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3D6N

Crystal Structure of Aquifex Dihydroorotase Activated by Aspartate Transcarbamoylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004038molecular_functionallantoinase activity
A0004151molecular_functiondihydroorotase activity
A0005737cellular_componentcytoplasm
A0006145biological_processpurine nucleobase catabolic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0008270molecular_functionzinc ion binding
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
A0044205biological_process'de novo' UMP biosynthetic process
A0046872molecular_functionmetal ion binding
B0004070molecular_functionaspartate carbamoyltransferase activity
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006520biological_processamino acid metabolic process
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 423
ChainResidue
AHIS61
AHIS63
AASP153
AASP305

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FLC A 424
ChainResidue
AHIS180
AHIS232
AASN278
AASP305
AALA307
AHIS309
APRO322
AGLY323
AHIS63
AARG65
AASN95
AASP153
AGLY154

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FLC B 292
ChainResidue
BTHR48
BARG97
BHIS126
BARG159
BARG213
BGLY251

Functional Information from PROSITE/UniProt
site_idPS00097
Number of Residues8
DetailsCARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FsEpSTRT
ChainResidueDetails
BPHE41-THR48

site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DIHVHLRdP
ChainResidueDetails
AASP59-PRO67

site_idPS00483
Number of Residues12
DetailsDIHYDROOROTASE_2 Dihydroorotase signature 2. ATDhAPHqtfeK
ChainResidueDetails
AALA303-LYS314

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15826652","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19128030","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24314009","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XRF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XRT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D6N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BJH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24314009","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4BJH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19128030","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24314009","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D6N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BJH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1at1
ChainResidueDetails
BARG97
BTHR48
BARG47
BHIS126

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1at1
ChainResidueDetails
AASP305

246704

PDB entries from 2025-12-24

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