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5L0V

human POGLUT1 in complex with 2F-glucose modified EGF(+) and UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0006486biological_processobsolete protein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0007369biological_processgastrulation
A0010470biological_processregulation of gastrulation
A0012505cellular_componentendomembrane system
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0035251molecular_functionUDP-glucosyltransferase activity
A0035252molecular_functionUDP-xylosyltransferase activity
A0045747biological_processpositive regulation of Notch signaling pathway
A0046527molecular_functionglucosyltransferase activity
A0060537biological_processmuscle tissue development
A0140561molecular_functionEGF-domain serine glucosyltransferase activity
A0140562molecular_functionEGF-domain serine xylosyltransferase activity
A0180059biological_processprotein O-linked glycosylation via glucose
A0180064biological_processprotein O-linked glycosylation via xylose
B0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNtvgsYtClC
ChainResidueDetails
BCYS16-CYS27

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. ClCppGftGPnC
ChainResidueDetails
BCYS25-CYS36

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 Residues10
DetailsRegion: {"description":"Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates","evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5L0U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates","evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5L0V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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