Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T24548 | Target Info | |||
| Target Name | Aspartate carbamoyltransferase (CAD) | ||||
| Synonyms | CAD | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | CAD | ||||
| Biochemical Class | Carbon-nitrogen ligase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Lysine Nz-Carboxylic Acid | Ligand Info | |||||
| Structure Description | Human dihydroorotase mutant F1563T co-crystallized with carbamoyl aspartate at pH 7.5 | PDB:6HFQ | ||||
| Method | X-ray diffraction | Resolution | 1.15 Å | Mutation | Yes | [1] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDGPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETTSELRLDS 1570 VVQWMEHFET1580 WPSHLPIVAH1590 AEQQTVAAVL1600 MVAQLTQRSV1610 HICHVARKEE 1620 ILLIKAAKAR1630 GLPVTCEVAP1640 HHLFLSHDDL1650 ERLGPGKGEV1660 RPELGSRQDV 1670 EALWENMAVI1680 DCFASDHAPH1690 TLEEKCGSRP1700 PPGFPGLETM1710 LPLLLTAVSE 1720 GRLSLDDLLQ1730 RLHHNPRRIF1740 HLPPQEDTYV1750 EVDLEHEWTI1760 PSHMPFSKAH 1770 WTPFEGQKVK1780 GTVRRVVLRG1790 EVAYIDGQVL1800 VPPGYGQDVR1810 KWPQGAVPQL 1820 P
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HIS1471
2.598
HIS1473
2.579
MET1503
2.674
PRO1504
2.451
ASN1505
4.944
PHE1534
3.225
LEU1535
2.006
GLY1536
2.717
ALA1537
2.104
GLY1554
3.910
LEU1555
1.332
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: N-Carbamoyl-L-Aspartate | Ligand Info | |||||
| Structure Description | Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 5.5 | PDB:4C6E | ||||
| Method | X-ray diffraction | Resolution | 1.26 Å | Mutation | No | [2] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDAPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETFSELRLDS 1570 VVQWMEHFET1580 WPSHLPIVAH1590 AEQQTVAAVL1600 MVAQLTQRSV1610 HICHVARKEE 1620 ILLIKAAKAR1630 GLPVTCEVAP1640 HHLFLSHDDL1650 ERLGPGKGEV1660 RPELGSRQDV 1670 EALWENMAVI1680 DCFASDHAPH1690 TLEEKCGSRP1700 PPGFPGLETM1710 LPLLLTAVSE 1720 GRLSLDDLLQ1730 RLHHNPRRIF1740 HLPPQEDTYV1750 EVDLEHEWTI1760 PSHMPFSKAH 1770 WTPFEGQKVK1780 GTVRRVVLRG1790 EVAYIDGQVL1800 VPPGYGQDVR1810 KWPQGAVPQL 1820 PPS
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: 5-Fluoro orotate | Ligand Info | |||||
| Structure Description | Crystal structure of the dihydroorotase domain of human CAD bound to the inhibitor fluoroorotate at pH 6.0 | PDB:4C6L | ||||
| Method | X-ray diffraction | Resolution | 1.55 Å | Mutation | No | [2] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDAPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETFSELRLDS 1570 VVQWMEHFET1580 WPSHLPIVAH1590 AEQQTVAAVL1600 MVAQLTQRSV1610 HICHVARKEE 1620 ILLIKAAKAR1630 GLPVTCEVAP1640 HHLFLSHDDL1650 ERLGPGKGEV1660 RPELGSRQDV 1670 EALWENMAVI1680 DCFASDHAPH1690 TLEEKCGSRP1700 PPGFPGLETM1710 LPLLLTAVSE 1720 GRLSLDDLLQ1730 RLHHNPRRIF1740 HLPPQEDTYV1750 EVDLEHEWTI1760 PSHMPFSKAH 1770 WTPFEGQKVK1780 GTVRRVVLRG1790 EVAYIDGQVL1800 VPPGYGQDVR1810 KWPQGAVPQL 1820 PP
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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 .FOT or .FOT2 or .FOT3 or :3FOT;style chemicals stick;color identity;select .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1561 or .A:1590 or .A:1614 or .A:1660 or .A:1661 or .A:1662 or .A:1686 or .A:1688 or .A:1690 or .A:1701 or .A:1702 or .A:1703 or .A:1704; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: N-(phosphonacetyl)-L-aspartate | Ligand Info | |||||
| Structure Description | Aspartate transcarbamoylase domain of human CAD bound to PALA | PDB:5G1N | ||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [3] |
| PDB Sequence |
SLVGQHILSV
1929 QQFTKDQMSH1939 LFNVAHTLRM1949 MVQKERSLDI1959 LKGKVMASMF1969 YEVSTRTSSS 1979 FAAAMARLGG1989 AVLSFSEATS1999 SVQKGESLAD2009 SVQTMSCYAD2019 VVVLRHPQPG 2029 AVELAAKHCR2039 RPVINAGDGV2049 GEHPTQALLD2059 IFTIREELGT2069 VNGMTITMVG 2079 DLKHGRTVHS2089 LACLLTQYRV2099 SLRYVAPPSL2109 RMPPTVRAFV2119 ASRGTKQEEF 2129 ESIEEALPDT2139 DVLYMTRIQK2149 ERFGSTQEYE2159 ACFGQFILTP2169 HIMTRAKKKM 2179 VVMHPMPRVN2189 EISVEVDSDP2199 RAAYFRQAEN2209 GMYIRMALLA2219 TVLGRF |
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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 .PAL or .PAL2 or .PAL3 or :3PAL;style chemicals stick;color identity;select .A:1972 or .A:1973 or .A:1974 or .A:1975 or .A:1976 or .A:1977 or .A:2024 or .A:2052 or .A:2055 or .A:2085 or .A:2086 or .A:2146 or .A:2148 or .A:2184 or .A:2185 or .A:2186; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: Aminocarbonyl dihydrogen phosphate | Ligand Info | |||||
| Structure Description | Aspartate transcarbamoylase domain of human CAD bound to carbamoyl phosphate | PDB:5G1P | ||||
| Method | X-ray diffraction | Resolution | 3.19 Å | Mutation | No | [3] |
| PDB Sequence |
VGQHILSVQQ
1931 FTKDQMSHLF1941 NVAHTLRMMV1951 QKERSLDILK1961 GKVMASMFYE1971 VSTRTSSSFA 1981 AAMARLGGAV1991 LSFSEATSSV2001 QKGESLADSV2011 QTMSCYADVV2021 VLRHPQPGAV 2031 ELAAKHCRRP2041 VINAGDGVGE2051 HPTQALLDIF2061 TIREELGTVN2071 GMTITMVGDL 2081 KHGRTVHSLA2091 CLLTQYRVSL2101 RYVAPPSLRM2111 PPTVRAFVAS2121 GTKQEEFESI 2132 EEALPDTDVL2142 YMTRIQKERF2152 QFILTPHIMT2173 RAKKKMVVMH2183 PMPRVNEISV 2193 EVDSDPRAAY2203 FRQAENGMYI2213 RMALLATVLG2223 RF
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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 .CP or .CP2 or .CP3 or :3CP;style chemicals stick;color identity;select .A:1972 or .A:1973 or .A:1974 or .A:1975 or .A:1976 or .A:1977 or .A:2024 or .A:2052 or .A:2055 or .A:2086 or .A:2184 or .A:2185 or .A:2186; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: L-Dihydroorotic acid | Ligand Info | |||||
| Structure Description | Human dihydroorotase mutant F1563T co-crystallized with carbamoyl aspartate at pH 7.5 | PDB:6HFQ | ||||
| Method | X-ray diffraction | Resolution | 1.15 Å | Mutation | Yes | [1] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDGPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETTSELRLDS 1570 VVQWMEHFET1580 WPSHLPIVAH1590 AEQQTVAAVL1600 MVAQLTQRSV1610 HICHVARKEE 1620 ILLIKAAKAR1630 GLPVTCEVAP1640 HHLFLSHDDL1650 ERLGPGKGEV1660 RPELGSRQDV 1670 EALWENMAVI1680 DCFASDHAPH1690 TLEEKCGSRP1700 PPGFPGLETM1710 LPLLLTAVSE 1720 GRLSLDDLLQ1730 RLHHNPRRIF1740 HLPPQEDTYV1750 EVDLEHEWTI1760 PSHMPFSKAH 1770 WTPFEGQKVK1780 GTVRRVVLRG1790 EVAYIDGQVL1800 VPPGYGQDVR1810 KWPQGAVPQL 1820 P
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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 .DOR or .DOR2 or .DOR3 or :3DOR;style chemicals stick;color identity;select .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1590 or .A:1614 or .A:1660 or .A:1661 or .A:1662 or .A:1686 or .A:1688 or .A:1690 or .A:1701 or .A:1702 or .A:1703 or .A:1704; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD. J Biol Chem. 2018 Dec 7;293(49):18903-18913. | ||||
| REF 2 | Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD. Structure. 2014 Feb 4;22(2):185-98. | ||||
| REF 3 | Structure and Functional Characterization of Human Aspartate Transcarbamoylase, the Target of the Anti-tumoral Drug PALA. Structure. 2016 Jul 6;24(7):1081-94. | ||||
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