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4YIW

DIHYDROOROTASE FROM BACILLUS ANTHRACIS WITH SUBSTRATE BOUND

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
B0004038molecular_functionallantoinase activity
B0004151molecular_functiondihydroorotase activity
B0005737cellular_componentcytoplasm
B0006145biological_processpurine nucleobase catabolic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0044205biological_process'de novo' UMP biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 501
ChainResidue
AHIS59
AHIS61
AASP151
AASP304
AZN502
ANCD503

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 502
ChainResidue
AZN501
ANCD503
AASP151
AHIS178
AHIS231

site_idAC3
Number of Residues11
Detailsbinding site for residue NCD A 503
ChainResidue
AHIS61
AARG63
AASN93
AMET276
AASN277
AASP304
AHIS308
APHE322
AGLY323
AZN501
AZN502

site_idAC4
Number of Residues6
Detailsbinding site for residue ZN B 501
ChainResidue
BHIS59
BHIS61
BASP151
BASP304
BZN502
BNCD503

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN B 502
ChainResidue
BASP151
BHIS178
BHIS231
BZN501
BNCD503

site_idAC6
Number of Residues14
Detailsbinding site for residue NCD B 503
ChainResidue
BHIS61
BARG63
BASN93
BGLY152
BHIS178
BMET276
BASN277
BASP304
BALA306
BHIS308
BPHE322
BGLY323
BZN501
BZN502

Functional Information from PROSITE/UniProt
site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DVHVHLReP
ChainResidueDetails
AASP57-PRO65

site_idPS00483
Number of Residues12
DetailsDIHYDROOROTASE_2 Dihydroorotase signature 2. ATDhAPHtaeeK
ChainResidueDetails
AALA302-LYS313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27499369","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21045288","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27499369","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YIW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27499369","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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