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 T86528 Target Info
Target Name Geranyltranstransferase (FDPS)
Synonyms KIAA1293; Geranylgeranyl pyrophosphate synthase; Geranylgeranyl diphosphate synthase; GGPS1; GGPPSase; GGPP synthase; Farnesyltranstransferase; Farnesyl pyrophosphate synthase; Farnesyl diphosphate synthase; FPS protein; FPP synthase; Dimethylallyltranstransferase; (2E,6E)-farnesyl diphosphate synthase
Target Type Successful Target
Gene Name FDPS
Biochemical Class Alkyl aryl transferase
UniProt ID
FPPS_HUMAN
Ligand General Information  Top
Ligand Name Risedronate Ligand Info
Canonical SMILES C1=CC(=CN=C1)CC(O)(P(=O)(O)O)P(=O)(O)O
InChI 1S/C7H11NO7P2/c9-7(16(10,11)12,17(13,14)15)4-6-2-1-3-8-5-6/h1-3,5,9H,4H2,(H2,10,11,12)(H2,13,14,15)
InChIKey IIDJRNMFWXDHID-UHFFFAOYSA-N
PubChem Compound ID 5245
Drug Binding Sites of Target  Top
PDB ID: 4NUA      The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
Method X-ray diffraction Resolution 1.43 Å Mutation Yes [1]
PDB Sequence
AYAQEKQDFV
18
QHFSQIVRVL
28
TEHPEIGDAI
42
ARLKEVLEYN
52
TIGGKYNRGL
62

TVVVAFRELV
72
EPRKQDADSL
82
QRAWTVGWCV
92
ELLQAFFLVA
102
DDIMDSSLTR
112

RGQICWYQKP
122
GVGLDAINDA
132
NLLEACIYRL
142
LKLYCREQPY
152
YLNLIELFLQ
162

SSYQTEIGQT
172
LDLLTAPQGN
182
VDLVRFTEKR
192
YKSIVKYKTA
202
FYSFYLPIAA
212

AMYMAGIDGE
222
KEHANAKKIL
232
LEMGEFAQIQ
242
DDYLDLFGDP
252
SVTGKIGTDI
262

QDNKCSWLVV
272
QCLQRATPEQ
282
YQILKENYGQ
292
KEAEKVARVK
302
ALYEELDLPA
312

VFLQYEEDSY
322
SHIMALIEQY
332
AAPLPPAVFL
342
GLARKIYK
Residue
Distance (Å)
PHE99
4.217
LEU100
3.719
ASP103
2.940
ASP104
4.397
ASP107
2.759
ARG112
2.852
THR167
4.052
GLN171
3.479
ASP174
4.574
Residue
Distance (Å)
LYS200
2.711
THR201
2.943
TYR204
3.935
GLN240
3.690
ASP243
2.922
ASP244
4.647
ASP247
4.542
LYS257
2.728
ASP261
4.339
PDB ID: 4NKE      The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
Method X-ray diffraction Resolution 1.46 Å Mutation Yes [2]
PDB Sequence
VYAQEKQDFV
18
QHFSQIVRVL
28
TEHPEIGDAI
42
ARLKEVLEYN
52
TIGGKYNRGL
62

