Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T16514 | Target Info | |||
| Target Name | Fatty acid synthase (FASN) | ||||
| Synonyms | Yeast fatty acid synthase; Fatty-acyl-CoA synthase; Fatty acyl-CoA synthetase enzyme; FAS | ||||
| Target Type | Successful Target | ||||
| Gene Name | FASN | ||||
| Biochemical Class | Acyltransferase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | NADPH | Ligand Info | |||
| Canonical SMILES | C1C=CN(C=C1C(=O)N)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OCC3C(C(C(O3)N4C=NC5=C(N=CN=C54)N)OP(=O)(O)O)O)O)O | ||||
| InChI | 1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 | ||||
| InChIKey | ACFIXJIJDZMPPO-NNYOXOHSSA-N | ||||
| PubChem Compound ID | 5884 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5C37 Structure of the beta-ketoacyl reductase domain of human fatty acid synthase bound to a spiro-imidazolone inhibitor | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | Yes | [1] |
| PDB Sequence |
EQQVPILEKF
1117 CFTPHTEEGC1127 LSERAALQEE1137 LQLCKGLVQA1147 LQTKAQIPRD1172 PSQQELPRLL 1182 SAACRLQLNG1192 NLQLELAQVL1202 AQERPKLPED1212 PLLSGLLDSP1222 ALKACLDTAV 1232 ENMPSLKMKV1242 VEVLAGHGHL1252 YSRIPGLLSP1262 HPLLQLSYTA1272 TDRHPQALEA 1282 AQAELQQHDV1292 AQGQWDPADP1302 APSALGSADL1312 LVCNCAVAAL1322 GDPASALSNM 1332 VAALREGGFL1342 LLHTLLRGHP1352 LGDIVAFLTS1362 GQGILSQDAW1377 ESLFSRVSLR 1387 LVGLKKSFYG1397 STLFLCRRPT1407 PQDSPIFLPV1417 DDTSFRWVES1427 LKGILADEDS 1437 SRPVWLKAIN1447 CATSGVVGLV1457 NCLRREPGGN1467 RLRCVLLSNL1477 SSTSHVPEVD 1487 PGSAELQKVL1497 QGDLVMNVYR1507 DGAWGAFRHF1517 LLEEDSKTGC1881 PAHKSYIIAG 1891 GLGGFGLELA1901 QWLIQRGVQK1911 LVLTSRSGIR1921 TGYQAKQVRR1931 WRRQGVQVQV 1941 STSNISSLEG1951 ARGLIAEAAQ1961 LGPVGGVFNL1971 AVVLRDGLLE1981 NQTPEFFQDV 1991 CKPKYSGTLN2001 LDRVTREACP2011 ELDYFVVFSS2021 VSCGRGNAGQ2031 SNYGFANSAM 2041 ERICEKRRHE2051 GLPGLAVQWG2061 AIGDVGILVE2071 TMSTNDTIVS2081 GTLPQRMASC 2091 LEVLDLFLNQ2101 PHMVLSSFVL2111 AE
|
|||||
|
|
ALA1890
4.023
GLY1891
2.581
GLY1892
4.538
LEU1893
4.522
GLY1894
2.432
GLY1895
2.347
PHE1896
2.031
GLY1897
3.666
THR1915
2.307
SER1916
2.939
ARG1917
1.817
SER1918
3.627
GLY1919
4.974
GLN1925
4.596
ASN1945
2.146
ILE1946
3.396
SER1947
3.010
ASN1970
3.830
LEU1971
2.435
ALA1972
2.545
VAL1973
2.006
VAL1974
2.690
LYS1993
4.889
PRO1994
2.486
LYS1995
1.952
PHE2019
2.579
SER2020
2.338
SER2021
2.261
VAL2022
3.596
SER2023
4.899
TYR2034
1.800
ASN2038
3.860
MET2041
4.659
TRP2060
2.423
GLY2061
2.398
ALA2062
3.351
ILE2063
2.265
VAL2066
4.332
GLY2067
2.670
ILE2068
2.199
LEU2069
2.348
VAL2070
4.419
|
|||||
| PDB ID: 6NNA Human Fatty Acid Synthase Psi/KR Tri-Domain with NADPH and Compound 22 | ||||||
| Method | X-ray diffraction | Resolution | 2.26 Å | Mutation | Yes | [2] |
| PDB Sequence |
QQVPILEKFC
