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2GMH

Structure of Porcine Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase in Complexed with Ubiquinone

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 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_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

218853

건을2024-04-24부터공개중

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