Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T08922 | Target Info | |||
| Target Name | Acetyl-CoA carboxylase 2 (ACACB) | ||||
| Synonyms | Acetyl-Coenzyme A carboxylase beta; Acetyl CoA carboxylase beta; ACCbeta; ACC2; ACC-beta; ACACB | ||||
| Target Type | Successful Target | ||||
| Gene Name | ACACB | ||||
| Biochemical Class | Carbon-carbon ligase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: CP-640186 | Ligand Info | |||||
| Structure Description | Human ACC2 CT domain with CP-640186 | PDB:3FF6 | ||||
| Method | X-ray diffraction | Resolution | 3.19 Å | Mutation | No | [1] |
| PDB Sequence |
PYVTKDLLQA
1704 KRFQAQTLGT1714 TYIYDFPEMF1724 RQALFKLWGS1734 PDKYPKDILT1744 YTELVLDSQG 1754 QLVEMNRLPG1764 GNEVGMVAFK1774 MRFKTQEYPE1784 GRDVIVIGND1794 ITFRIGSFGP 1804 GEDLLYLRAS1814 EMARAEGIPK1824 IYVAANSGAR1834 IGMAEEIKHM1844 FHVAWVDPED 1854 PHKGFKYLYL1864 TPQDYTRISS1874 LNSVHCKHIE1884 EGGESRYMIT1894 DIIGKDDGLG 1904 VENLRGSGMI1914 AGESSLAYEE1924 IVTISLVTCR1934 AIGIGAYLVR1944 LGQRVIQVEN 1954 SHIILTGASA1964 LNKVLGREVY1974 TSNNQLGGVQ1984 IMHYNGVSHI1994 TVPDDFEGVY 2004 TILEWLSYMP2014 KDNHSPVPII2024 TPTDPIDREI2034 EFLPSRAPYD2044 PRWMLAGRPH 2054 PTLKGTWQSG2064 FFDHGSFKEI2074 MAPWAQTVVT2084 GRARLGGIPV2094 GVIAVETRTV 2104 EVAVPADPAN2114 LDSEAKIIQQ2124 AGQVWFPDSA2134 YKTAQAIKDF2144 NREKLPLMIF 2154 ANWRGFSGGM2164 KDMYDQVLKF2174 GAYIVDGLRQ2184 YKQPILIYIP2194 PYAELRGGSW 2204 VVIDATINPL2214 CIEMYADKES2224 RGGVLEPEGT2234 VEIKFRKKDL2244 IKSMRRIDPA 2254 YKKLMEQLGE2264 PDLSDKDRKD2274 LEGRLKARED2284 LLLPIYHQVA2294 VQFADFHDTP 2304 GRMLEKGVIS2314 DILEWKTART2324 FLYWRLRRLL2334 LEDQVKQEIL2344 QASGELSHVH 2354 IQSMLRRWFV2364 ETEGAVKAYL2374 WDNNQVVVQW2384 LEQHWQRSTI2399 RENITYLKHD 2409 SVLKTIRGLV2419 EENPEVAVDC2429 VIYLSQHISP2439 AERAQVVHLL2449 |
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| Ligand Name: Soraphen A | Ligand Info | |||||
| Structure Description | The biotin carboxylase (BC) domain of human Acetyl-CoA Carboxylase 2 (ACC2) in complex with Soraphen A | PDB:3GID | ||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [2] |
| PDB Sequence |
DFTVASPAEF
250 VTRFGGDRVI260 EKVLIANNGI270 AAVKCMRSIR280 RWAYEMFRNE290 RAIRFVVMVT 300 PEDLKANAEY310 IKMADHYVPV320 PGGPNNNNYA330 NVELIVDIAK340 RIPVQAVWAG 350 WGHASENPKL360 PELLCKNGVA370 FLGPPSEAMW380 ALGDKIASTV390 VAQTLQVPTL 400 PWSGSGLTVE410 KGCVKDVDEG440 LEAAERIGFP450 LMIKASEGKG463 IRKAESAEDF 473 PILFRQVQSE483 IPGSPIFLMK493 LAQHARHLEV503 QILADQYGNA513 VSLFGRDCSI 523 QHQKIVEEAP535 ATIAPLAIFE545 FMEQCAIRLA555 KTVGYVSAGT565 VEYLYSQDGS 575 FHFLELNPRL585 QVEHPCTEMI595 ADVNLPAAQL605 QIAMGVPLHR615 LKDIRLLYGE 625 SPWGVTPISF635 ETPSNPPLAR645 GHVIAARITS655 GTVQELNFRS676 SKNVWGYFSV 686 ASQFGHCFSW706 GENREEAISN716 MVVALKELSI726 RTTVEYLINL740 LETESFQNND 750
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ILE270
4.291
VAL273
3.987
LYS274
3.101
ARG277
2.806
SER278
2.637
ARG281
3.652
PRO590
3.738
CYS591
4.698
GLU593
2.680
MET594
3.592
ASP597
3.950
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: 1-[3-({4-[(5s)-3,3-Dimethyl-1-Oxo-2-Oxa-7-Azaspiro[4.5]dec-7-Yl]piperidin-1-Yl}carbonyl)-1-Benzothiophen-2-Yl]-3-Ethylurea | Ligand Info | |||||
| Structure Description | Crystal Structure of Human Acetyl-CoA carboxylase 2 | PDB:3TDC | ||||
| Method | X-ray diffraction | Resolution | 2.41 Å | Mutation | No | [3] |
| PDB Sequence |
TPYVTKDLLQ
