eF-site ID 6oa3-A PDB Code 6oa3 Chain A click to enlarge Title Structure of human PARG complexed with JA2131 Classification hydrolase/hydrolase inhibitor Compound Poly(ADP-ribose) glycohydrolase Source (PARG_HUMAN) Sequence A:  DKKWLGTPIEEMRRMPRCGIRLPLLRPSANHTVTIRVDLL RAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVTAGSRW ELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALIDF WDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLA AAMNHSITMSQEQIASLLANAFFCTFPRRNSSYPDINFNR LFEGRSSRKPEKLKTLFCYFRRVTAAAPTGLVTFTRQSLE DFPEWERCEKPLTRLHVTYEGTIEENGQGMLQVDFANRFV GGGVTSAGLVQEEIRFLINPELIISRLFTEVLDHNECLII TGTEQYSEYTGYAETYRWSRSHEDGSERDDWQRRCTEIVA IDALHFRRYLDQFVPEKMRRELNKAYCGFLRPGVSSENLS AVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYFTFG DSELMRDIYSMHIFLTERKLTVGDVYKLLLRYYNEECRNC STPGPDIKLYPFIYHAVESC Description Functional site 1) chain A residue 725 type sequence T description binding site for residue M0M A 1001 source : AC1 2) chain A residue 726 type sequence I description binding site for residue M0M A 1001 source : AC1 3) chain A residue 727 type sequence E description binding site for residue M0M A 1001 source : AC1 4) chain A residue 738 type sequence F description binding site for residue M0M A 1001 source : AC1 5) chain A residue 753 type sequence V description binding site for residue M0M A 1001 source : AC1 6) chain A residue 754 type sequence Q description binding site for residue M0M A 1001 source : AC1 7) chain A residue 792 type sequence Y description binding site for residue M0M A 1001 source : AC1 8) chain A residue 869 type sequence N description binding site for residue M0M A 1001 source : AC1 9) chain A residue 872 type sequence C description binding site for residue M0M A 1001 source : AC1 10) chain A residue 873 type sequence G description binding site for residue M0M A 1001 source : AC1 11) chain A residue 900 type sequence F description binding site for residue M0M A 1001 source : AC1 12) chain A residue 902 type sequence F description binding site for residue M0M A 1001 source : AC1 13) chain A residue 737 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:23251397 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 755 type ACT_SITE sequence E description ACT_SITE => ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23251397 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 756 type ACT_SITE sequence E description ACT_SITE => ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23251397 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 726 type BINDING sequence I description BINDING => ECO:0000269|PubMed:23251397, ECO:0000269|PubMed:30472116 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 740 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23251397, ECO:0000269|PubMed:30472116 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 754 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:23251397, ECO:0000269|PubMed:30472116 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 869 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23251397, ECO:0000269|PubMed:30472116 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 795 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:Q9QYM2 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links