Structure of PDB 6lk4 Chain A Binding Site BS01

Receptor Information
>6lk4 Chain A (length=424) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FNESASIPTGLTYDDVLIIPQHSRVTSRKEVNTTTRLSRNVKLSIPIVAS
NMDTVCEQRMAVAMAREGGIGILHRFCSIEEQCAMLREVKRAQSFLIESP
RIILPHETAREAWEGLNWKGRVGGVGCLLVVNCKNERKLLGIITRHDLKL
ADESTTVESLMTPVDKMVVSTNTSISLEEVTHLMRKGRTANVPIVGQNGQ
LLYLVTLSDVVKLRKNKQASLDSRGRLLVGAAVGVKKDDMNRAIRLVEAG
ADVLVVDIAHGHSDLCINMVKRLKGDPRTASVDIIAGNIASAEAAEALID
AGADGLKIGVGPGSICITRLVAGAGVPQLSAVLACTRVARRRGVPCIADG
GLRTSGDISKAIGAGADTVMLGNMLAGTDEAPCKGPVGPIVRQLVGGLRS
GMSYSGAKSIEEMQRRTRFVRMTG
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 chain6lk4 Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6lk4 Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-beta-synthase domain.
Resolution2.503 Å
Binding residue
(original residue number in PDB)		R93 I99 P102 R103 R123 V127 G128 C129 L206 S210 D211 K214
Binding residue
(residue number reindexed from 1)		R91 I97 P100 R101 R121 V125 G126 C127 L204 S208 D209 K212
Annotation score2
Binding affinityMOAD: Kd=6.75uM
Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003920 GMP reductase activity
GO:0003938 IMP dehydrogenase activity
GO:0005525 GTP binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006183 GTP biosynthetic process
Cellular Component
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0020015 glycosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6lk4, PDBe:6lk4, PDBj:6lk4
PDBsum6lk4
PubMed32296055
UniProtQ57ZS7

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