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 | (2S,3S)-1,4-Dimercaptobutane-2,3-diol | Ligand Info | |||
| Canonical SMILES | C(C(C(CS)O)O)S | ||||
| InChI | 1S/C4H10O2S2/c5-3(1-7)4(6)2-8/h3-8H,1-2H2/t3-,4-/m1/s1 | ||||
| InChIKey | VHJLVAABSRFDPM-QWWZWVQMSA-N | ||||
| PubChem Compound ID | 446094 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4A0D Structure of unliganded human PARG catalytic domain | ||||||
| Method | X-ray diffraction | Resolution | 1.75 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 EWERCEKPLT 716 RLHVTYEGTI726 EENGQGMLQV736 DFANRFVGGG746 VTSAGLVQEE756 IRFLINPELI 766 ISRLFTEVLD776 HNECLIITGT786 EQYSEYTGYA796 ETYRWSRSHE806 DGSERDDWQR 816 RCTEIVAIDA826 LHFRRYLDQF836 VPEKMRRELN846 KAYCGFLRPG856 VSSENLSAVA 866 TGNWGCGAFG876 GDARLKALIQ886 ILAAAAAERD896 VVYFTFGDSE906 LMRDIYSMHI 916 FLTERKLTVG926 DVYKLLLRYY936 NEECRNCSTP946 GPDIKLYPFI956 YHAVESC |
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| PDB ID: 4B1G Structure of unliganded human PARG catalytic domain | ||||||
| Method | X-ray diffraction | Resolution | 1.83 Å | Mutation | Yes | [1] |
| PDB Sequence |
KKWLGTPIEE
460 RRPRCGIRLP472 LLRPSANHTV482 TIRVDLLRAG492 EVPKPFPTHY502 KDLWDNKHVK 512 PCSEQNLYPV523 RTAGSRWELI539 QTALLNKFTR549 PQNLKDAILK559 YNVAYSKKWD 569 FTALIDFWDK579 VLEEAEAQHL589 YQSILPDVKI600 ALCLPNICTQ610 PIPLLAAANH 621 SITSQEQIAS632 LLANAFFCTF642 PRRNASEYSS655 YPDINFNRLF665 EGRSSRKPEK 675 LKTLFCYFRR685 VTAAAPTGLV695 TFTRQSLEDF705 PEWERCEKPL715 TRLHVTYEGT 725 IEENGQGLQV736 DFANRFVGGG746 VTSAGLVQEE756 IRFLINPELI766 ISRLFTEVLD 776 HNECLIITGT786 EQYSEYTGYA796 ETYRWSRSHE806 DGSERDDWQR816 RCTEIVAIDA 826 LHFRRYLDQF836 VPEKRRELNK847 AYCGFLRPGV857 SSENLSAVAT867 GNWGCGAFGG 877 DARLKALIQI887 LAAAAAERDV897 VYFTFGDSEL907 RDIYSHIFLT919 ERKLTVGDVY 929 KLLLRYYNEE939 CRNCPDIKLY953 PFIYHAVES
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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 | [1] |
| 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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| PDB ID: 4B1I Structure of human PARG catalytic domain in complex with OA-ADP-HPD | ||||||
| Method | X-ray diffraction | Resolution | 2.14 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 EWERCEKPLT 716 RLHVTYEGTI726 EENGQGMLQV736 DFANRFVGGG746 VTSAGLVQEE756 IRFLINPELI 766 ISRLFTEVLD776 HNECLIITGT786 EQYSEYTGYA796 ETYRWSRSHE806 DGSERDDWQR 816 RCTEIVAIDA826 LHFRRYLDQF836 VPEKMRRELN846 KAYCGFLRPG856 VSSENLSAVA 866 TGNWGCGAFG876 GDARLKALIQ886 ILAAAAAERD896 VVYFTFGDSE906 LMRDIYSMHI 916 FLTERKLTVG926 DVYKLLLRYY936 NEECRNCSTP946 GPDIKLYPFI956 YHAVESC |
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | 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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