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3PNU

2.4 Angstrom Crystal Structure of Dihydroorotase (pyrC) from Campylobacter jejuni.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004151molecular_functiondihydroorotase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A0019856biological_processpyrimidine nucleobase biosynthetic process
A0044205biological_process'de novo' UMP biosynthetic process
A0046872molecular_functionmetal ion binding
B0004151molecular_functiondihydroorotase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0019856biological_processpyrimidine nucleobase biosynthetic process
B0044205biological_process'de novo' UMP biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 336
ChainResidue
AKCX92
AHIS131
AHIS165
AZN337
AHOH447

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 337
ChainResidue
AZN336
AHOH447
AHIS10
AHIS12
AKCX92
AASP237

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 338
ChainResidue
AGLU78
ATYR82

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 336
ChainResidue
BKCX92
BHIS131
BHIS165
BZN337
BHOH466

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 337
ChainResidue
BHIS10
BHIS12
BKCX92
BASP237
BZN336
BHOH466

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 338
ChainResidue
BGLU78
BTYR82

Functional Information from PROSITE/UniProt
site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DMHLHLRdN
ChainResidueDetails
AASP8-ASN16

site_idPS00483
Number of Residues12
DetailsDIHYDROOROTASE_2 Dihydroorotase signature 2. GSDsAPHpkdtK
ChainResidueDetails
AGLY235-LYS246

246704

PDB entries from 2025-12-24

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