS553
AVAL554
ACYS556
ALYS557
ACYS559
ATRP570

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD A 611
ChainResidue
AGLY42
AGLY44
APRO45
AALA46
AGLU71
ALYS72
AHIS79
ASER82
AGLY83
AALA84
ACYS85
AALA167
AALA212
AGLU213
AGLY214
AHIS218
APHE275
ALEU333
AGLY353
ACYS354
AILE364
ALYS365
AGLY366
ATHR367
AHOH706
AHOH719
AHOH801

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 B 612
ChainResidue
BLEU504
BCYS528
BPRO529
BVAL532
BCYS553
BVAL554
BCYS556
BLYS557
BCYS559

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FAD B 613
ChainResidue
BGLY42
BGLY44
BPRO45
BALA46
BGLU71
BLYS72
BHIS79
BSER82
BGLY83
BALA84
BCYS85
BALA167
BGLU213
BGLY214
BHIS218
BPHE275
BTYR277
BARG331
BLEU333
BGLY353
BCYS354
BILE364
BLYS365
BGLY366
BTHR367
BVAL572

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TBU A 621
ChainResidue
AILE364
AHOH788

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TBU A 622
ChainResidue
ATYR271
ATHR438
ATBU623

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TBU A 623
ChainResidue
ALEU131
ATBU622

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TBU A 624
ChainResidue
ALYS324
ALEU491

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE TBU B 625
ChainResidue
BTBU626

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TBU B 626
ChainResidue
BGLY273
BTBU625

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsINTRAMEM:
ChainResidueDetails
ALEU86-THR107
AASN405-SER424
BLEU86-THR107
BASN405-SER424

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17050691
ChainResidueDetails
ATHR52
AGLY282
AGLU283
BTHR52
BGLY282
BGLU283

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ALEU538
AASP563
AGLN566
AASN569
BLEU538
BASP563
BGLN566
BASN569

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7
ChainResidueDetails
AALA73
AVAL109
AARG200
AASN334
BALA73
BVAL109
BARG200
BASN334

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16134
ChainResidueDetails
ACYS528
BCYS528

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ATHR80
ACYS85

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BTHR80
BCYS85

site_idMCSA1
Number of Residues7
DetailsM-CSA 281
ChainResidueDetails
AGLU92electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AILE341activator, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
AALA377electrostatic stabiliser
ALEU538activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand
AASP563activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand
AGLN566activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, metal ligand
AASN569activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 281
ChainResidueDetails
BGLU92electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BILE341activator, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
BALA377electrostatic stabiliser
BLEU538activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand
BASP563activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand
BGLN566activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, metal ligand
BASN569activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand

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PDB entries from 2024-09-18

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