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 | Lysine Nz-Carboxylic Acid | Ligand Info | |||
| Canonical SMILES | C(CCNC(=O)O)CC(C(=O)O)N | ||||
| InChI | 1S/C7H14N2O4/c8-5(6(10)11)3-1-2-4-9-7(12)13/h5,9H,1-4,8H2,(H,10,11)(H,12,13)/t5-/m0/s1 | ||||
| InChIKey | PWIKLEYMFKCERQ-YFKPBYRVSA-N | ||||
| PubChem Compound ID | 17754054 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6HFQ Human dihydroorotase mutant F1563T co-crystallized with carbamoyl aspartate at pH 7.5 | ||||||
| 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
|
|||||
|
|
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
|
|||||
| PDB ID: 6HFJ Human dihydroorotase mutant F1563A co-crystallized with carbamoyl aspartate at pH 7.5 | ||||||
| Method | X-ray diffraction | Resolution | 1.20 Å | Mutation | Yes | [1] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDAPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETASELRLDS 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
2.579
HIS1473
2.580
MET1503
2.681
PRO1504
2.456
ASN1505
4.942
PHE1534
3.265
LEU1535
2.010
GLY1536
2.754
ALA1537
2.082
GLY1554
3.926
LEU1555
1.334
|
|||||
| PDB ID: 6HFP Human dihydroorotase mutant F1563T co-crystallized with carbamoyl aspartate at pH 7.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.20 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
|
|||||
|
|
HIS1471
2.622
HIS1473
2.587
MET1503
2.568
PRO1504
2.451
ASN1505
4.897
PHE1534
3.270
LEU1535
2.009
GLY1536
2.702
ALA1537
2.111
GLY1554
3.914
LEU1555
1.337
|
|||||
| 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 | [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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.800
HIS1473
2.612
MET1503
2.419
PRO1504
2.466
ASN1505
4.865
PHE1534
3.337
LEU1535
1.977
GLY1536
2.689
ALA1537
2.082
GLY1554
3.910
LEU1555
1.337
|
|||||
| 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 | [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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.704
HIS1473
2.582
MET1503
2.463
PRO1504
2.468
ASN1505
4.838
PHE1534
3.290
LEU1535
1.967
GLY1536
2.743
ALA1537
2.083
GLY1554
3.921
LEU1555
1.339
|
|||||
| 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 | [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 P
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.744
HIS1473
2.608
MET1503
2.437
PRO1504
2.461
ASN1505
4.875
PHE1534
3.325
LEU1535
2.864
GLY1536
2.706
ALA1537
2.092
GLY1554
4.175
LEU1555
1.330
|
|||||
| 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 | [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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.669
HIS1473
2.589
MET1503
2.577
PRO1504
2.483
ASN1505
4.864
PHE1534
3.297
LEU1535
1.972
GLY1536
2.751
ALA1537
2.088
GLY1554
3.960
LEU1555
1.339
|
|||||
| 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 | [1] |
| 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.707
HIS1473
2.587
MET1503
2.642
PRO1504
2.469
ASN1505
4.735
PHE1534
3.286
LEU1535
2.040
GLY1536
2.762
ALA1537
2.080
GLY1554
3.975
LEU1555
1.342
|
|||||
| 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 | [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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.697
HIS1473
2.580
MET1503
2.497
PRO1504
2.450
ASN1505
4.779
PHE1534
3.329
LEU1535
1.999
GLY1536
2.723
ALA1537
2.077
GLY1554
3.975
LEU1555
1.338
|
|||||
| PDB ID: 6HFL Human dihydroorotase mutant F1563L co-crystallized with carbamoyl aspartate at pH 7.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.35 Å | Mutation | Yes | [1] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDAPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETLSELRLDS 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.701
HIS1473
2.572
MET1503
2.652
PRO1504
2.468
ASN1505
4.817
PHE1534
3.258
LEU1535
2.017
GLY1536
2.733
ALA1537
2.077
GLY1554
3.939
LEU1555
1.336
|
|||||
| 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 | [1] |
| 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.719
HIS1473
2.608
MET1503
2.589
PRO1504
2.464
ASN1505
4.755
