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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7Q21

III2-IV2 respiratory supercomplex from Corynebacterium glutamicum

Functional Information from GO Data
ChainGOidnamespacecontents
a0004497molecular_functionmonooxygenase activity
a0005886cellular_componentplasma membrane
a0016491molecular_functionoxidoreductase activity
a0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
a0022904biological_processrespiratory electron transport chain
a0046872molecular_functionmetal ion binding
a0051536molecular_functioniron-sulfur cluster binding
a0051537molecular_function2 iron, 2 sulfur cluster binding
A0004497molecular_functionmonooxygenase activity
A0005886cellular_componentplasma membrane
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0022904biological_processrespiratory electron transport chain
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
b0005886cellular_componentplasma membrane
b0008121molecular_functionquinol-cytochrome-c reductase activity
b0009055molecular_functionelectron transfer activity
b0016020cellular_componentmembrane
b0016491molecular_functionoxidoreductase activity
b0022904biological_processrespiratory electron transport chain
b0046872molecular_functionmetal ion binding
b1902600biological_processproton transmembrane transport
B0005886cellular_componentplasma membrane
B0008121molecular_functionquinol-cytochrome-c reductase activity
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0022904biological_processrespiratory electron transport chain
B0046872molecular_functionmetal ion binding
B1902600biological_processproton transmembrane transport
c0005506molecular_functioniron ion binding
c0005886cellular_componentplasma membrane
c0008121molecular_functionquinol-cytochrome-c reductase activity
c0009055molecular_functionelectron transfer activity
c0016020cellular_componentmembrane
c0020037molecular_functionheme binding
c0022904biological_processrespiratory electron transport chain
c0046872molecular_functionmetal ion binding
c1902600biological_processproton transmembrane transport
C0005506molecular_functioniron ion binding
C0005886cellular_componentplasma membrane
C0008121molecular_functionquinol-cytochrome-c reductase activity
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0020037molecular_functionheme binding
C0022904biological_processrespiratory electron transport chain
C0046872molecular_functionmetal ion binding
C1902600biological_processproton transmembrane transport
d0004129molecular_functioncytochrome-c oxidase activity
d0005886cellular_componentplasma membrane
d0006119biological_processoxidative phosphorylation
d0009060biological_processaerobic respiration
d0015990biological_processelectron transport coupled proton transport
d0016020cellular_componentmembrane
d0020037molecular_functionheme binding
d0022904biological_processrespiratory electron transport chain
d0046872molecular_functionmetal ion binding
D0004129molecular_functioncytochrome-c oxidase activity
D0005886cellular_componentplasma membrane
D0006119biological_processoxidative phosphorylation
D0009060biological_processaerobic respiration
D0015990biological_processelectron transport coupled proton transport
D0016020cellular_componentmembrane
D0020037molecular_functionheme binding
D0022904biological_processrespiratory electron transport chain
D0046872molecular_functionmetal ion binding
e0004129molecular_functioncytochrome-c oxidase activity
e0005886cellular_componentplasma membrane
e0009055molecular_functionelectron transfer activity
e0009060biological_processaerobic respiration
e0016020cellular_componentmembrane
e0019646biological_processaerobic electron transport chain
e0022904biological_processrespiratory electron transport chain
e1902600biological_processproton transmembrane transport
E0004129molecular_functioncytochrome-c oxidase activity
E0005886cellular_componentplasma membrane
E0009055molecular_functionelectron transfer activity
E0009060biological_processaerobic respiration
E0016020cellular_componentmembrane
E0019646biological_processaerobic electron transport chain
E0022904biological_processrespiratory electron transport chain
E1902600biological_processproton transmembrane transport
f0004129molecular_functioncytochrome-c oxidase activity
f0005886cellular_componentplasma membrane
f0016020cellular_componentmembrane
f0022900biological_processelectron transport chain
f1902600biological_processproton transmembrane transport
F0004129molecular_functioncytochrome-c oxidase activity
F0005886cellular_componentplasma membrane
F0016020cellular_componentmembrane
F0022900biological_processelectron transport chain
F1902600biological_processproton transmembrane transport
g0004129molecular_functioncytochrome-c oxidase activity
g0005507molecular_functioncopper ion binding
g0016020cellular_componentmembrane
g0022900biological_processelectron transport chain
G0004129molecular_functioncytochrome-c oxidase activity
G0005507molecular_functioncopper ion binding
G0016020cellular_componentmembrane
G0022900biological_processelectron transport chain
h0005886cellular_componentplasma membrane
H0005886cellular_componentplasma membrane
Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues100
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. medesvkslnlaarrgalvtvaaasalalascsagqitqtssqvaavdgnqagsandpvlvrdvtvhlttdgeagvkftainqdtshtshtl.......................ESVTVDGE
ChainResidueDetails
LMET-4-GLU95
site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyvlalpffgivseiipvfsrkpmfgyvglifatlsigalsmavwa..HH
ChainResidueDetails
DTRP261-HIS315
site_idPS00078
Number of Residues55
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VaHsfwvpeflfkrdayahpeanksqrvfqieeiteegafvgrCaemCgtyHamM
ChainResidueDetails
GVAL242-MET296
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues118
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues30
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues194
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11382224","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues360
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00968","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues8
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00968","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11382224","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues160
DetailsDomain: {"description":"Cytochrome c 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues156
DetailsDomain: {"description":"Cytochrome c 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"11382224","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11382224","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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