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5KY5

mouse POFUT1 in complex with EGF(+) 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_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. ClCppGftGPnC
ChainResidueDetails
BCYS25-CYS36

site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNtvgsYtClC
ChainResidueDetails
BCYS16-CYS27

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. ClCppGFtgpn....C
ChainResidueDetails
BCYS25-CYS36

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DiDECasnp..........Cqnggt..CvNtvgsYtC
ChainResidueDetails
BASP1-CYS25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9H488
ChainResidueDetails
AHIS243
AASP345
ASER362
AARG48

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN67
AASN165

221051

PDB entries from 2024-06-12

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