Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TH8

Structure of E. coli undecaprenyl diphosphate synthase complexed with BPH-1063

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008360biological_processregulation of cell shape
A0008834molecular_functiondi-trans,poly-cis-undecaprenyl-diphosphate synthase 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_functiondehydrodolichyl diphosphate synthase activity
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0071555biological_processcell wall organization
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008360biological_processregulation of cell shape
B0008834molecular_functiondi-trans,poly-cis-undecaprenyl-diphosphate synthase 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_functiondehydrodolichyl diphosphate synthase activity
B0046872molecular_functionmetal ion binding
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TH9 B 289
ChainResidue
BASP26
BILE141
BHOH293
BASN28
BGLY29
BARG39
BHIS43
BGLY46
BALA47
BALA69
BPHE70

Functional Information from PROSITE/UniProt
site_idPS01066
Number of Residues18
DetailsUPP_SYNTHASE Undecaprenyl pyrophosphate synthase family signature. DLVIRTGGehRiSnFLLW
ChainResidueDetails
BASP190-TRP207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
BASP26
AASP26

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
BASN74
AASN74

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
BASP26
BHIS199
BARG200
BGLU213
AASP26
AHIS199
AARG200
AGLU213

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:15044730
ChainResidueDetails
BTRP31
BTRP75
ATRP31
ATRP75

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15044730
ChainResidueDetails
BARG39
BHIS43
BARG77
BARG194
AARG39
AHIS43
AARG77
AARG194

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BSER71
ASER71

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Required for continued chain elongation
ChainResidueDetails
BALA69
AALA69

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Important for determining product length
ChainResidueDetails
BLEU137
ALEU137

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon