Target Binding Site Detail
| 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 | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | N-Carbamoyl-L-Aspartate | Ligand Info | |||
| Canonical SMILES | C(C(C(=O)O)NC(=O)N)C(=O)O | ||||
| InChI | 1S/C5H8N2O5/c6-5(12)7-2(4(10)11)1-3(8)9/h2H,1H2,(H,8,9)(H,10,11)(H3,6,7,12)/t2-/m0/s1 | ||||
| InChIKey | HLKXYZVTANABHZ-REOHCLBHSA-N | ||||
| PubChem Compound ID | 93072 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4C6E Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 5.5 | ||||||
| Method | X-ray diffraction | Resolution | 1.26 Å | Mutation | No | [1] |
| 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
|
|||||
|
|
||||||
| PDB ID: 4C6F Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.5 | ||||||
| Method | X-ray diffraction | Resolution | 1.26 Å | Mutation | No | [1] |
| 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
|
|||||
|
|
HIS1471
3.493
HIS1473
2.840
ARG1475
1.933
ASN1505
2.152
TYR1558
3.290
THR1562
2.205
PHE1563
2.797
HIS1590
2.814
HIS1614
3.230
HIS1641
4.420
|
|||||
| PDB ID: 4C6D Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.30 Å | Mutation | No | [1] |
| 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 P
|
|||||
|
|
HIS1471
3.465
HIS1473
3.066
ARG1475
1.973
ASN1505
2.162
TYR1558
3.253
THR1562
2.052
PHE1563
2.792
SER1564
4.741
HIS1590
2.805
HIS1614
3.258
|
|||||
| PDB ID: 4C6J Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.5 | ||||||
| Method | X-ray diffraction | Resolution | 1.30 Å | Mutation | No | [1] |
| 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NCD or .NCD2 or .NCD3 or :3NCD;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1562 or .A:1563 or .A:1564 or .A:1590 or .A:1614 or .A:1641 or .A:1660 or .A:1661 or .A:1662 or .A:1686 or .A:1688 or .A:1690 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
|
HIS1471
3.552
HIS1473
2.945
ARG1475
1.981
ASN1505
2.158
TYR1558
3.299
THR1562
2.062
PHE1563
2.792
SER1564
4.693
HIS1590
2.687
HIS1614
3.443
|
|||||
| PDB ID: 6HFR Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at pH 7.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.30 Å | Mutation | Yes | [2] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDGPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETYSELRLDS 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NCD or .NCD2 or .NCD3 or :3NCD;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1562 or .A:1563 or .A:1564 or .A:1590 or .A:1614 or .A:1641 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
|
HIS1471
3.494
HIS1473
2.931
ARG1475
1.977
ASN1505
2.058
TYR1558
3.323
THR1562
1.971
TYR1563
2.708
SER1564
4.722
HIS1590
2.865
HIS1614
3.242
HIS1641
4.501
|
|||||
| PDB ID: 4C6I Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.35 Å | Mutation | No | [1] |
| 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NCD or .NCD2 or .NCD3 or :3NCD;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1562 or .A:1563 or .A:1564 or .A:1590 or .A:1614 or .A:1641 or .A:1660 or .A:1661 or .A:1662 or .A:1686 or .A:1688 or .A:1690 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
|
HIS1471
3.568
HIS1473
3.047
ARG1475
1.959
ASN1505
2.111
TYR1558
3.292
THR1562
1.987
PHE1563
2.747
SER1564
4.622
HIS1590
2.762
HIS1614
3.425
|
|||||
| PDB ID: 6HFS Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at pH 6.5 | ||||||
| Method | X-ray diffraction | Resolution | 1.35 Å | Mutation | Yes | [2] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDGPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETYSELRLDS 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NCD or .NCD2 or .NCD3 or :3NCD;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1562 or .A:1563 or .A:1564 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
