Structure of PDB 4z87 Chain C Binding Site BS02

Receptor Information
>4z87 Chain C (length=495) Species: 284811 (Eremothecium gossypii ATCC 10895) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TYRDAATALEHLATYAEKDGLSVEQLMDSGGLTYNDFLVLPGKIDFPSSE
VVLSSRLTKKITLNAPFVSSPMDTVTEADMAIHMALLGGIGIIHHNCTAE
EQAEMVRRVKKYENGFINAPVVVGPDATVADVRRMKNEFGFAGFPVTDDG
KPGKLQGIITSRDIQFVEDETLLVSEIMTKDVITGKQGINLEEANQILKN
TKKGKLPIVDEAGCLVSMLSRTDLMKNQSYPLASKSADTKQLLCGAAIGT
IDADRQRLAMLVEAGLDVVVLDSSQGNSVFQINMIKWIKETFPDLQVIAG
NVVTREQAASLIHAGADGLRIGMGSGSICITQEVMACGRPQGTAVYNVTQ
FANQFGVPCIADGGVQNIGHITKAIALGASTVMMGGMLAGTTESPGEYFF
DGKRLKTYRGMGSIDAMQVLVAQGVTGSVIDKGSIKKYIPYLYNGLQHSC
QDIGVRSLVEFREKVDSGSVRFEFRTPSAQLEGGVHNLHSYEKLF
Ligand information
Ligand IDGDP
InChIInChI=1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKeyQGWNDRXFNXRZMB-UUOKFMHZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.385NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.385NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
FormulaC10 H15 N5 O11 P2
NameGUANOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL384759
DrugBankDB04315
ZINCZINC000008215481
PDB chain4z87 Chain C Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4z87 Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.
Resolution2.25 Å
Binding residue
(original residue number in PDB)		T165 D168 T184 D186 I188 K208 G209
Binding residue
(residue number reindexed from 1)		T160 D163 T179 D181 I183 K203 G204
Annotation score2
Binding affinityMOAD: Ki=210uM
Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0005524 ATP 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:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4z87, PDBe:4z87, PDBj:4z87
PDBsum4z87
PubMed26558346
UniProtQ756Z6

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