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6WXR

CryoEM structure of mouse DUOX1-DUOXA1 complex in the absence of NADPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005509molecular_functioncalcium ion binding
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0008104biological_processintracellular protein localization
B0010729biological_processpositive regulation of hydrogen peroxide biosynthetic process
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0019899molecular_functionenzyme binding
B0031252cellular_componentcell leading edge
B0042743biological_processhydrogen peroxide metabolic process
B0043020cellular_componentNADPH oxidase complex
B0045666biological_processpositive regulation of neuron differentiation
B0050665biological_processhydrogen peroxide biosynthetic process
B0050727biological_processregulation of inflammatory response
B0072659biological_processprotein localization to plasma membrane
B2000379biological_processpositive regulation of reactive oxygen species metabolic process
B2000609biological_processregulation of thyroid hormone generation
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGNGYLSfrEF
ChainResidueDetails
AASP828-PHE840
AASP864-PHE876

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues234
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues174
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues140
DetailsDomain: {"description":"Ferric oxidoreductase","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9NRD9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WXV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32929281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WXU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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