Structure of PDB 1pl0 Chain C Binding Site BS01

Receptor Information
>1pl0 Chain C (length=585) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSEL
TGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLY
PFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVV
STEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQM
PLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELK
EALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYA
RARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTIL
SKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVV
TKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHC
TRLAGDKANYWWLRHHPQVLSMKFKTGAEISNAIDQYVTGTIGEDEDLIK
WKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSGVA
YIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
Ligand information
Ligand IDXMP
InChIInChI=1S/C10H13N4O9P/c15-5-3(1-22-24(19,20)21)23-9(6(5)16)14-2-11-4-7(14)12-10(18)13-8(4)17/h2-3,5-6,9,15-16H,1H2,(H2,19,20,21)(H2,12,13,17,18)/p+1/t3-,5-,6-,9-/m1/s1
InChIKeyDCTLYFZHFGENCW-UUOKFMHZSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1[nH+]c2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)NC(=O)NC2=O
CACTVS 3.341O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(O)=O)n2c[nH+]c3C(=O)NC(=O)Nc23
OpenEye OEToolkits 1.5.0c1[nH+]c2c(n1C3C(C(C(O3)COP(=O)(O)O)O)O)NC(=O)NC2=O
ACDLabs 10.04O=C3Nc1c([nH+]cn1C2OC(C(O)C2O)COP(=O)(O)O)C(=O)N3
CACTVS 3.341O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(O)=O)n2c[nH+]c3C(=O)NC(=O)Nc23
FormulaC10 H14 N4 O9 P
NameXANTHOSINE-5'-MONOPHOSPHATE;
5-MONOPHOSPHATE-9-BETA-D-RIBOFURANOSYL XANTHINE
ChEMBL
DrugBank
ZINC
PDB chain1pl0 Chain C Residue 903 [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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PDB1pl0 Crystal Structures of Human Bifunctional Enzyme Aminoimidazole-4-carboxamide Ribonucleotide Transformylase/IMP Cyclohydrolase in Complex with Potent Sulfonyl-containing Antifolates.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		S10 V11 S34 G36 T37 R64 K66 T67 L68 N102 Y104 D125 G127
Binding residue
(residue number reindexed from 1)		S6 V7 S30 G32 T33 R60 K62 T63 L64 N98 Y100 D121 G123
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) K266 H267 N431 H592
Catalytic site (residue number reindexed from 1) K262 H263 N427 H585
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

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1pl0, PDBe:1pl0, PDBj:1pl0
PDBsum1pl0
PubMed14966129
UniProtP31939|PUR9_HUMAN Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

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