1118 FTPHTEEGCL1128 SERAALQEEL1138 QLCKGLVQAL1148 QTPSQQELPR1180 LLSAACRLAQ 1200 VLAQERPKLP1210 EDPLLSGLLD1220 SPALKACLDT1230 AVENMPSLKM1240 KVVEVLAGHG 1250 HLYSRIPGLL1260 SPHPLLQLSY1270 TATDRHPQAL1280 EAAQAELQQH1290 DVAQGQWDPA 1300 DPAPSALGSA1310 DLLVCNCAVA1320 ALGDPASALS1330 NMVAALREGG1340 FLLLHTLLRG 1350 HPLGDIVAFL1360 TSQGILSQDA1376 WESLFSRVSL1386 RLVGLKKSFY1396 GSTLFLCRRP 1406 TPQDSPIFLP1416 VDDTSFRWVE1426 SLKGILADED1436 SARPVWLKAI1446 NCATSGVVGL 1456 VNCLRREPGG1466 NRLRCVLLSN1476 LSSTSHVPEV1486 DPGSAELQKV1496 LQGDLVMNVY 1506 RDGAWGAFRH1516 FLLEEDSKTF1880 PAHKSYIIAG1891 GLGGFGLELA1901 QWLIQRGVQK 1911 LVLTSRSGIR1921 TGYQAKQVRR1931 WRRQGVQVQV1941 STSNISSLEG1951 ARGLIAEAAQ 1961 LGPVGGVFNL1971 AVVLRDGLLE1981 NQTPEFFQDV1991 CKPKYSGTLN2001 LDRVTREACP 2011 ELDYFVVFSS2021 VSCGRGNAGQ2031 SNYGFANSAM2041 ERICEKRRHE2051 GLPGLAVQWG 2061 AIGDVGILVE2071 DTIVSGTLPQ2086 RMASCLEVLD2096 LFLNQPHMVL2106 SSFVLAE |
|||||
|
|
ALA1890
4.647
GLY1891
3.536
LEU1893
4.429
GLY1894
3.198
GLY1895
2.942
PHE1896
2.908
GLY1897
4.239
THR1915
3.284
SER1916
2.684
ARG1917
2.804
SER1918
3.472
GLY1919
4.616
ARG1921
4.104
SER1944
4.829
ASN1945
2.950
ILE1946
4.522
SER1947
3.684
ASN1970
4.280
LEU1971
3.412
|
|||||
| PDB ID: 4PIV Human Fatty Acid Synthase Psi/KR Tri-Domain with NADPH and GSK2194069 | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | Yes | [3] |
| PDB Sequence |
MQVPILEKFC
1118 FTPHTEEGCL1128 SERAALQEEL1138 QLCKGLVQAL1148 QTPSQQELPR1180 LLSAACRLAQ 1200 VLAQERPKLP1210 EDPLLSGLLD1220 SPALKACLDT1230 AVENMPSLKM1240 KVVEVLAGHG 1250 HLYSRIPGLL1260 SPHPLLQLSY1270 TATDRHPQAL1280 EAAQAELQQH1290 DVAQGQWDPA 1300 DPAPSALGSA1310 DLLVCNCAVA1320 ALGDPASALS1330 NMVAALREGG1340 FLLLHTLLRG 1350 HPLGDIVAFL1360 TSQGILSQDA1376 WESLFSRVSL1386 RLVGLKKSFY1396 GSTLFLCRRP 1406 TPQDSPIFLP1416 VDDTSFRWVE1426 SLKGILADED1436 SARPVWLKAI1446 NCATSGVVGL 1456 VNCLRREPGG1466 NRLRCVLLSN1476 LSSTSHVPEV1486 DPGSAELQKV1496 LQGDLVMNVY 1506 RDGAWGAFRH1516 FLLEEDSKTF1880 CPAHKSYIIA1890 GGLGGFGLEL1900 AQWLIQRGVQ 1910 KLVLTSRSGI1920 RTGYQAKQVR1930 RWRRQGVQVQ1940 VSTSNISSLE1950 GARGLIAEAA 1960 QLGPVGGVFN1970 LAVVLRDGLL1980 ENQTPEFFQD1990 VCKPKYSGTL2000 NLDRVTREAC 2010 PELDYFVVFS2020 SVSCGRGNAG2030 QSNYGFANSA2040 MERICEKRRH2050 EGLPGLAVQW 2060 GAIGDVGILV2070 ETNDTIVSGT2083 LPQRMASCLE2093 VLDLFLNQPH2103 MVLSSFVLAE 2113
|
|||||
|
|
ALA1890
4.710
GLY1891
3.555
LEU1893
4.591
GLY1894
3.174
GLY1895
2.905
PHE1896
2.837
GLY1897
4.235
THR1915
3.408
SER1916
2.834
ARG1917
2.896
SER1918
2.850
GLY1919
4.492
ARG1921
3.873
SER1944
4.880
ASN1945
2.910
ILE1946
4.682
SER1947
3.496
ASN1970
4.220
LEU1971
3.409
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Design and Synthesis of a Series of Bioavailable Fatty Acid Synthase (FASN) KR Domain Inhibitors for Cancer Therapy | ||||
| REF 2 | Discovery and optimization of novel piperazines as potent inhibitors of fatty acid synthase (FASN). Bioorg Med Chem Lett. 2019 Apr 15;29(8):1001-1006. | ||||
| REF 3 | A human fatty acid synthase inhibitor binds beta-ketoacyl reductase in the keto-substrate site. Nat Chem Biol. 2014 Sep;10(9):774-9. | ||||
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