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8PBQ

Mutant R1810Q of the dihydroorotase domain of human CAD protein bound to the substrates

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 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
ACYS1613
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

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PDB entries from 2024-11-06

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