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9UOK

Structure of the complex of LGR4_ECD with Norrin

Functional Information from GO Data
ChainGOidnamespacecontents
E0005109molecular_functionfrizzled binding
E0005125molecular_functioncytokine activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0007033biological_processvacuole organization
E0007399biological_processnervous system development
E0007601biological_processvisual perception
E0009986cellular_componentcell surface
E0016055biological_processWnt signaling pathway
E0035426biological_processextracellular matrix-cell signaling
E0042803molecular_functionprotein homodimerization activity
E0045893biological_processpositive regulation of DNA-templated transcription
E0045944biological_processpositive regulation of transcription by RNA polymerase II
E0046697biological_processdecidualization
E0110135biological_processNorrin signaling pathway
F0005109molecular_functionfrizzled binding
F0005125molecular_functioncytokine activity
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
F0007033biological_processvacuole organization
F0007399biological_processnervous system development
F0007601biological_processvisual perception
F0009986cellular_componentcell surface
F0016055biological_processWnt signaling pathway
F0035426biological_processextracellular matrix-cell signaling
F0042803molecular_functionprotein homodimerization activity
F0045893biological_processpositive regulation of DNA-templated transcription
F0045944biological_processpositive regulation of transcription by RNA polymerase II
F0046697biological_processdecidualization
F0110135biological_processNorrin signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues22
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cdc..CesfLltkpvsckHliks.H
ChainResidueDetails
CCYS858-HIS879

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FSCSVMH
ChainResidueDetails
EPHE363-HIS369

site_idPS01185
Number of Residues37
DetailsCTCK_1 C-terminal cystine knot signature. CCrpqtsklkalrlrCsgGmrltatyryilsChCee..C
ChainResidueDetails
ECYS95-CYS131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues23
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues21
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues21
DetailsRepeat: {"description":"LRR 8"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsRepeat: {"description":"LRR 9"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsRepeat: {"description":"LRR 10"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues21
DetailsRepeat: {"description":"LRR 11"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues21
DetailsRepeat: {"description":"LRR 12"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues21
DetailsRepeat: {"description":"LRR 13"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues21
DetailsRepeat: {"description":"LRR 14"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues21
DetailsRepeat: {"description":"LRR 15"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23756652","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues93
DetailsDomain: {"description":"CTCK","evidences":[{"source":"PROSITE-ProRule","id":"PRU00039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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