TVVVAFRELV
72
EPRKQDADSL
82
QRAWTVGWCV
92
ELLQAFFLVA
102
DDIMDSSLTR
112

RGQICWYQKP
122
GVGLDAINDA
132
NLLEACIYRL
142
LKLYCREQPY
152
YLNLIELFLQ
162

SSYQTEIGQT
172
LDLLTAPQGN
182
VDLVRFTEKR
192
YKSIVKYKTA
202
FYSFYLPIAA
212

AMYMAGIDGE
222
KEHANAKKIL
232
LEMGEFAQIQ
242
DDYLDLFGDP
252
SVTGKIGTDI
262

QDNKCSWLVV
272
QCLQRATPEQ
282
YQILKENYGQ
292
KEAEKVARVK
302
ALYEELDLPA
312

VFLQYEEDSY
322
SHIMALIEQY
332
AAPLPPAVFL
342
GLARKIYK
Residue
Distance (Å)
PHE99
4.251
LEU100
3.961
ASP103
2.921
ASP104
4.358
ASP107
2.708
ARG112
2.730
THR167
4.161
GLN171
3.498
ASP174
4.599
Residue
Distance (Å)
LYS200
2.708
THR201
2.918
TYR204
3.817
GLN240
3.623
ASP243
2.922
ASP244
4.614
ASP247
4.692
LYS257
2.822
ASP261
4.335
PDB ID: 4KPD      Crystal Structure of Human Farnesyl Pyrophosphate Synthase (Y204F) Mutant Complexed with Mg, Risedronate and Isopentenyl Pyrophosphate
Method X-ray diffraction Resolution 1.96 Å Mutation Yes [3]
PDB Sequence
VYAQEKQDFV
18
QHFSQIVRVL
28
TEHPEIGDAI
42
ARLKEVLEYN
52
AIGGKYNRGL
62

TVVVAFRELV
72
EPRKQDADSL
82
QRAWTVGWCV
92
ELLQAFFLVA
102
DDIMDSSLTR
112

RGQICWYQKP
122
GVGLDAINDA
132
NLLEACIYRL
142
LKLYCREQPY
152
YLNLIELFLQ
162

SSYQTEIGQT
172
LDLLTAPQGN
182
VDLVRFTEKR
192
YKSIVKYKTA
202
FFSFYLPIAA
212

AMYMAGIDGE
222
KEHANAKKIL
232
LEMGEFFQIQ
242
DDYLDLFGDP
252
SVTGKIGTDI
262

QDNKCSWLVV
272
QCLQRATPEQ
282
YQILKENYGQ
292
KEAEKVARVK
302
ALYEELDLPA
312

VFLQYEEDSY
322
SHIMALIEQY
332
AAPLPPAVFL
342
GLARKIYKRR
352
K
Residue
Distance (Å)
PHE99
4.139
LEU100
3.986
ASP103
3.014
ASP104
4.486
ASP107
2.729
ARG112
2.495
THR167
4.079
GLN171
3.521
ASP174
4.410
Residue
Distance (Å)
LYS200
2.509
THR201
3.009
PHE204
3.882
GLN240
3.710
ASP243
2.957
ASP244
4.598
ASP247
4.569
LYS257
2.677
ASP261
4.387
PDB ID: 4KQS      Crystal Structure of Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg, Risedronate and Isopentenyl Pyrophosphate
Method X-ray diffraction Resolution 1.97 Å Mutation Yes [4]
PDB Sequence
VYAQEKQDFV
18
QHFSQIVRVL
28
TEPEIGDAIA
43
RLKEVLEYNA
53
IGGKYNRGLT
63

VVVAFRELVE
73
PRKQDADSLQ
83
RAWTVGWCVE
93
LLQAFFLVAD
103
DIMDSSLTRR
113

GQICWYQKPG
123
VGLDAINDAN
133
LLEACIYRLL
143
KLYCREQPYY
153
LNLIELFLQS
163

SYQTEIGQTL
173
DLLTAPQGNV
183
DLVRFTEKRY
193
KSIVKYKTAF
203
ASFYLPIAAA
213

MYMAGIDGEK
223
EHANAKKILL
233
EMGEFFQIQD
243
DYLDLFGDPS
253
VTGKIGTDIQ
263

DNKCSWLVVQ
273
CLQRATPEQY
283
QILKENYGQK
293
EAEKVARVKA
303
LYEELDLPAV
313

FLQYEEDSYS
323
HIMALIEQYA
333
APLPPAVFLG
343
LARKIYKRRK
353
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:99 or .A:100 or .A:103 or .A:104 or .A:107 or .A:112 or .A:167 or .A:171 or .A:174 or .A:200 or .A:201 or .A:240 or .A:243 or .A:244 or .A:247 or .A:257 or .A:261; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE99
4.345
LEU100
3.795
ASP103
3.033
ASP104
4.347
ASP107
2.717
ARG112
2.650
THR167
4.186
GLN171
3.373
ASP174
4.516
Residue
Distance (Å)
LYS200
2.703
THR201
2.982
GLN240
3.706
ASP243
2.857
ASP244
4.533
ASP247
4.667
LYS257
2.638
ASP261
4.293
PDB ID: 4Q23      The role of threonine 201 and tyrosine 204 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
Method X-ray diffraction Resolution 1.98 Å Mutation Yes [5]
PDB Sequence
VYAQEKQDFV
18
QHFSQIVRVL
28
TGHPEIGDAI
42
ARLKEVLEYN
52
AIGGKYNRGL
62

