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4C6Q

Crystal structure of the dihydroorotase domain of human CAD C1613S mutant bound to substrate at pH 7.0

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ORO A 2823
ChainResidue
AHIS1473
AHIS1690
APRO1702
AGLY1703
AHOH2092
AZN2825
AARG1475
AASN1505
ATHR1562
APHE1563
AHIS1590
AVAL1660
AARG1661
AALA1688

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 2824
ChainResidue
AHIS1471
AHIS1473
AKCX1556
AASP1686
AHOH2092
AZN2825
ANCD2826

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 2825
ChainResidue
AKCX1556
AHIS1590
AHIS1614
AHOH2092
AORO2823
AZN2824
ANCD2826

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NCD A 2826
ChainResidue
AHIS1471
AHIS1473
AARG1475
AASN1505
AKCX1556
ATHR1562
APHE1563
AHIS1590
AHIS1614
AVAL1660
AARG1661
AASP1686
AALA1688
AHIS1690
APRO1702
AGLY1703
AHOH2092
AZN2824
AZN2825

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 2827
ChainResidue
APRO1586
AILE1587
AARG1608
ASER1609
AVAL1610
AHIS1611
AHOH2215
AHOH2242

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT A 2828
ChainResidue
AVAL1470
AHIS1471
AMET1503
APHE1534
AVAL1588
AHIS1611
ASER1613
AGLU1637
APHE1740

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 2829
ChainResidue
AHIS1734
AHIS1734
AARG1737
AARG1737

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 2830
ChainResidue
AGLN1604
ALEU1605
AARG1630
AHOH2236

Functional Information from PROSITE/UniProt
site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DVHVHLReP
ChainResidueDetails
AASP1469-PRO1477

site_idPS00483
Number of Residues12
DetailsDIHYDROOROTASE_2 Dihydroorotase signature 2. ASDhAPHtleeK
ChainResidueDetails
AALA1684-LYS1695

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For DHOase activity => ECO:0000250|UniProtKB:P05020
ChainResidueDetails
AASP1686

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
ChainResidueDetails
AHIS1471
AHIS1473
AHIS1590
ASER1613
AHIS1614
AGLU1637
AASP1686

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q
ChainResidueDetails
AARG1475
AASN1505
AARG1661
AHIS1690
APRO1702

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: via carbamate group => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D
ChainResidueDetails
AKCX1556

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:24332717
ChainResidueDetails
AKCX1556

218853

PDB entries from 2024-04-24

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