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5UK5

Complex of Notch1(EGF8-12) bound to Jagged1(N-EGF3)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
B0005509molecular_functioncalcium ion binding
B0007154biological_processcell communication
B0007219biological_processNotch signaling pathway
B0007275biological_processmulticellular organism development
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CrCqyGwqGLyC
ChainResidueDetails
ACYS359-CYS370
ACYS321-CYS332
BCYS251-CYS262
BCYS282-CYS293
BCYS322-CYS333
ACYS398-CYS409
ACYS438-CYS449
ACYS476-CYS487

site_idPS01186
Number of Residues15
DetailsEGF_2 EGF-like domain signature 2. CrCqyGWqglycdk.C
ChainResidueDetails
ACYS398-CYS409
ACYS321-CYS332
BCYS251-CYS265
BCYS322-CYS333
ACYS438-CYS449
ACYS476-CYS487

site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNshggYnCvC
ChainResidueDetails
ACYS312-CYS323
ACYS350-CYS361
ACYS429-CYS440
ACYS467-CYS478

site_idPS01187
Number of Residues27
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvDECqlmpna........Cqnggt..ChNshggYnC
ChainResidueDetails
AASP295-CYS321
AASN335-CYS359
AASP412-CYS438
AASP452-CYS476

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASP452
AVAL453
AGLU455
AASP469
AGLN470
BASN143
BASN217

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Interaction with DLL4 => ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1
ChainResidueDetails
AASP469

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: O-linked (Fuc...) threonine => ECO:0000250|UniProtKB:Q01705
ChainResidueDetails
ATHR311
ATHR349

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q01705
ChainResidueDetails
ASER341
ASER378

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1
ChainResidueDetails
ASER435

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:25700513
ChainResidueDetails
ASER458

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) threonine => ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1
ChainResidueDetails
ATHR466

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PDB entries from 2024-05-15

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