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9ZNN

Cryo-EM structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) in complex with APPB

This is a non-PDB format compatible entry.
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=Helix 1","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues228
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=Helix 2","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues52
DetailsTransmembrane: {"description":"Helical; Name=Helix 3","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=Helix 4","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues54
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=Helix 5","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=Helix 6","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=Helix 7","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues36
DetailsTransmembrane: {"description":"Helical; Name=Helix 8","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=Helix 9","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=Helix 10","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30388443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BW6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30388443","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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