Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T52189 | Target Info | |||
| Target Name | ATP-citrate synthase (ACLY) | ||||
| Synonyms | Citrate cleavage enzyme; ATP-citrate (pro-S-)-lyase; ACL | ||||
| Target Type | Successful Target | ||||
| Gene Name | ACLY | ||||
| Biochemical Class | Acyltransferase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | 1-Phosphono-L-histidine | Ligand Info | |||
| Canonical SMILES | C1=C(N=CN1P(=O)(O)O)CC(C(=O)O)N | ||||
| InChI | 1S/C6H10N3O5P/c7-5(6(10)11)1-4-2-9(3-8-4)15(12,13)14/h2-3,5H,1,7H2,(H,10,11)(H2,12,13,14)/t5-/m0/s1 | ||||
| InChIKey | MOYPZVWCTBPWEH-YFKPBYRVSA-N | ||||
| PubChem Compound ID | 15458486 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5TDF TEV Cleaved Human ATP Citrate Lyase Bound to 4S hydroxycitrate | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [1] |
| PDB Sequence |
> Chain A
SAKAISEQTG 11 KELLYKFICT21 TSAIQNRFKY31 ARVTPDTDWA41 RLLQDHPWLL51 SQNLVVKPDQ 61 LIKRRGKLGL71 VGVNLTLDGV81 KSWLKPRLGQ91 EATVGKATGF101 LKNFLIEPFV 111 PHSQAEEFYV121 CIYATREGDY131 VLFHHEGGAQ150 KLLVGVDEKL160 NPEDIKKHLL 170 VHAPEDKKEI180 LASFISGLFN190 FYEDLYFTYL200 EINPLVVTKD210 GVYVLDLAAK 220 VDATADYICK230 VKWGDIEFPP240 PFGREAYPEE250 AYIADLDAKS260 GASLKLTLLN 270 PKGRIWTMVA280 GGGASVVYSD290 TICDLGGVNE300 LANYGEYSGA310 PSEQQTYDYA 320 KTILSLMTRE330 KHPDGKILII340 GGSIANFTNV350 AATFKGIVRA360 IRDYQGPLKE 370 HEVTIFVRRG380 GPNYQEGLRV390 MGEVGKTTGI400 PIHVFGTETH410 MTAIVGMALG 420 HRPIPENLYF430 Q> Chain B SKSTTLFSRH 496 TKAIVWGMQT506 RAVQGMLDFD516 YVCSRDEPSV526 AAMVYPFTGD536 HKQKFYWGHK 546 EILIPVFKNM556 ADAMRKHPEV566 DVLINFASLR576 SAYDSTMETM586 NYAQIRTIAI 596 IAEGIPEALT606 RKLIKKADQK616 GVTIIGPATV626 GGIKPGCFKI636 GNTGGMLDNI 646 LASKLYRPGS656 VAYVSRSGGM666 SNELNNIISR676 TTDGVYEGVA686 IGGDRYPGST 696 FMDHVLRYQD706 TPGVKMIVVL716 GEIGGTEEYK726 ICRGIKEGRL736 TKPIVCWCIG 746 TCATMFSSEV756 QFGAGACANQ767 ASETAVAKNQ777 ALKEAGVFVP787 RSFDELGEII 797 QSVYEDLVAN807 GVI
|
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SER2[A]
4.745
GLY281[A]
4.278
GLY282[A]
2.553
GLY283[A]
2.036
ALA284[A]
4.425
GLU599[B]
3.869
ALA624[B]
4.656
THR625[B]
4.996
ARG662[B]
3.336
SER663[B]
1.849
GLY664[B]
2.222
GLY665[B]
3.709
|
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| PDB ID: 5TDZ TEV Cleaved Human ATP Citrate Lyase Bound to Tartrate and ADP | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
> Chain A