TVVVAFRELV
72
EPRKQDADSL
82
QRAWTVGWCV
92
ELLQAFFLVA
102
DDIMDSSLTR
112

RGQICWYQKP
122
GVGLDAINDA
132
NLLEACIYRL
142
LKLYCREQPY
152
YLNLIELFLQ
162

SSYQTEIGQT
172
LDLLTAPQGN
182
VDLVRFTEKR
192
YKSIVKYKAA
202
FYSFYLPIAA
212

AMYMAGIDGE
222
KEHANAKKIL
232
LEMGEFFQIQ
242
DDYLDLFGDP
252
SVTGKIGTDI
262

QDNKCSWLVV
272
QCLQRATPEQ
282
YQILKENYGQ
292
KEAEKVARVK
302
ALYEELDLPA
312

VFLQYEEDSY
322
SHIMALIEQY
332
AAPLPPAVFL
342
GLARKIY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:99 or .A:100 or .A:103 or .A:104 or .A:107 or .A:112 or .A:167 or .A:171 or .A:174 or .A:200 or .A:201 or .A:204 or .A:240 or .A:243 or .A:244 or .A:247 or .A:257 or .A:261; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE99
4.147
LEU100
3.613
ASP103
2.871
ASP104
4.445
ASP107
2.701
ARG112
2.748
THR167
4.008
GLN171
3.531
ASP174
4.337
Residue
Distance (Å)
LYS200
2.626
ALA201
4.600
TYR204
3.901
GLN240
3.793
ASP243
2.881
ASP244
4.655
ASP247
4.554
LYS257
2.996
ASP261
4.461
PDB ID: 4N9U      The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
Method X-ray diffraction Resolution 2.11 Å Mutation Yes [6]
PDB Sequence
DVYAQEKQDF
17
VQHFSQIVRV
27
LTEHPEIGDA
41
IARLKEVLEY
51
NTIGGKYNRG
61

LTVVVAFREL
71
VEPRKQDADS
81
LQRAWTVGWC
91
VELLQAFFLV
101
ADDIMDSSLT
111

RRGQICWYQK
121
PGVGLDAIND
131
ANLLEACIYR
141
LLKLYCREQP
151
YYLNLIELFL
161

QSSYQTEIGQ
171
TLDLLTAPQG
181
NVDLVRFTEK
191
RYKSIVKYGT
201
AFYSFYLPIA
211

AAMYMAGIDG
221
EKEHANAKKI
231
LLEMGEFFQI
241
QDDYLDLFGD
251
PSVTGKIGTD
261

IQDNKCSWLV
271
VQCLQRATPE
281
QYQILKENYG
291
QKEAEKVARV
301
KALYEELDLP
311

AVFLQYEEDS
321
YSHIMALIEQ
331
YAAPLPPAVF
341
LGLARKIY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:99 or .A:100 or .A:103 or .A:104 or .A:107 or .A:112 or .A:167 or .A:171 or .A:200 or .A:201 or .A:204 or .A:240 or .A:243 or .A:244 or .A:247 or .A:257 or .A:261; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE99
4.102
LEU100
3.682
ASP103
2.971
ASP104
4.665
ASP107
2.887
ARG112
2.659
THR167
3.798
GLN171
3.553
GLY200
2.894
Residue
Distance (Å)
THR201
2.962
TYR204
3.887
GLN240
3.646
ASP243
2.958
ASP244
4.568
ASP247
4.765
LYS257
2.905
ASP261
4.349
PDB ID: 4NG6      The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
Method X-ray diffraction Resolution 2.35 Å Mutation Yes [7]
PDB Sequence
YAQEKQDFVQ
19
HFSQIVRVLT
29
EDEMGHPEIG
39
DAIARLKEVL
49
EYNAIGGKYN
59

