Structure of PDB 5upy Chain A Binding Site BS01

Receptor Information
>5upy Chain A (length=350) Species: 169963 (Listeria monocytogenes EGD-e) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NAMWETKFAKEGLTFDDVLLVPAKSDVLPNDVDLSVEMAPSLKLNVPIWS
AGMDTITEAKMAIAIARQGGIGVVHKNMSIEQQAEEIEKVKRSGGLLAAA
AVGITNDTFVRVEKLIEAGVDAIVIDTAHGHSAGVINKISEIRQTFKDVV
IVAGNVATAEGARALFEVGVDIVKVGIGPGSICTTRVVAGVGVPQITAIY
DCATVAREFGKTIIADGGIKYSGDIVKALAAGGNAVMLGSMLAGTDESPG
ETEIFQGRQFKTYRGMGSLAAMEHGKLVPEGIEGRVPYKGSVADIIFQLV
GGIRSGMGYTGSPDLRHLREEAAFVRMTGAGLRESHPHDIQITKEAPNYS
Ligand information
Ligand IDIMP
InChIInChI=1S/C10H13N4O8P/c15-6-4(1-21-23(18,19)20)22-10(7(6)16)14-3-13-5-8(14)11-2-12-9(5)17/h2-4,6-7,10,15-16H,1H2,(H,11,12,17)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyGRSZFWQUAKGDAV-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.5c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N=CNC2=O
ACDLabs 10.04O=C1c2ncn(c2N=CN1)C3OC(C(O)C3O)COP(=O)(O)O
OpenEye OEToolkits 1.7.5c1nc2c(n1C3C(C(C(O3)COP(=O)(O)O)O)O)N=CNC2=O
CACTVS 3.385O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(O)=O)n2cnc3C(=O)NC=Nc23
CACTVS 3.385O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(O)=O)n2cnc3C(=O)NC=Nc23
FormulaC10 H13 N4 O8 P
NameINOSINIC ACID
ChEMBLCHEMBL1207374
DrugBankDB04566
ZINCZINC000004228242
PDB chain5upy Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5upy Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Listeria Monocytogenes in the complex with IMP and Q21
Resolution2.35 Å
Binding residue
(original residue number in PDB)		M51 G305 S306 I307 C308 D341 G343 G364 S365 Y388 G390 M391 G392 E416
Binding residue
(residue number reindexed from 1)		M53 G180 S181 I182 C183 D216 G218 G239 S240 Y263 G265 M266 G267 E280
Annotation score4
Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5upy, PDBe:5upy, PDBj:5upy
PDBsum5upy
PubMed
UniProtQ926Y9

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