Structure of PDB 5uz0 Chain D Binding Site BS06

Receptor Information
>5uz0 Chain D (length=588) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSE
LTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNL
YPFVKTVASPVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVV
STEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQM
PLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELK
EALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYA
RARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTIL
SKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVV
TKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHC
TRLAGDKANYWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEDED
LIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRS
GVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain5uz0 Chain D Residue 605 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5uz0 Discovery of N-(6-Fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5-[(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), a Potent and Selective Nonclassical Antifolate Aminoimidazole-4-carboxamide Ribonucleotide Formyltransferase (AICARFT) Inhibitor Effective at Tumor Suppression in a Cancer Xenograft Model.
Resolution1.79 Å
Binding residue
(original residue number in PDB)		V425 T428 D539 L589 H591
Binding residue
(residue number reindexed from 1)		V421 T424 D535 L585 H587
Annotation score1
Enzymatic activity
Enzyme Commision number 2.1.2.3: phosphoribosylaminoimidazolecarboxamide formyltransferase.
3.5.4.10: IMP cyclohydrolase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003937 IMP cyclohydrolase activity
GO:0004643 phosphoribosylaminoimidazolecarboxamide formyltransferase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0042803 protein homodimerization activity
GO:0045296 cadherin binding
Biological Process
GO:0003360 brainstem development
GO:0006139 nucleobase-containing compound metabolic process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0021549 cerebellum development
GO:0021987 cerebral cortex development
GO:0031100 animal organ regeneration
GO:0044208 'de novo' AMP biosynthetic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0097294 'de novo' XMP biosynthetic process
GO:0098761 cellular response to interleukin-7
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5uz0, PDBe:5uz0, PDBj:5uz0
PDBsum5uz0
PubMed29072452
UniProtP31939|PUR9_HUMAN Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

[Back to BioLiP]