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7U8G

Cryo-EM structure of the core human NADPH oxidase NOX2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005635cellular_componentnuclear envelope
A0005737cellular_componentcytoplasm
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0006091biological_processgeneration of precursor metabolites and energy
A0006801biological_processsuperoxide metabolic process
A0006811biological_processmonoatomic ion transport
A0006952biological_processdefense response
A0006954biological_processinflammatory response
A0007584biological_processresponse to nutrient
A0008218biological_processbioluminescence
A0009055molecular_functionelectron transfer activity
A0009410biological_processresponse to xenobiotic stimulus
A0016174molecular_functionNAD(P)H oxidase H2O2-forming activity
A0016175molecular_functionsuperoxide-generating NAD(P)H oxidase activity
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0030171molecular_functionvoltage-gated proton channel activity
A0030425cellular_componentdendrite
A0030670cellular_componentphagocytic vesicle membrane
A0032760biological_processpositive regulation of tumor necrosis factor production
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0035579cellular_componentspecific granule membrane
A0042554biological_processsuperoxide anion generation
A0043020cellular_componentNADPH oxidase complex
A0043025cellular_componentneuronal cell body
A0045087biological_processinnate immune response
A0045335cellular_componentphagocytic vesicle
A0045471biological_processresponse to ethanol
A0045730biological_processrespiratory burst
A0045766biological_processpositive regulation of angiogenesis
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
A0070402molecular_functionNADPH binding
A0070821cellular_componenttertiary granule membrane
A0071276biological_processcellular response to cadmium ion
A0071361biological_processcellular response to ethanol
A0071456biological_processcellular response to hypoxia
A0071949molecular_functionFAD binding
A0097038cellular_componentperinuclear endoplasmic reticulum
A0097411biological_processhypoxia-inducible factor-1alpha signaling pathway
A0106292molecular_functionsuperoxide-generating NADPH oxidase activity
A1904044biological_processresponse to aldosterone
A1904845biological_processcellular response to L-glutamine
A1990776biological_processresponse to angiotensin
B0001666biological_processresponse to hypoxia
B0001725cellular_componentstress fiber
B0001938biological_processpositive regulation of endothelial cell proliferation
B0003106biological_processnegative regulation of glomerular filtration by angiotensin
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006801biological_processsuperoxide metabolic process
B0006954biological_processinflammatory response
B0009055molecular_functionelectron transfer activity
B0009410biological_processresponse to xenobiotic stimulus
B0014823biological_processresponse to activity
B0014895biological_processsmooth muscle hypertrophy
B0016020cellular_componentmembrane
B0016175molecular_functionsuperoxide-generating NAD(P)H oxidase activity
B0016324cellular_componentapical plasma membrane
B0016491molecular_functionoxidoreductase activity
B0017004biological_processcytochrome complex assembly
B0017124molecular_functionSH3 domain binding
B0020037molecular_functionheme binding
B0030141cellular_componentsecretory granule
B0030307biological_processpositive regulation of cell growth
B0030425cellular_componentdendrite
B0030670cellular_componentphagocytic vesicle membrane
B0031667biological_processresponse to nutrient levels
B0032755biological_processpositive regulation of interleukin-6 production
B0032760biological_processpositive regulation of tumor necrosis factor production
B0032930biological_processpositive regulation of superoxide anion generation
B0034137biological_processpositive regulation of toll-like receptor 2 signaling pathway
B0035579cellular_componentspecific granule membrane
B0042554biological_processsuperoxide anion generation
B0043020cellular_componentNADPH oxidase complex
B0043025cellular_componentneuronal cell body
B0045087biological_processinnate immune response
B0045730biological_processrespiratory burst
B0045777biological_processpositive regulation of blood pressure
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B0048661biological_processpositive regulation of smooth muscle cell proliferation
B0050665biological_processhydrogen peroxide biosynthetic process
B0050766biological_processpositive regulation of phagocytosis
B0070555biological_processresponse to interleukin-1
B0070821cellular_componenttertiary granule membrane
B0071260biological_processcellular response to mechanical stimulus
B0071333biological_processcellular response to glucose stimulus
B0071356biological_processcellular response to tumor necrosis factor
B0071480biological_processcellular response to gamma radiation
B0097038cellular_componentperinuclear endoplasmic reticulum
B1900426biological_processpositive regulation of defense response to bacterium
B1903428biological_processpositive regulation of reactive oxygen species biosynthetic process
B1904044biological_processresponse to aldosterone
B1904385biological_processcellular response to angiotensin
B1904628biological_processcellular response to phorbol 13-acetate 12-myristate
B1904845biological_processcellular response to L-glutamine
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
ETYR195-HIS201
DTYR202-HIS208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues226
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"36241643","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7U8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GZ3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues85
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38355798","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GZ3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GZ3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38355798","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GZ3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38355798","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GZ3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q61093","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues5
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"36241643","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"36241643","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"36413210","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues10
DetailsIntramembrane: {"evidences":[{"source":"PubMed","id":"36241643","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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