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1UEH

E. coli undecaprenyl pyrophosphate synthase in complex with Triton X-100, magnesium and sulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004659molecular_functionprenyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008360biological_processregulation of cell shape
A0008834molecular_functionditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016094biological_processpolyprenol biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0036094molecular_functionsmall molecule binding
A0042803molecular_functionprotein homodimerization activity
A0043164biological_processGram-negative-bacterium-type cell wall biogenesis
A0045547molecular_functionditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0071555biological_processcell wall organization
B0000287molecular_functionmagnesium ion binding
B0004659molecular_functionprenyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008360biological_processregulation of cell shape
B0008834molecular_functionditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016094biological_processpolyprenol biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0036094molecular_functionsmall molecule binding
B0042803molecular_functionprotein homodimerization activity
B0043164biological_processGram-negative-bacterium-type cell wall biogenesis
B0045547molecular_functionditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity
B0046872molecular_functionmetal ion binding
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AGLY27
AASN28
AGLY29
AARG30
AARG39
AHOH1170

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 902
ChainResidue
BARG241
AARG194
AARG200
ASER202

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 903
ChainResidue
BGLY27
BASN28
BGLY29
BARG30
BHOH1037

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 904
ChainResidue
BARG194
BARG200
BSER202
BHOH1038

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 905
ChainResidue
BLYS33
BARG102
BHOH973
BHOH1163
BHOH1261

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 701
ChainResidue
AHIS199
AHOH1205
AHOH1206
BGLU213
BHOH1292
BHOH1293

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 702
ChainResidue
AGLU213
AHOH1207
AHOH1208
BHIS199
BHOH1294
BHOH1295

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OXN B 801
ChainResidue
BVAL54
BSER55
BASN59
BGLU96
BHIS103
BOXN802

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OXN B 802
ChainResidue
BMET25
BASN28
BHIS43
BGLY46
BALA47
BALA69
BILE109
BALA143
BTRP221
BOXN801

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE UNL B 803
ChainResidue
BILE38
BARG39
BSER99
BARG102
BHIS103
BHOH948

Functional Information from PROSITE/UniProt
site_idPS01066
Number of Residues18
DetailsUPP_SYNTHASE Undecaprenyl pyrophosphate synthase family signature. DLVIRTGGehRiSnFLLW
ChainResidueDetails
AASP190-TRP207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15044730","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15044730","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Required for continued chain elongation"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Important for determining product length"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1f75
ChainResidueDetails
AARG30
AARG200
AARG39
AARG194

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1f75
ChainResidueDetails
BARG30
BARG200
BARG39
BARG194

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PDB entries from 2025-10-15

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