PHE1534
3.285
LEU1535
2.037
GLY1536
2.746
ALA1537
2.081
GLY1554
4.004
LEU1555
1.340
|
|||||
| 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 | [1] |
| 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.705
HIS1473
2.562
MET1503
2.650
PRO1504
2.458
ASN1505
4.736
PHE1534
3.312
LEU1535
2.048
GLY1536
2.767
ALA1537
2.083
GLY1554
4.001
LEU1555
1.343
|
|||||
| PDB ID: 6HFH Human dihydroorotase mutant F1563A co-crystallized with carbamoyl aspartate at pH 7.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.45 Å | Mutation | Yes | [1] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDAPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETASELRLDS 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.663
HIS1473
2.545
MET1503
2.656
PRO1504
2.470
ASN1505
4.855
PHE1534
3.217
LEU1535
2.025
GLY1536
2.746
ALA1537
2.110
GLY1554
3.965
LEU1555
1.340
|
|||||
| PDB ID: 6HFN Human dihydroorotase mutant F1563L co-crystallized with carbamoyl aspartate at pH 7.5 | ||||||
| Method | X-ray diffraction | Resolution | 1.45 Å | Mutation | No | [1] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDGPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETLSELRLDS 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.588
HIS1473
2.588
MET1503
2.582
PRO1504
2.471
ASN1505
4.841
PHE1534
3.258
LEU1535
1.994
GLY1536
2.724
ALA1537
2.080
GLY1554
4.014
LEU1555
1.338
|
|||||
| PDB ID: 6HFK Human dihydroorotase mutant F1563L co-crystallized with carbamoyl aspartate at pH 6.5 | ||||||
| Method | X-ray diffraction | Resolution | 1.46 Å | Mutation | Yes | [1] |
| PDB Sequence |
KLVRLPGLID
1469 VHVHLREPGG1479 THKEDFASGT1489 AAALAGGITM1499 VCAMPNTRPP1509 IIDAPALALA 1519 QKLAEAGARC1529 DFALFLGASS1539 ENAGTLGTVA1549 GSAAGLLYLN1560 ETLSELRLDS 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.697
HIS1473
2.554
MET1503
2.642
PRO1504
2.499
ASN1505
4.830
PHE1534
3.167
LEU1535
2.025
GLY1536
2.742
ALA1537
2.085
GLY1554
3.987
LEU1555
1.332
|
|||||
| 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 | [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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.637
HIS1473
2.545
MET1503
2.606
PRO1504
2.455
ASN1505
4.864
PHE1534
3.267
LEU1535
1.977
GLY1536
2.744
ALA1537
2.087
GLY1554
3.945
LEU1555
1.338
|
|||||
| PDB ID: 4C6L Crystal structure of the dihydroorotase domain of human CAD bound to the inhibitor fluoroorotate at pH 6.0 | ||||||
| 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.811
HIS1473
2.537
MET1503
2.391
PRO1504
2.498
ASN1505
4.815
PHE1534
3.257
LEU1535
1.981
GLY1536
2.713
ALA1537
2.123
GLY1554
3.973
LEU1555
1.333
|
|||||
| PDB ID: 4C6M Crystal structure of the dihydroorotase domain of human CAD bound to the inhibitor fluoroorotate at pH 7.0 | ||||||
| Method | X-ray diffraction | Resolution | 1.62 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
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1566 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.716
HIS1473
2.550
MET1503
2.586
PRO1504
2.521
ASN1505
4.874
PHE1534
3.237
LEU1535
1.985
GLY1536
2.668
ALA1537
2.067
GLY1554
3.997
LEU1555
1.342
|
|||||
| 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 | [2] |
| 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1505 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1562 or .A:1587 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS1471
2.725
HIS1473
2.580
MET1503
2.392
PRO1504
2.493
ASN1505
4.829
PHE1534
3.128
LEU1535
2.079
GLY1536
2.682
ALA1537
2.061
GLY1554
4.142
LEU1555
1.344
|
|||||
| 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 | [2] |
| 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 .KCX or .KCX2 or .KCX3 or :3KCX;style chemicals stick;color identity;select .A:1471 or .A:1473 or .A:1503 or .A:1504 or .A:1534 or .A:1535 or .A:1536 or .A:1537 or .A:1554 or .A:1555 or .A:1557 or .A:1558 or .A:1588 or .A:1589 or .A:1590 or .A:1613 or .A:1614 or .A:1686; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| 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. | ||||
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