RGLTVVVAFR
69
ELVEPRKQDA
79
DSLQRAWTVG
89
WCVELLQAFF
99
LVADDIMDSS
109

LTRRGQICWY
119
QKPGVGLDAI
129
NDANLLEACI
139
YRLLKLYCRE
149
QPYYLNLIEL
159

FLQSSYQTEI
169
GQTLDLLTAP
179
QGNVDLVRFT
189
EKRYKSIVKY
199
LTAFYSFYLP
209

IAAAMYMAGI
219
DGEKEHANAK
229
KILLEMGEFF
239
QIQDDYLDLF
249
GDPSVTGKIG
259

TDIQDNKCSW
269
LVVQCLQRAT
279
PEQYQILKEN
289
YGQKEAEKVA
299
RVKALYEELD
309

LPAVFLQYEE
319
DSYSHIMALI
329
EQYAAPLPPA
339
VFLGLARKIY
349
KRRK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:99 or .A:100 or .A:103 or .A:104 or .A:107 or .A:109 or .A:112 or .A:167 or .A:171 or .A:174 or .A:200 or .A:201 or .A:204 or .A:240 or .A:243 or .A:244 or .A:247 or .A:257 or .A:261; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE99
4.135
LEU100
3.968
ASP103
3.067
ASP104
4.343
ASP107
2.533
SER109
4.903
ARG112
2.511
THR167
3.864
GLN171
3.934
ASP174
4.290
Residue
Distance (Å)
LEU200
3.162
THR201
2.961
TYR204
3.803
GLN240
3.672
ASP243
2.855
ASP244
4.513
ASP247
4.681
LYS257
2.747
ASP261
4.244
PDB ID: 2QIS      Crystal structure of human farnesyl pyrophosphate synthase T210S mutant bound to risedronate
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [8]
PDB Sequence
DVYAQEKQDF
31
VQHFSQIVRV
41
LTEDEHPEIG
53
DAIARLKEVL
63
EYNAIGGKYN
73

RGLTVVVAFR
83
ELVEPRKQDA
93
DSLQRAWTVG
103
WCVELLQAFF
113
LVADDIMDSS
123

LTRRGQICWY
133
QKPGVGLDAI
143
NDANLLEACI
153
YRLLKLYCRE
163
QPYYLNLIEL
173

FLQSSYQTEI
183
GQTLDLLTAP
193
QGNVDLVRFT
203
EKRYKSIVKY
213
KSAFYSFYLP
223

IAAAMYMAGI
233
DGEKEHANAK
243
KILLEMGEFF
253
QIQDDYLDLF
263
GDPSVTGKIG
273

TDIQDNKCSW
283
LVVQCLQRAT
293
PEQYQILKEN
303
YGQKEAEKVA
313
RVKALYEELD
323

LPAVFLQYEE
333
DSYSHIMALI
343
EQYAAPLPPA
353
VFLGLARKIY
363
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:113 or .A:114 or .A:117 or .A:118 or .A:121 or .A:123 or .A:126 or .A:181 or .A:185 or .A:188 or .A:214 or .A:215 or .A:218 or .A:254 or .A:257 or .A:258 or .A:261 or .A:271 or .A:275; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE113
4.490
LEU114
3.681
ASP117
3.054
ASP118
4.369
ASP121
2.849
SER123
4.989
ARG126
2.893
THR181
4.114
GLN185
3.448
ASP188
4.497
Residue
Distance (Å)
LYS214
2.520
SER215
2.843
TYR218
4.098
GLN254
3.830
ASP257
2.906
ASP258
4.657
ASP261
4.792
LYS271
2.733
ASP275
4.351
PDB ID: 1YV5      Human farnesyl diphosphate synthase complexed with Mg and risedronate
Method X-ray diffraction Resolution 2.00 Å Mutation No [9]
PDB Sequence
EKQDFVQHFS
36
QIVRVLTEDE
46
HPEIGDAIAR
58
LKEVLEYNAI
68
GGKYNRGLTV
78

