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5KY2

mouse POFUT1 in complex with O-glucosylated mouse Factor VII EGF1 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. CqDhlksYvCfC
ChainResidueDetails
BCYS102-CYS113

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CfCllDfeGRnC
ChainResidueDetails
BCYS111-CYS122

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCasnp..........Cqnggt..CqDhlksYvC
ChainResidueDetails
BASP87-CYS111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000250
ChainResidueDetails
BASP104
AHIS243
AASP345
ASER362

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: O-linked (Xyl...) serine; alternate => ECO:0000250|UniProtKB:P08709
ChainResidueDetails
BSER93
AASN165

219140

PDB entries from 2024-05-01

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