Structure of PDB 1j79 Chain B Binding Site BS01

Receptor Information
>1j79 Chain B (length=339) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SQVLKIRRPDDWHLHLRDGDMLKTVVPYTSEIYGRAIVMPNLAPPVTTVE
AAVAYRQRILDAVPAPHDFTPLMTCYLTDSLDPNELERGFNEGVFTAAKL
YPANASHGVTSVDAIMPVLERMEKIGMPLLVHGEVTHADIDIFDREARFI
ESVMEPLRQRLTALKVVFEHITTKDAADYVRDGNERLAATITPQHLMFNR
NHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFQRVFLGTDSAPHARH
RKESSCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSVNGPQFYGLPV
NDTFIELVREEQQVAESIALTDDTLVPFLAGETVRWSVK
Ligand information
Ligand IDNCD
InChIInChI=1S/C5H8N2O5/c6-5(12)7-2(4(10)11)1-3(8)9/h2H,1H2,(H,8,9)(H,10,11)(H3,6,7,12)/t2-/m0/s1
InChIKeyHLKXYZVTANABHZ-REOHCLBHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)N[C@@H](CC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0C([C@@H](C(=O)O)NC(=O)N)C(=O)O
ACDLabs 10.04O=C(O)C(NC(=O)N)CC(=O)O
OpenEye OEToolkits 1.5.0C(C(C(=O)O)NC(=O)N)C(=O)O
CACTVS 3.341NC(=O)N[CH](CC(O)=O)C(O)=O
FormulaC5 H8 N2 O5
NameN-CARBAMOYL-L-ASPARTATE
ChEMBL
DrugBankDB04252
ZINCZINC000000895230
PDB chain1j79 Chain A Residue 950 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1j79 Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		A145 R152
Binding residue
(residue number reindexed from 1)		A138 R145
Annotation score5
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 H132 H170 D243
Enzyme Commision number 3.5.2.3: dihydroorotase.
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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Molecular Function
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Biological Process
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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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