Target Binding Site Detail
| 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 | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Pamidronate | Ligand Info | |||
| Canonical SMILES | C(CN)C(O)(P(=O)(O)O)P(=O)(O)O | ||||
| InChI | 1S/C3H11NO7P2/c4-2-1-3(5,12(6,7)8)13(9,10)11/h5H,1-2,4H2,(H2,6,7,8)(H2,9,10,11) | ||||
| InChIKey | WRUUGTRCQOWXEG-UHFFFAOYSA-N | ||||
| PubChem Compound ID | 4674 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4KPJ Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant complexed with Mg, Pamidronate | ||||||
| Method | X-ray diffraction | Resolution | 1.95 Å | Mutation | Yes | [1] |
| PDB Sequence |
VYAQEKQDFV
18 QHFSQIVRVL28 TEHPEIGDAI42 ARLKEVLEYN52 AIGGKYNRGL62 TVVVAFRELV 72 EPRKQDADSL82 QRAWTVGWCV92 ELLQAFFLVA102 DDIMDSSLTR112 RGQICWYQKP 122 GVGLDAINDA132 NLLEACIYRL142 LKLYCREQPY152 YLNLIELFLQ162 SSYQTEIGQT 172 LDLLTAPQGN182 VDLVRFTEKR192 YKSIVKYKTA202 FASFYLPIAA212 AMYMAGIDGE 222 KEHANAKKIL232 LEMGEFFQIQ242 DDYLDLFGDP252 SVTGKIGTDI262 QDNKCSWLVV 272 QCLQRATPEQ282 YQILKENYGQ292 KEAEKVARVK302 ALYEELDLPA312 VFLQYEEDSY 322 SHIMALIEQY332 AAPLPPAVFL342 GLARKIYK
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| PDB ID: 4NKF 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 | 2.00 Å | Mutation | Yes | [2] |
| PDB Sequence |
DVYAQEKQDF
17 VQHFSQIVRV27 LTEHPEIGDA41 IARLKEVLEY51 NTIGGKYNRG61 LTVVVAFREL 71 VEPRKQDADS81 LQRAWTVGWC91 VELLQAFFLV101 ADDIMDSSLT111 RRGQICWYQK 121 PGVGLDAIND131 ANLLEACIYR141 LLKLYCREQP151 YYLNLIELFL161 QSSYQTEIGQ 171 TLDLLTAPQG181 NVDLVRFTEK191 RYKSIVKYKT201 AFYSFYLPIA211 AAMYMAGIDG 221 EKEHANAKKI231 LLEMGEFAQI241 QDDYLDLFGD251 PSVTGKIGTD261 IQDNKCSWLV 271 VQCLQRATPE281 QYQILKENYG291 QKEAEKVARV301 KALYEELDLP311 AVFLQYEEDS 321 YSHIMALIEQ331 YAAPLPPAVF341 LGLARKIYK
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| PDB ID: 4OGU 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 | 2.10 Å | Mutation | Yes | [3] |
| PDB Sequence |
DVYAQEKQDF
17 VQHFSQIVRV27 LTEHPEIGDA41 IARLKEVLEY51 NTIGGKYNRG61 LTVVVAFREL 71 VEPRKQDADS81 LQRAWTVGWC91 VELLQAFFLV101 ADDIMDSSLT111 RRGQICWYQK 121 PGVGLDAIND131 ANLLEACIYR141 LLKLYCREQP151 YYLNLIELFL161 QSSYQTEIGQ 171 TLDLLTAPQG181 NVDLVRFTEK191 RYKSIVKYKT201 AFYSFYLPIA211 AAMYMAGIDG 221 EKEHANAKKI231 LLEMGEFAQI241 QDDYLDLFGD251 PSVTGKIGTD261 IQDNKCSWLV 271 VQCLQRATPE281 QYQILKENYG291 QKEAEKVARV301 KALYEELDLP311 AVFLQYEEDS 321 YSHIMALIEQ331 YAAPLPPAVF341 LGLARKIYK
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| PDB ID: 2F89 Crystal structure of human FPPS in complex with pamidronate | ||||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [4] |
| PDB Sequence |
DVYAQEKQDF
17 VQHFSQIVRV27 LTEDEMGHPE37 IGDAIARLKE47 VLEYNAIGGK57 YNRGLTVVVA 67 FRELVEPRKQ77 DADSLQRAWT87 VGWCVELLQA97 FFLVADDIMD107 SSLTRRGQIC 117 WYQKPGVGLD127 AINDANLLEA137 CIYRLLKLYC147 REQPYYLNLI157 ELFLQSSYQT 167 EIGQTLDLLT177 APQGNVDLVR187 FTEKRYKSIV197 KYKTAFYSFY207 LPIAAAMYMA 217 GIDGEKEHAN227 AKKILLEMGE237 FFQIQDDYLD247 LFGDPSVTGK257 IGTDIQDNKC 267 SWLVVQCLQR277 ATPEQYQILK287 ENYGQKEAEK297 VARVKALYEE307 LDLPAVFLQY 317 EEDSYSHIMA327 LIEQYAAPLP337 PAVFLGLARK347 IYKRRK
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .210 or .2102 or .2103 or :3210;style chemicals stick;color identity;select .F:60 or .F:100 or .F:103 or .F:104 or .F:107 or .F:112 or .F:174 or .F:200 or .F:201 or .F:204 or .F:240 or .F:243 or .F:244 or .F:247 or .F:257 or .F:261; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant complexed with Mg, Pamidronate | ||||
| 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 | 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 4 | Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs. ChemMedChem. 2006 Feb;1(2):267-73. | ||||
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