Structure of PDB 1j79 Chain A

Receptor sequence
>1j79A (length=343) Species: 562 (Escherichia coli) [Search protein sequence]
SQVLKIRRPDDWHLHLRDGDMLKTVVPYTSEIYGRAIVMPNLAPPVTTVE
AAVAYRQRILDAVPAPHDFTPLMTCYLTDSLDPNELERGFNEGVFTAAKL
YPANATTNSSHGVTSVDAIMPVLERMEKIGMPLLVHGEVTHADIDIFDRE
ARFIESVMEPLRQRLTALKVVFEHITTKDAADYVRDGNERLAATITPQHL
MFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFQRVFLGTDSAP
HARHRKESSCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSVNGPQFY
GLPVNDTFIELVREEQQVAESIALTDDTLVPFLAGETVRWSVK
3D structure
PDB1j79 Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H16 H18 K102 H139 H177 D250
Catalytic site (residue number reindexed from 1) H13 H15 K99 H136 H174 D247
Enzyme Commision number 3.5.2.3: dihydroorotase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A H16 H18 K102 D250 H13 H15 K99 D247
BS02 ZN A K102 H139 H177 K99 H136 H174
BS03 NCD A N208 H209 V212 N205 H206 V209
Gene Ontology
Molecular Function
GO:0004151 dihydroorotase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0019856 pyrimidine nucleobase biosynthetic process
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1j79, PDBe:1j79, PDBj:1j79
PDBsum1j79
PubMed11401542
UniProtP05020|PYRC_ECOLI Dihydroorotase (Gene Name=pyrC)

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