Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4H3A

Structure of E. coli undecaprenyl diphosphate synthase in complex with BPH-1330

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004659molecular_functionprenyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008834molecular_functionditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016094biological_processpolyprenol biosynthetic process
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
B0000287molecular_functionmagnesium ion binding
B0004659molecular_functionprenyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008834molecular_functionditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016094biological_processpolyprenol biosynthetic process
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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0YY A 301
ChainResidue
AALA47
BGLN164
BGLY165
BASN166
AARG51
AVAL54
ASER55
ALEU93
AGLU96
ASER99
ALEU100
AHIS103

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 0YY B 301
ChainResidue
BILE38
BALA47
BVAL50
BARG51
BSER55
BGLU96
BSER99
BARG102
BHIS103

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 Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15044730","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
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

251174

PDB entries from 2026-03-25

PDB statisticsPDBj update infoContact PDBjnumon