VVAFRELVEP
88
RKQDADSLQR
98
AWTVGWCVEL
108
LQAFFLVADD
118
IMDSSLTRRG
128

QICWYQKPGV
138
GLDAINDANL
148
LEACIYRLLK
158
LYCREQPYYL
168
NLIELFLQSS
178

YQTEIGQTLD
188
LLTAPQGNVD
198
LVRFTEKRYK
208
SIVKYKTAFY
218
SFYLPIAAAM
228

YMAGIDGEKE
238
HANAKKILLE
248
MGEFFQIQDD
258
YLDLFGDPSV
268
TGKIGTDIQD
278

NKCSWLVVQC
288
LQRATPEQYQ
298
ILKENYGQKE
308
AEKVARVKAL
318
YEELDLPAVF
328

LQYEEDSYSH
338
IMALIEQYAA
348
PLPPAVFLGL
358
ARKIYK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:113 or .A:114 or .A:117 or .A:118 or .A:121 or .A:123 or .A:126 or .A:181 or .A:185 or .A:188 or .A:214 or .A:215 or .A:218 or .A:254 or .A:257 or .A:258 or .A:261 or .A:271 or .A:275; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE113
4.273
LEU114
3.805
ASP117
2.922
ASP118
4.420
ASP121
3.098
SER123
4.955
ARG126
2.658
THR181
4.118
GLN185
3.489
ASP188
4.639
Residue
Distance (Å)
LYS214
2.442
THR215
3.026
TYR218
3.922
GLN254
3.580
ASP257
2.846
ASP258
4.594
ASP261
4.830
LYS271
2.760
ASP275
4.362
PDB ID: 1YQ7      Human farnesyl diphosphate synthase complexed with risedronate
Method X-ray diffraction Resolution 2.20 Å Mutation No [10]
PDB Sequence
EKQDFVQHFS
36
QIVRVLTEDE
46
PEIGDAIARL
59
KEVLEYNAIG
69
GKYNRGLTVV
79

VAFRELVEPR
89
KQDADSLQRA
99
WTVGWCVELL
109
QAFFLVADDI
119
MDSSLTRRGQ
129

ICWYQKPGVG
139
LDAINDANLL
149
EACIYRLLKL
159
YCREQPYYLN
169
LIELFLQSSY
179

QTEIGQTLDL
189
LTAPQGNVDL
199
VRFTEKRYKS
209
IVKYKTAFYS
219
FYLPIAAAMY
229

MAGIDGEKEH
239
ANAKKILLEM
249
GEFFQIQDDY
259
LDLFGDPSVT
269
GKIGTDIQDN
279

KCSWLVVQCL
289
QRATPEQYQI
299
LKENYGQKEA
309
EKVARVKALY
319
EELDLPAVFL
329

QYEEDSYSHI
339
MALIEQYAAP
349
LPPAVFLGLA
359
RKIY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:113 or .A:114 or .A:117 or .A:118 or .A:121 or .A:123 or .A:126 or .A:181 or .A:185 or .A:188 or .A:214 or .A:215 or .A:218 or .A:254 or .A:257 or .A:261 or .A:271 or .A:275; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE113
4.554
LEU114
3.822
ASP117
2.968
ASP118
4.688
ASP121
3.152
SER123
4.993
ARG126
2.228
THR181
4.258
GLN185
3.494
Residue
Distance (Å)
ASP188
4.351
LYS214
2.361
THR215
2.751
TYR218
3.826
GLN254
3.349
ASP257
2.809
ASP261
4.857
LYS271
2.622
ASP275
4.387
PDB ID: 5CG5      Neutron crystal structure of human farnesyl pyrophosphate synthase in complex with risedronate
Method X-ray diffraction Resolution 1.40 Å Mutation No [11]
PDB Sequence
DVYAQEKQDF
17
VQHFSQIVRV
27
LTEDEMGHPE
37
IGDAIARLKE
47
VLEYNAIGGK
57

