Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T66935 | Target Info | |||
| Target Name | Poly [ADP-ribose] glycohydrolase (PARG) | ||||
| Synonyms | Poly(ADP-ribose) glycohydrolase | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | PARG | ||||
| Biochemical Class | Glycosylase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Cysteine Sulfenic Acid | Ligand Info | |||
| Canonical SMILES | C(C(C(=O)O)N)SO | ||||
| InChI | 1S/C3H7NO3S/c4-2(1-8-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 | ||||
| InChIKey | FXIRVRPOOYSARH-REOHCLBHSA-N | ||||
| PubChem Compound ID | 165339 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6HMM POLYADPRIBOSYL GLYCOHYDROLASE IN COMPLEX WITH PDD00013907 | ||||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | Yes | [1] |
| PDB Sequence |
DKKWLGTPIE
459 EMRRMPRCGI469 RLPLLRPSAN479 HTVTIRVDLL489 RAGEVPKPFP499 THYKDLWDNK 509 HVKMPCSEQN519 LYPVTAGSRW536 ELIQTALLNK546 FTRPQNLKDA556 ILKYNVAYSK 566 KWDFTALIDF576 WDKVLEEAEA586 QHLYQSILPD596 MVKIALCLPN606 ICTQPIPLLA 616 AAMNHSITMS626 QEQIASLLAN636 AFFCTFPRRN646 AKMKSEYSSY656 PDINFNRLFE 666 GRSSRKPEKL676 KTLFCYFRRV686 TAAAPTGLVT696 FTRQSLEDFP706 EWEREKPLTR 717 LHVTYEGTIE727 ENGQGMLQVD737 FANRFVGGGV747 TSAGLVQEEI757 RFLINPELII 767 SRLFTEVLDH777 NECLIITGTE787 QYSEYTGYAE797 TYRWSRSHED807 GSERDDWQRR 817 CTEIVAIDAL827 HFRRYLDQFV837 PEKMRRELNK847 AYCGFLRPGV857 SSENLSAVAT 867 GNWGCGAFGG877 DARLKALIQI887 LAAAAAERDV897 VYFTFGDSEL907 MRDIYSMHIF 917 LTERKLTVGD927 VYKLLLRYYN937 EECRNSTPGP948 DIKLYPFIYH958 AVESC |
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PRO706
4.656
GLU707
3.394
TRP708
3.088
GLU709
3.599
ARG710
1.349
GLU712
1.349
LYS713
3.410
LEU833
3.811
ALA892
4.633
THR924
3.424
VAL925
3.606
|
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| PDB ID: 4B1H Structure of human PARG catalytic domain in complex with ADP-ribose | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | Yes | [2] |
| PDB Sequence |
KKWLGTPIEE
460 MRRMPRGIRL471 PLLRPSANHT481 VTIRVDLLRA491 GEVPKPFPTH501 YKDLWDNKHV 511 KMPCSEQNLY521 PVRTAGSRWE537 LIQTALLNKF547 TRPQNLKDAI557 LKYNVAYSKK 567 WDFTALIDFW577 DKVLEEAEAQ587 HLYQSILPDM597 VKIALCLPNI607 CTQPIPLLAA 617 AMNHSITMSQ627 EQIASLLANA637 FFCTFPRRNA647 KMKSEYSSYP657 DINFNRLFEG 667 RSSRKPEKLK677 TLFCYFRRVT687 AAAPTGLVTF697 TRQSLEDFPE707 WERCEKPLTR 717 LHVTYEGTIE727 ENGQGMLQVD737 FANRFVGGGV747 TSAGLVQEEI757 RFLINPELII 767 SRLFTEVLDH777 NECLIITGTE787 QYSEYTGYAE797 TYRWSRSHED807 GSERDDWQRR 817 CTEIVAIDAL827 HFRRYLDQFV837 PEKMRRELNK847 AYCGFLRPGV857 SSENLSAVAT 867 GNWGCGAFGG877 DARLKALIQI887 LAAAAAERDV897 VYFTFGDSEL907 MRDIYSMHIF 917 LTERKLTVGD927 VYKLLLRYYN937 EECRNCSTPG947 PDIKLYPFIY957 HAVESC |
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Cell-Active Small Molecule Inhibitors of the DNA-Damage Repair Enzyme Poly(ADP-ribose) Glycohydrolase (PARG): Discovery and Optimization of Orally Bioavailable Quinazolinedione Sulfonamides. J Med Chem. 2018 Dec 13;61(23):10767-10792. | ||||
| REF 2 | Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives. PLoS One. 2012;7(12):e50889. | ||||
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