SAKAISEQTG 11 KELLYKFICT21 TSAIQNRFKY31 ARVTPDTDWA41 RLLQDHPWLL51 SQNLVVKPDQ 61 LIKRRGKLGL71 VGVNLTLDGV81 KSWLKPRLGQ91 EATVGKATGF101 LKNFLIEPFV 111 PHSQAEEFYV121 CIYATREGDY131 VLFHHAQKLL153 VGVDEKLNPE163 DIKKHLLVHA 173 PEDKKEILAS183 FISGLFNFYE193 DLYFTYLEIN203 PLVVTKDGVY213 VLDLAAKVDA 223 TADYICKVKW233 GDIEFPPPFG243 REAYPEEAYI253 ADLDAKSGAS263 LKLTLLNPKG 273 RIWTMVAGGG283 ASVVYSDTIC293 DLGGVNELAN303 YGEYSGAPSE313 QQTYDYAKTI 323 LSLMTREKHP333 DGKILIIGGS343 IANFTNVAAT353 FKGIVRAIRD363 YQGPLKEHEV 373 TIFVRRGGPN383 YQEGLRVMGE393 VGKTTGIPIH403 VFGTETHMTA413 IVGMALGHRP 423 IPENLYFQ> Chain B SKSTTLFSRH 496 TKAIVWGMQT506 RAVQGMLDFD516 YVCSRDEPSV526 AAMVYPFTGD536 HKQKFYWGHK 546 EILIPVFKNM556 ADAMRKHPEV566 DVLINFASLR576 SAYDSTMETM586 NYAQIRTIAI 596 IAEGIPEALT606 RKLIKKADQK616 GVTIIGPATV626 GGIKPGCFKI636 GNTGGMLDNI 646 LASKLYRPGS656 VAYVSRSGGM666 SNELNNIISR676 TTDGVYEGVA686 IGGDRYPGST 696 FMDHVLRYQD706 TPGVKMIVVL716 GEIGGTEEYK726 ICRGIKEGRL736 TKPIVCWCIG 746 TCATMFSSEV756 QFGAGACANQ767 ASETAVAKNQ777 ALKEAGVFVP787 RSFDELGEII 797 QSVYEDLVAN807 GVI
|
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SER2[A]
4.511
LYS265[A]
4.892
GLY281[A]
3.966
GLY282[A]
2.379
GLY283[A]
2.296
ALA284[A]
4.683
GLU306[A]
4.863
SER308[A]
4.411
GLU599[B]
4.007
ALA624[B]
4.418
THR625[B]
4.528
ARG662[B]
3.993
SER663[B]
1.866
GLY664[B]
2.267
|
|||||
| PDB ID: 5TDM TEV Cleaved Human ATP Citrate Lyase Bound to 4R-Hydroxycitrate and ADP | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [1] |
| PDB Sequence |
> Chain A
SAKAISEQTG 11 KELLYKFICT21 TSAIQNRFKY31 ARVTPDTDWA41 RLLQDHPWLL51 SQNLVVKPDQ 61 LIKRRGKLGL71 VGVNLTLDGV81 KSWLKPRLGQ91 EATVGKATGF101 LKNFLIEPFV 111 PHSQAEEFYV121 CIYATREGDY131 VLFHHEGGVD141 VGAKAQKLLV154 GVDEKLNPED 164 IKKHLLVHAP174 EDKKEILASF184 ISGLFNFYED194 LYFTYLEINP204 LVVTKDGVYV 214 LDLAAKVDAT224 ADYICKVKWG234 DIEFPPPFGR244 EAYPEEAYIA254 DLDAKSGASL 264 KLTLLNPKGR274 IWTMVAGGGA284 SVVYSDTICD294 LGGVNELANY304 GEYSGAPSEQ 314 QTYDYAKTIL324 SLMTREKHPD334 GKILIIGGSI344 ANFTNVAATF354 KGIVRAIRDY 364 QGPLKEHEVT374 IFVRRGGPNY384 QEGLRVMGEV394 GKTTGIPIHV404 FGTETHMTAI 414 VGMALGHRPI424 PENLYFQ> Chain B KSTTLFSRHT 497 KAIVWGMQTR507 AVQGMLDFDY517 VCSRDEPSVA527 AMVYPFTGDH537 KQKFYWGHKE 547 ILIPVFKNMA557 DAMRKHPEVD567 VLINFASLRS577 AYDSTMETMN587 YAQIRTIAII 597 AEGIPEALTR607 KLIKKADQKG617 VTIIGPATVG627 GIKPGCFKIG637 NTGGMLDNIL 647 ASKLYRPGSV657 AYVSRSGGMS667 NELNNIISRT677 TDGVYEGVAI687 GGDRYPGSTF 697 MDHVLRYQDT707 PGVKMIVVLG717 EIGGTEEYKI727 CRGIKEGRLT737 KPIVCWCIGT 747 CATMFSSEVQ757 FGAGACANQA768 SETAVAKNQA778 LKEAGVFVPR788 SFDELGEIIQ 798 SVYEDLVANG808 VI
