4C6J

Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 7.5

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Functional Information from GO Data

ChainGOidnamespacecontents
A0042995cellular_componentcell projection
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0070062cellular_componentextracellular exosome
A0016020cellular_componentmembrane
A0043025cellular_componentneuronal cell body
A0016363cellular_componentnuclear matrix
A0005654cellular_componentnucleoplasm
A0005634cellular_componentnucleus
A0032991cellular_componentprotein-containing complex
A0043195cellular_componentterminal bouton
A0070335molecular_functionaspartate binding
A0004070molecular_functionaspartate carbamoyltransferase activity
A0005524molecular_functionATP binding
A0004088molecular_functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
A0004151molecular_functiondihydroorotase activity
A0019899molecular_functionenzyme binding
A0042802molecular_functionidentical protein binding
A0004672molecular_functionprotein kinase activity
A0008270molecular_functionzinc ion binding
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0044205biological_process'de novo' UMP biosynthetic process
A0031100biological_processanimal organ regeneration
A0035690biological_processcellular response to drug
A0071364biological_processcellular response to epidermal growth factor stimulus
A0019240biological_processcitrulline biosynthetic process
A0017144biological_processdrug metabolic process
A0007565biological_processfemale pregnancy
A0006541biological_processglutamine metabolic process
A0007507biological_processheart development
A0007595biological_processlactation
A0001889biological_processliver development
A0006807biological_processnitrogen compound metabolic process
A0018107biological_processpeptidyl-threonine phosphorylation
A0046777biological_processprotein autophosphorylation
A0046134biological_processpyrimidine nucleoside biosynthetic process
A0014075biological_processresponse to amine
A0031000biological_processresponse to caffeine
A0051414biological_processresponse to cortisol
A0032868biological_processresponse to insulin
A0042594biological_processresponse to starvation
A0033574biological_processresponse to testosterone
A0006228biological_processUTP biosynthetic process
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC17BINDING SITE FOR RESIDUE ZN A 2823
ChainResidue
AHIS1471
AHIS1473
AKCX1556
AASP1686
AHOH2087
AZN2824
ADOR2826

AC26BINDING SITE FOR RESIDUE ZN A 2824
ChainResidue
AKCX1556
AHIS1590
AHIS1614
AHOH2087
AZN2823
ADOR2826

AC34BINDING SITE FOR RESIDUE ZN A 2825
ChainResidue
AHIS1471
ACYS1613
AGLU1637
AHOH2086

AC415BINDING SITE FOR RESIDUE DOR A 2826
ChainResidue
AHIS1473
AARG1475
AASN1505
ATHR1562
APHE1563
AHIS1590
AVAL1660
AARG1661
AALA1688
AHIS1690
APRO1702
AGLY1703
AHOH2087
AZN2823
AZN2824

AC58BINDING SITE FOR RESIDUE FMT A 2828
ChainResidue
APRO1586
AILE1587
AARG1608
ASER1609
AVAL1610
AHIS1611
AHOH2205
AHOH2235

AC64BINDING SITE FOR RESIDUE FMT A 2829
ChainResidue
AHIS1734
AHIS1734
AARG1737
AARG1737

AC74BINDING SITE FOR RESIDUE FMT A 2830
ChainResidue
AGLN1604
ALEU1605
AARG1630
AHOH2229

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
NCD_4c6j_A_282721N-CARBAMOYL-L-ASPARTATE binding site
ChainResidueligand
AHIS1471NCD: N-CARBAMOYL-L-ASPARTATE
AHIS1473NCD: N-CARBAMOYL-L-ASPARTATE
AARG1475NCD: N-CARBAMOYL-L-ASPARTATE
AASN1505NCD: N-CARBAMOYL-L-ASPARTATE
AKCX1556NCD: N-CARBAMOYL-L-ASPARTATE
ATYR1558NCD: N-CARBAMOYL-L-ASPARTATE
ATHR1562-SER1564NCD: N-CARBAMOYL-L-ASPARTATE
AHIS1590NCD: N-CARBAMOYL-L-ASPARTATE
AHIS1614NCD: N-CARBAMOYL-L-ASPARTATE
AHIS1641NCD: N-CARBAMOYL-L-ASPARTATE
AVAL1660-PRO1662NCD: N-CARBAMOYL-L-ASPARTATE
AASP1686NCD: N-CARBAMOYL-L-ASPARTATE
AALA1688NCD: N-CARBAMOYL-L-ASPARTATE
AHIS1690NCD: N-CARBAMOYL-L-ASPARTATE
APRO1702-PHE1704NCD: N-CARBAMOYL-L-ASPARTATE

DOR_4c6j_A_282621(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID binding site
ChainResidueligand
AHIS1471DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AHIS1473DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AARG1475DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AASN1505DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AKCX1556DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
ATYR1558DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
ATHR1562-SER1564DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AHIS1590DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AHIS1614DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AVAL1660-PRO1662DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AASP1686DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AALA1688DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
AHIS1690DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID
APRO1701-PHE1704DOR: (4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC ACID

FMT_4c6j_A_282810FORMIC ACID binding site
ChainResidueligand
ALEU1585-VAL1588FMT: FORMIC ACID
AARG1608-HIS1611FMT: FORMIC ACID
ATHR1635FMT: FORMIC ACID
AILE1739FMT: FORMIC ACID

FMT_4c6j_A_28303FORMIC ACID binding site
ChainResidueligand
AGLN1604FMT: FORMIC ACID
AARG1630FMT: FORMIC ACID
ALEU1632FMT: FORMIC ACID

FMT_4c6j_A_28294FORMIC ACID binding site
ChainResidueligand
AHIS1733-HIS1734FMT: FORMIC ACID
AARG1737-ARG1738FMT: FORMIC ACID

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI13For GATase activity (By similarity).
ChainResidueDetails
ANA*
ANA*
ANA*

SWS_FT_FI22Zinc
ChainResidueDetails
AHIS18
AHIS20

SWS_FT_FI31Zinc (Probable)
ChainResidueDetails
AHIS137

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Catalytic Information from CSA

site_idNumber of ResiduesDetails