YNRGLTVVVA
67
FRELVEPRKQ
77
DADSLQRAWT
87
VGWCVELLQA
97
FFLVADDIMD
107

SSLTRRGQIC
117
WYQKPGVGLD
127
AINDANLLEA
137
CIYRLLKLYC
147
REQPYYLNLI
157

ELFLQSSYQT
167
EIGQTLDLLT
177
APQGNVDLVR
187
FTEKRYKSIV
197
KYKTAFYSFY
207

LPIAAAMYMA
217
GIDGEKEHAN
227
AKKILLEMGE
237
FFQIQDDYLD
247
LFGDPSVTGK
257

IGTDIQDNKC
267
SWLVVQCLQR
277
ATPEQYQILK
287
ENYGQKEAEK
297
VARVKALYEE
307

LDLPAVFLQY
317
EEDSYSHIMA
327
LIEQYAAPLP
337
PAVFLGLARK
347
IYK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:99 or .A:100 or .A:103 or .A:104 or .A:107 or .A:109 or .A:112 or .A:167 or .A:171 or .A:174 or .A:200 or .A:201 or .A:204 or .A:240 or .A:243 or .A:244 or .A:247 or .A:257 or .A:261 or .A:266; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE99
2.721
LEU100
2.673
ASP103
2.468
ASP104
4.429
ASP107
2.780
SER109
4.825
ARG112
1.861
THR167
2.716
GLN171
2.940
ASP174
4.649
Residue
Distance (Å)
LYS200
1.770
THR201
1.963
TYR204
2.956
GLN240
2.347
ASP243
1.998
ASP244
4.655
ASP247
4.654
LYS257
2.310
ASP261
4.350
LYS266
4.921
PDB ID: 5CG6      Neutron crystal structure of human farnesyl pyrophosphate synthase in complex with risedronate and isopentenyl pyrophosphate
Method X-ray diffraction Resolution 1.70 Å Mutation No [11]
PDB Sequence
DVYAQEKQDF
17
VQHFSQIVRV
27
LTEDEMGHPE
37
IGDAIARLKE
47
VLEYNAIGGK
57

YNRGLTVVVA
67
FRELVEPRKQ
77
DADSLQRAWT
87
VGWCVELLQA
97
FFLVADDIMD
107

SSLTRRGQIC
117
WYQKPGVGLD
127
AINDANLLEA
137
CIYRLLKLYC
147
REQPYYLNLI
157

ELFLQSSYQT
167
EIGQTLDLLT
177
APQGNVDLVR
187
FTEKRYKSIV
197
KYKTAFYSFY
207

LPIAAAMYMA
217
GIDGEKEHAN
227
AKKILLEMGE
237
FFQIQDDYLD
247
LFGDPSVTGK
257

IGTDIQDNKC
267
SWLVVQCLQR
277
ATPEQYQILK
287
ENYGQKEAEK
297
VARVKALYEE
307

LDLPAVFLQY
317
EEDSYSHIMA
327
LIEQYAAPLP
337
PAVFLGLARK
347
IYK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RIS or .RIS2 or .RIS3 or :3RIS;style chemicals stick;color identity;select .A:99 or .A:100 or .A:103 or .A:104 or .A:107 or .A:109 or .A:112 or .A:167 or .A:171 or .A:174 or .A:200 or .A:201 or .A:204 or .A:205 or .A:240 or .A:243 or .A:244 or .A:247 or .A:257 or .A:261 or .A:266; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PHE99
2.742
LEU100
2.734
ASP103
2.419
ASP104
4.323
ASP107
2.756
SER109
4.982
ARG112
1.825
THR167
3.071
GLN171
3.026
ASP174
4.580
LYS200
1.728
Residue
Distance (Å)
THR201
1.843
TYR204
2.788
SER205
4.913
GLN240
2.316
ASP243
2.874
ASP244
4.594
ASP247
4.689
LYS257
1.884
ASP261
4.359
LYS266
4.915
References  Top
REF 1 The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
REF 2 The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
REF 3 Crystal Structure of Human Farnesyl Pyrophosphate Synthase (Y204F) Mutant Complexed with Mg, Risedronate and Isopentenyl Pyrophosphate
REF 4 Crystal Structure of Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg, Risedronate and Isopentenyl Pyrophosphate
REF 5 The role of threonine 201 and tyrosine 204 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
REF 6 The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
REF 7 The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
REF 8 Crystal structure of human farnesyl pyrophosphate synthase T210S mutant bound to risedronate.
REF 9 The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs. Proc Natl Acad Sci U S A. 2006 May 16;103(20):7829-34.
REF 10 Human farnesyl diphosphate complexed with clinical inhibitor risedronate
REF 11 Protonation State and Hydration of Bisphosphonate Bound to Farnesyl Pyrophosphate Synthase. J Med Chem. 2015 Sep 24;58(18):7549-56.

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