|
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SER2[A]
4.444
LYS265[A]
4.618
GLY281[A]
4.418
GLY282[A]
2.798
GLY283[A]
2.267
ALA284[A]
4.480
GLU306[A]
4.463
GLU599[B]
3.706
ALA624[B]
4.481
THR625[B]
4.805
ARG662[B]
3.743
SER663[B]
1.958
GLY664[B]
2.467
|
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| PDB ID: 5TES TEV Cleaved Human ATP Citrate Lyase Bound to Citrate and ADP | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [1] |
| PDB Sequence |
> Chain A
SAKAISEQTG 11 KELLYKFICT21 TSAIQNRFKY31 ARVTPDTDWA41 RLLQDHPWLL51 SQNLVVKPDQ 61 LIKRRGKLGL71 VGVNLTLDGV81 KSWLKPRLGQ91 EATVGKATGF101 LKNFLIEPFV 111 PHSQAEEFYV121 CIYATREGDY131 VLFHHEGGVD141 VKAQKLLVGV156 DEKLNPEDIK 166 KHLLVHAPED176 KKEILASFIS186 GLFNFYEDLY196 FTYLEINPLV206 VTKDGVYVLD 216 LAAKVDATAD226 YICKVKWGDI236 EFPPPFGREA246 YPEEAYIADL256 DAKSGASLKL 266 TLLNPKGRIW276 TMVAGGGASV286 VYSDTICDLG296 GVNELANYGE306 YSGAPSEQQT 316 YDYAKTILSL326 MTREKHPDGK336 ILIIGGSIAN346 FTNVAATFKG356 IVRAIRDYQG 366 PLKEHEVTIF376 VRRGGPNYQE386 GLRVMGEVGK396 TTGIPIHVFG406 TETHMTAIVG 416 MALGHRPIPE426 NLYFQ> Chain B SKSTTLFSRH 496 TKAIVWGMQT506 RAVQGMLDFD516 YVCSRDEPSV526 AAMVYPFTGD536 HKQKFYWGHK 546 EILIPVFKNM556 ADAMRKHPEV566 DVLINFASLR576 SAYDSTMETM586 NYAQIRTIAI 596 IAEGIPEALT606 RKLIKKADQK616 GVTIIGPATV626 GGIKPGCFKI636 GNTGGMLDNI 646 LASKLYRPGS656 VAYVSRSGGM666 SNELNNIISR676 TTDGVYEGVA686 IGGDRYPGST 696 FMDHVLRYQD706 TPGVKMIVVL716 GEIGGTEEYK726 ICRGIKEGRL736 TKPIVCWCIG 746 TCATMFSSEV756 QFGAGACANQ767 ASETAVAKNQ777 ALKEAGVFVP787 RSFDELGEII 797 QSVYEDLVAN807 GVI
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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 .NEP or .NEP2 or .NEP3 or :3NEP;style chemicals stick;color identity;select .A:2 or .A:281 or .A:282 or .A:283 or .A:284 or .A:306 or .B:599 or .B:624 or .B:625 or .B:662 or .B:663 or .B:664 or .B:665 or .B:666 or .B:688 or .B:689 or .B:690 or .B:718 or .B:745 or .B:757 or .B:758 or .B:759 or .B:761 or .B:762 or .B:763 or .B:764; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
SER2[A]
4.626
GLY281[A]
4.315
GLY282[A]
2.589
GLY283[A]
2.182
ALA284[A]
4.288
GLU306[A]
4.999
GLU599[B]
3.864
ALA624[B]
4.543
THR625[B]
4.985
ARG662[B]
3.330
SER663[B]
1.899
GLY664[B]
2.408
GLY665[B]
3.597
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Binding of hydroxycitrate to human ATP-citrate lyase. Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):660-671. | ||||
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