1728 AKRFQAQTLG1738 TTYIYDFPEM1748 FRQALFKLWG1758 SPDKYPKDIL1768 TYTELVLDSQ 1778 GQLVEMNRLP1788 GGNEVGMVAF1798 KMRFKTQEYP1808 EGRDVIVIGN1818 DITFRIGSFG 1828 PGEDLLYLRA1838 SEMARAEGIP1848 KIYVAANSGA1858 RIGMAEEIKH1868 MFHVAWVDPE 1878 DPHKGFKYLY1888 LTPQDYTRIS1898 SLNSVHCKHI1908 EEGGESRYMI1918 TDIIGKDDGL 1928 GVENLRGSGM1938 IAGESSLAYE1948 EIVTISLVTC1958 RAIGIGAYLV1968 RLGQRVIQVE 1978 NSHIILTGAS1988 ALNKVLGREV1998 YTSNNQLGGV2008 QIMHYNGVSH2018 ITVPDDFEGV 2028 YTILEWLSYM2038 PKDNHSPVPI2048 ITPTDPIDRE2058 IEFLPSRAPY2068 DPRWMLAGRP 2078 HPTLKGTWQS2088 GFFDHGSFKE2098 IMAPWAQTVV2108 TGRARLGGIP2118 VGVIAVETRT 2128 VEVAVPADPA2138 NLDSEAKIIQ2148 QAGQVWFPDS2158 AYKTAQAIKD2168 FNREKLPLMI 2178 FANWRGFSGG2188 MKDMYDQVLK2198 FGAYIVDGLR2208 QYKQPILIYI2218 PPYAELRGGS 2228 WVVIDATINP2238 LCIEMYADKE2248 SRGGVLEPEG2258 TVEIKFRKKD2268 LIKSMRRIDP 2278 AYKKLMEQLG2288 EPDLSDKDRK2298 DLEGRLKARE2308 DLLLPIYHQV2318 AVQFADFHDT 2328 PGRMLEKGVI2338 SDILEWKTAR2348 TFLYWRLRRL2358 LLEDQVKQEI2368 LQASGELSHV 2378 HIQSMLRRWF2388 VETEGAVKAY2398 LWDNNQVVVQ2408 WLEQHWITYL2431 KHDSVLKTIR 2441 GLVEENPEVA2451
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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 .0EU or .0EU2 or .0EU3 or :30EU;style chemicals stick;color identity;select .A:1985 or .A:1989 or .A:1990 or .A:1992 or .A:1993 or .A:1994; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 2-[1-[(2~{r})-2-(2-Methoxyphenyl)-2-(Oxan-4-Yloxy)ethyl]-5-Methyl-6-(1,3-Oxazol-2-Yl)-2,4-Bis(Oxidanylidene)thieno[2,3-D]pyrimidin-3-Yl]-2-Methyl-Propanamide | Ligand Info | |||||
| Structure Description | Crystal structure of human ACC2 BC domain in complex with ND-646, the primary amide of ND-630 | PDB:5KKN | ||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [4] |
| PDB Sequence |
DFTVASPAEF
250 VTRFGGDRVI260 EKVLIANNGI270 AAVKCMRSIR280 RWAYEMFRNE290 RAIRFVVMVT 300 PEDLKANAEY310 IKMADHYVPV320 PGGPNNNNYA330 NVELIVDIAK340 RIPVQAVWAG 350 WGHASENPKL360 PELLCKNGVA370 FLGPPSEAMW380 ALGDKIASTV390 VAQTLQVPTL 400 PWSGSGLTVE410 WKRISVPEDV428 YDKGCVKDVD438 EGLEAAERIG448 FPLMIKASEG 458 KGIRKAESAE471 DFPILFRQVQ481 SEIPGSPIFL491 MKLAQHARHL501 EVQILADQYG 511 NAVSLFGRDC521 SIQRRHQKIV531 EEAPATIAPL541 AIFEFMEQCA551 IRLAKTVGYV 561 SAGTVEYLYS571 QDGSFHFLEL581 NPRLQVEHPC591 TEMIADVNLP601 AAQLQIAMGV 611 PLHRLKDIRL621 LYGESPWGVT631 PISFNPPLAR645 GHVIAARITS655 TVQELNFRSS 677 KNVWGYFSVA687 QFGHCFSWGE708 NREEAISNMV718 VALKELSIRG728 DFRTTVEYLI 738 NLLETESFQN748 NDIDTGWLDY758 LI
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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 .6U3 or .6U32 or .6U33 or :36U3;style chemicals stick;color identity;select .B:270 or .B:271 or .B:273 or .B:274 or .B:277 or .B:281 or .B:351 or .B:587 or .B:589 or .B:590 or .B:591 or .B:593 or .B:594 or .B:648 or .B:671 or .B:678 or .B:679 or .B:680 or .B:681 or .B:683 or .B:704 or .B:705 or .B:706; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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ILE270
3.475
ALA271
4.959
VAL273
4.295
LYS274
3.236
ARG277
3.140
ARG281
2.585
TRP351
4.099
VAL587
3.252
HIS589
4.634
PRO590
3.410
CYS591
4.758
GLU593
3.693
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | The human ACC2 CT-domain C-terminus is required for full functionality and has a novel twist. Acta Crystallogr D Biol Crystallogr. 2009 May;65(Pt 5):449-61. | ||||
| REF 2 | Synthesis and characterization of a BODIPY-labeled derivative of Soraphen A that binds to acetyl-CoA carboxylase. Bioorg Med Chem Lett. 2009 May 15;19(10):2804-7. | ||||
| REF 3 | Design, synthesis, and structure-activity relationships of spirolactones bearing 2-ureidobenzothiophene as acetyl-CoA carboxylases inhibitors. Bioorg Med Chem Lett. 2011 Nov 1;21(21):6314-8. | ||||
| REF 4 | Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats. Proc Natl Acad Sci U S A. 2016 Mar 29;113(13):E1796-805. | ||||
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