Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T34337 Target Info
Target Name Bacterial Undecaprenyl pyrophosphate synthetase (Bact ispU)
Synonyms ispU; Undecaprenyl diphosphate synthase; Undecaprenyl diphosphate synthase; UPP synthetase; UPP synthase; UDS; Di-trans-poly-cis-decaprenylcistransferase
Target Type Literature-reported Target
Gene Name Bact ispU
Biochemical Class Alkyl aryl transferase
UniProt ID
UPPS_ECOLI
Ligand General Information  Top
Ligand Name Farnesyl thiopyrophosphate Ligand Info
Canonical SMILES CC(=CCCC(=CCCC(=CCSP(=O)(O)OP(=O)(O)O)C)C)C
InChI 1S/C15H28O6P2S/c1-13(2)7-5-8-14(3)9-6-10-15(4)11-12-24-23(19,20)21-22(16,17)18/h7,9,11H,5-6,8,10,12H2,1-4H3,(H,19,20)(H2,16,17,18)/b14-9+,15-11+
InChIKey MYMLCRQRXFRQGP-YFVJMOTDSA-N
PubChem Compound ID 657041
Drug Binding Sites of Target  Top
PDB ID: 1X06      Crystal structure of undecaprenyl pyrophosphate synthase in complex with Mg, IPP and Fspp
Method X-ray diffraction Resolution 1.90 Å Mutation No [1]
PDB Sequence
KLPAHGCRHV
21
AIIMDGNGRW
31
AKKQGKIRAF
41
GHKAGAKSVR
51
RAVSFAANNG
61

IEALTLYAFS
71
SENWNRPAQE
81
VSALMELFVW
91
ALDSEVKSLH
101
RHNVRLRIIG
111

DTSRFNSRLQ
121
ERIRKSEALT
131
AGNTGLTLNI
141
AANYGGRWDI
151
VQGVRQLAEK
161

VQQGNLQPDQ
171
IDEEMLNQHV
181
CMHELAPVDL
191
VIRTGGEHRI
201
SNFLLWQIAY
211

AELYFTDVLW
221
PDFDEQDFEG
231
ALNAFANRE
Residue
Distance (Å)
MET25
3.662
ASP26
2.824
GLY27
3.555
ASN28
3.058
GLY29
2.940
ARG30
2.778
ARG39
2.541
HIS43
2.934
GLY46
3.844
ALA47
3.813
VAL50
3.405
ARG51
3.872
VAL54
4.450
TYR68
3.994
ALA69
3.455
PHE70
4.934
Residue
Distance (Å)
ASN74
3.283
ARG77
2.892
GLU81
4.348
LEU85
4.496
LEU88
4.134
PHE89
4.053
ALA92
3.822
LEU93
3.477
GLU96
3.053
VAL97
4.335
LEU100
4.083
LEU107
4.079
ILE109
4.911
LEU139
3.876
ILE141
3.841
TRP221
3.640
PDB ID: 1X08      Crystal structure of D26A mutant UPPs in complex with Mg, IPP and FsPP
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [1]
PDB Sequence
LPAHGCRHVA
22
IIMAGNGRWA
32
KKQGKIRAFG
42
HKAGAKSVRR
52
AVSFAANNGI
62

EALTLYAFSS
72
ENWNRPAQEV
82
SALMELFVWA
92
LDSEVKSLHR
102
HNVRLRIIGD
112

TSRFNSRLQE
122
RIRKSEALTA
132
GNTGLTLNIA
142
ANYGGRWDIV
152
QGVRQLAEKV
162

QQGNLQPDQI
172
DEEMLNQHVC
182
MHELAPVDLV
192
IRTGGEHRIS
202
NFLLWQIAYA
212

ELYFTDVLWP
222
DFDEQDFEGA
232
LNAFANRE
Residue
Distance (Å)
MET25
3.760
ALA26
3.555
GLY27
2.771
ASN28
2.760
GLY29
2.899
ARG30
2.958
TRP31
4.992
ARG39
3.732
HIS43
2.600
GLY46
3.853
ALA47
3.732
VAL50
3.713
ARG51
3.663
VAL54
4.321
TYR68
4.457
ALA69
3.374
PHE70
4.856
Residue
Distance (Å)
ASN74
3.401
ARG77
2.784
GLU81
4.229
LEU85
3.672
LEU88
4.140
PHE89
4.139
ALA92
3.513
LEU93
3.552
GLU96
3.139
VAL97
4.426
LEU100
4.120
LEU107
4.006
ILE109
4.979
LEU139
4.186
ILE141
3.930
TRP221
3.539
References  Top
REF 1 Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J Biol Chem. 2005 May 27;280(21):20762-74.

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