|
HIS1471
3.440
HIS1473
2.957
ARG1475
2.001
ASN1505
2.025
TYR1558
3.347
THR1562
2.006
TYR1563
2.734
SER1564
4.754
HIS1590
2.897
HIS1614
3.228
|
|||||
| PDB ID: 6HFU Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at pH 7.5 | ||||||
| Method | X-ray diffraction | Resolution | 1.40 Å | Mutation | No | [2] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDAPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETYSELRLDS 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NCD or .NCD2 or .NCD3 or :3NCD;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1562 or .A:1563 or .A:1564 or .A:1590 or .A:1614 or .A:1641 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
|
HIS1471
3.484
HIS1473
2.893
ARG1475
1.979
ASN1505
2.070
TYR1558
3.330
THR1562
1.980
TYR1563
2.709
SER1564
4.711
HIS1590
2.814
HIS1614
3.263
HIS1641
4.521
|
|||||
| PDB ID: 4C6K Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 8.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.48 Å | Mutation | No | [1] |
| 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NCD or .NCD2 or .NCD3 or :3NCD;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1562 or .A:1563 or .A:1564 or .A:1590 or .A:1614 or .A:1641 or .A:1660 or .A:1661 or .A:1662 or .A:1686 or .A:1688 or .A:1690 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
|
HIS1471
3.559
HIS1473
2.964
ARG1475
1.977
ASN1505
2.129
TYR1558
3.186
THR1562
1.965
PHE1563
2.780
SER1564
4.553
HIS1590
2.608
HIS1614
3.551
|
|||||
| PDB ID: 4C6Q Crystal structure of the dihydroorotase domain of human CAD C1613S mutant bound to substrate at pH 7.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.66 Å | Mutation | Yes | [1] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDAPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETFSELRLDS 1570 VVQWMEHFET1580 WPSHLPIVAH1590 AEQQTVAAVL1600 MVAQLTQRSV1610 HISHVARKEE 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NCD or .NCD2 or .NCD3 or :3NCD;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1562 or .A:1563 or .A:1564 or .A:1590 or .A:1614 or .A:1641 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
|
HIS1471
3.688
HIS1473
3.079
ARG1475
1.999
ASN1505
2.195
TYR1558
3.314
THR1562
2.104
PHE1563
2.708
SER1564
4.596
HIS1590
2.632
HIS1614
3.523
HIS1641
4.561
|
|||||
| PDB ID: 4C6N Crystal structure of the dihydroorotase domain of human CAD E1637T mutant bound to substrate at pH 6.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | Yes | [1] |
| PDB Sequence |
LVRLPGLIDV
1470 HVHLREPGGT1480 HKEDFASGTA1490 AALAGGITMV1500 CAMPNTRPPI1510 IDAPALALAQ 1520 KLAEAGARCD1530 FALFLGASSE1540 NAGTLGTVAG1550 SAAGLLYLNE1561 TFSELRLDSV 1571 VQWMEHFETW1581 PSHLPIVAHA1591 EQQTVAAVLM1601 VAQLTQRSVH1611 ICHVARKEEI 1621 LLIKAAKARG1631 LPVTCTVAPH1641 HLFLSHDDLE1651 RLGPGKGEVR1661 PELGSRQDVE 1671 ALWENMAVID1681 CFASDHAPHT1691 LEEKCGSRPP1701 PGFPGLETML1711 PLLLTAVSEG 1721 RLSLDDLLQR1731 LHHNPRRIFH1741 LPPQEDTYVE1751 VDLEHEWTIP1761 SHMPFSKAHW 1771 TPFEGQKVKG1781 TVRRVVLRGE1791 VAYIDGQVLV1801 PPGYGQDVRK1811 WPQGAVPQLP 1821 PS
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NCD or .NCD2 or .NCD3 or :3NCD;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1475 or .A:1505 or .A:1558 or .A:1562 or .A:1563 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:1702 or .A:1703; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD. Structure. 2014 Feb 4;22(2):185-98. | ||||
| REF 2 | 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. | ||||
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