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6Z1N

Structure of the human heterotetrameric cis-prenyltransferase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0002094molecular_functionpolyprenyltransferase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006486biological_processprotein glycosylation
A0006489biological_processdolichyl diphosphate biosynthetic process
A0006629biological_processlipid metabolic process
A0016020cellular_componentmembrane
A0016094biological_processpolyprenol biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0045547molecular_functiondehydrodolichyl diphosphate synthase activity
A0046872molecular_functionmetal ion binding
A1904423cellular_componentdehydrodolichyl diphosphate synthase complex
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0019408biological_processdolichol biosynthetic process
B1904423cellular_componentdehydrodolichyl diphosphate synthase complex
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue FPP A 401
ChainResidue
ATRP3
APHE55
AALA77
AARG85
AVAL152
AMG403
AHOH507
AHOH547
AMET33
AASP34
AGLY35
AASN36
AARG37
AARG38
AHIS51
AGLY54

site_idAC2
Number of Residues10
Detailsbinding site for residue PO4 A 402
ChainResidue
AARG205
AARG211
ASER213
AHOH512
AHOH534
AHOH538
AHOH553
AHOH555
BLEU291
BGLY292

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 403
ChainResidue
AASP34
AFPP401
AHOH507
AHOH547
AHOH555

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 Residues18
DetailsTRANSMEM: Helical; Name=3 => ECO:0000303|PubMed:21572394
ChainResidueDetails
BILE117-TYR135
AARG38
AARG85
AARG205
AARG211
ASER213

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32817466
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21572394
ChainResidueDetails
BASN144
BALA280

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PDB entries from 2024-07-24

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