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5KY8

mouse POFUT1 in complex with O-glucosylated mouse Notch1 EGF12 mutant (D464G) and GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001756biological_processsomitogenesis
A0005783cellular_componentendoplasmic reticulum
A0006004biological_processfucose metabolic process
A0006486biological_processprotein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0007219biological_processNotch signaling pathway
A0007399biological_processnervous system development
A0007507biological_processheart development
A0008417molecular_functionfucosyltransferase activity
A0008593biological_processregulation of Notch signaling pathway
A0016020cellular_componentmembrane
A0016757molecular_functionglycosyltransferase activity
A0036066biological_processprotein O-linked fucosylation
A0046922molecular_functionpeptide-O-fucosyltransferase activity
B0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ClDqigeFqCiC
ChainResidueDetails
BCYS467-CYS478

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CiCmpGyeGVyC
ChainResidueDetails
BCYS476-CYS487

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CiCmpGYegvy....C
ChainResidueDetails
BCYS476-CYS487

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvNECisnp..........Cqngat..ClDqigeFqC
ChainResidueDetails
BASP452-CYS476

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q07008
ChainResidueDetails
BASP452
BVAL453
BGLU455
BASP469
BGLN470
BASN490
BTHR491

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Interaction with DLL4 => ECO:0000250|UniProtKB:Q07008
ChainResidueDetails
BASP469
AASN165

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:21757702, ECO:0000269|PubMed:28089369
ChainResidueDetails
BSER458

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) threonine => ECO:0000269|PubMed:21757702, ECO:0000269|PubMed:28089369
ChainResidueDetails
BTHR466

222415

PDB entries from 2024-07-10

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