Structure of PDB 1jlr Chain B Binding Site BS02

Receptor Information
>1jlr Chain B (length=235) Species: 5811 (Toxoplasma gondii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LLVDPRYSTNDQEESILQDIITRFPNVVLMKQTAQLRAMMTIIRDKETPK
EEFVFYADRLIRLLIEEALNELPFQKKEVTTPLDVSYHGVSFYSKICGVS
IVRAGESMESGLRAVCRGVRIGKILIQRDETTAEPKLIYEKLPADIRERW
VMLLDPMCATAGSVCKAIEVLLRLGVKEERIIFVNILAAPQGIERVFKEY
PKVRMVTAAVDICLNSRYYIVPGIGDFGDRYFGTM
Ligand information
Ligand IDGTP
InChIInChI=1S/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKeyXKMLYUALXHKNFT-UUOKFMHZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.370NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.370NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
OpenEye OEToolkits 1.7.6c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
FormulaC10 H16 N5 O14 P3
NameGUANOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL1233147
DrugBankDB04137
ZINCZINC000060094177
PDB chain1jlr Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1jlr The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase.
Resolution2.45 Å
Binding residue
(original residue number in PDB)		F101 Y102 S103 K104 I105 C125 R129 R158
Binding residue
(residue number reindexed from 1)		F92 Y93 S94 K95 I96 C116 R120 R149
Annotation score2
Binding affinityMOAD: Kd=465uM
Enzymatic activity
Catalytic site (original residue number in PDB) R137 T141 D235 D238
Catalytic site (residue number reindexed from 1) R128 T132 D226 D229
Enzyme Commision number 2.4.2.9: uracil phosphoribosyltransferase.
Gene Ontology
Molecular Function
GO:0004845 uracil phosphoribosyltransferase activity
GO:0005525 GTP binding
GO:0016757 glycosyltransferase activity
Biological Process
GO:0044206 UMP salvage
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jlr, PDBe:1jlr, PDBj:1jlr
PDBsum1jlr
PubMed11773618
UniProtQ26998|UPP_TOXGO Uracil phosphoribosyltransferase (Gene Name=uprt)

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