Structure of PDB 2eg8 Chain A Binding Site BS03

Receptor Information
>2eg8 Chain A (length=343) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SQVLKIRRPDDWHLHLRDGDMLKTVVPYTSEIYGRAIVMPNLAPPVTTVE
AAVAYRQRILDAVPAGHDFTPLMTCYLTDSLDPNELERGFNEGVFTAAKL
YPANATTNSSHGVTSVDAIMPVLERMEKIGMPLLVHGEVTHADIDIFDRE
ARFIESVMEPLRQRLTALKVVFEHITTKDAADYVRDGNERLAATITPQHL
MFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFNRVFLGTDSAP
HARHRKESSCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSVNGPQFY
GLPVNDTFIELVREEQQVAESIALTDDTLVPFLAGETVRWSVK
Ligand information
Ligand IDFOT
InChIInChI=1S/C5H3FN2O4/c6-1-2(4(10)11)7-5(12)8-3(1)9/h(H,10,11)(H2,7,8,9,12)
InChIKeySEHFUALWMUWDKS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1(=C(NC(=O)NC1=O)C(=O)O)F
ACDLabs 10.04O=C(O)C1=C(F)C(=O)NC(=O)N1
CACTVS 3.341OC(=O)C1=C(F)C(=O)NC(=O)N1
FormulaC5 H3 F N2 O4
Name5-FLUORO-2,6-DIOXO-1,2,3,6-TETRAHYDROPYRIMIDINE-4-CARBOXYLIC ACID;
5-FLUOROOROTIC ACID
ChEMBLCHEMBL1232805
DrugBank
ZINCZINC000001663959
PDB chain2eg8 Chain A Residue 410 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2eg8 Structures of Ligand-free and Inhibitor Complexes of Dihydroorotase from Escherichia coli: Implications for Loop Movement in Inhibitor Design
Resolution2.2 Å
Binding residue
(original residue number in PDB)		R20 N44 H139 C221 L222 H254 A266 G267
Binding residue
(residue number reindexed from 1)		R17 N41 H136 C218 L219 H251 A263 G264
Annotation score1
Binding affinityMOAD: Ki=31.8uM
PDBbind-CN: -logKd/Ki=4.50,Ki=31.8uM
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.
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:2eg8, PDBe:2eg8, PDBj:2eg8
PDBsum2eg8
PubMed17550785
UniProtP05020|PYRC_ECOLI Dihydroorotase (Gene Name=pyrC)

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