Structure of PDB 7pmz Chain G Binding Site BS01

Receptor Information
>7pmz Chain G (length=426) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GVPEKFATLGLTYDDVLLLPGASAVLPNAVDTSSRISRNVRVNIPLLSAA
MDKVTESRMAISMARQGGVGVLHRNLSIEDQANQVDLVKRSESGMVANPI
TIHPDATLGEADALCAKFRISGVPVTDGKLLGIVTNRDMAFETDRSRQVR
EVMTPMPLVTGQVGISGVDAMELLRRHKIEKLPLVDGDGILKGLITVKDF
VKAEQYPHAAKDAKGRLLVGAAVGASPEALDRAQALAEAGVDFLVVDTSH
GHNSNALSWMSKIKSSVGIDVVGGNVATRDGAQALIDAGVDGIKVGVGPG
SICTTRVVAGIGVPQVTAIYEASLAARAAGVPLIGDGGLQYSGDIGKALA
AGADTVMLGSLLAGCEESPGELQFINGKQFKVPYRGPLANVLHQLVGGLR
QTMGYVGAATIEEMESKGRFVRITSA
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[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
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain7pmz Chain G Residue 600 [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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PDB7pmz Diversity of mechanisms to control bacterial GTP homeostasis by the mutually exclusive binding of adenine and guanine nucleotides to IMP dehydrogenase.
Resolution2.03 Å
Binding residue
(original residue number in PDB)		S127 T143 N144 R145 D146 T162 L166 V167 I187 E188 K189
Binding residue
(residue number reindexed from 1)		S121 T135 N136 R137 D138 T154 L158 V159 I179 E180 K181
Annotation score3
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7pmz, PDBe:7pmz, PDBj:7pmz
PDBsum7pmz
PubMed35481629
UniProtQ9L0I7

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