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7PB1

Structure of the human heterotetrameric cis-prenyltransferase complex in complex with magnesium, GGPP and IsPP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004659molecular_functionprenyltransferase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006486biological_processobsolete protein glycosylation
A0006489biological_processdolichyl diphosphate biosynthetic process
A0006629biological_processlipid metabolic process
A0016094biological_processpolyprenol biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0043048biological_processdolichyl monophosphate biosynthetic process
A0045547molecular_functionditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
A0046872molecular_functionmetal ion binding
A1904423cellular_componentdehydrodolichyl diphosphate synthase complex
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0043048biological_processdolichyl monophosphate biosynthetic process
B1904423cellular_componentdehydrodolichyl diphosphate synthase complex
Functional Information from PROSITE/UniProt
site_idPS01066
Number of Residues18
DetailsUPP_SYNTHASE Undecaprenyl pyrophosphate synthase family signature. DILIRTSGevRlSdFLLW
ChainResidueDetails
AASP201-TRP218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32817466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33077723","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35584224","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6Z1N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7PAX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7PAY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7PB0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7PB1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35584224","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7PAX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32817466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35584224","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7PAX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"21572394","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsMotif: {"description":"RXG motif; crucial for prenyltransferase activity","evidences":[{"source":"PubMed","id":"32817466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28842490","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32817466","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21572394","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-12-03

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