eF-site ID 6cxs-ABCD PDB Code 6cxs Chain A, B, C, D click to enlarge Title Crystal Structure of Clostridium perfringens beta-glucuronidase bound with a novel, potent inhibitor 4-(8-(piperazin-1-yl)-1,2,3,4-tetrahydro-[1,2,3]triazino[4',5':4,5]thieno[2,3-c]isoquinolin-5-yl)morpholine Classification HYDROLASE/HYDROLASE INHIBITOR Compound Beta-glucuronidase Source (MALE_ECOLI) Sequence A:  SNAMLYPIITESRQLIDLSGIWKFKLNEGNGLTEELSKAP LEDTIEMAVPSSYNDLVESQEVRDHVGWVWYERNFTIPKT LLNERIVLRFGSATHEAKVYLNGELLVEHKGGFTPFEAEI NDLLVSGDNRLTVAVNNIIDETTLPVGLVKEVEVDGKKVI KNSVNFDFFNYAGIHRPVKIYTTPKSYIEDITIVTDFKEN NGYVNYEVQAVGKCNIKVTIIDEENNIVAEGEGKEGKLTI NNVHLWEPMNAYLYKLKVELLDDEEIIDTYFEEFGVRTVE VKDGKFLINNKPFYFKGFGKHEDSYVNGRGINEAINIKDF NLMKWIGANSFRTSHYPYSEEIMRLADREGIVVIDETPAV GLHLNFMATGFPKRDTWKEIGTKEAHERILRELVSRDKNH PCVVMWSVANEPDSDSEGAKEYFEPLIKLTKELDPQKRPV TVVTYLMSTPDRCKVGDIVDVLCLNRYYGWYVAGGDLEEA KRMLEDELKGWEERCPKTPIMFTEYGADTVAGLHDTVPVM FTEEYQVEYYKANHEVMDKCKNFVGEQVWNFADFATSQGI IRVQGNKKGIFTRERKPKMIAHSLRERWTNIPEFGYKK B:  SNAMLYPIITESRQLIDLSGIWKFKLNEGNGLTEELSKAP LEDTIEMAVPSSYNDLVESQEVRDHVGWVWYERNFTIPKT LLNERIVLRFGSATHEAKVYLNGELLVEHKGGFTPFEAEI NDLLVSGDNRLTVAVNNIIDETTLPVGLVKEVEVDGKKVI KNSVNFDFFNYAGIHRPVKIYTTPKSYIEDITIVTDFKEN NGYVNYEVQAVGKCNIKVTIIDEENNIVAEGEGKEGKLTI NNVHLWEPMNAYLYKLKVELLDDEEIIDTYFEEFGVRTVE VKDGKFLINNKPFYFKGFGKHEDSYVNGRGINEAINIKDF NLMKWIGANSFRTSHYPYSEEIMRLADREGIVVIDETPAV GLHLNFMATGFAPKRDTWKEIGTKEAHERILRELVSRDKN HPCVVMWSVANEPDSDSEGAKEYFEPLIKLTKELDPQKRP VTVVTYLMSTPDRCKVGDIVDVLCLNRYYGWYVAGGDLEE AKRMLEDELKGWEERCPKTPIMFTEYGADTVAGLHDTVPV MFTEEYQVEYYKANHEVMDKCKNFVGEQVWNFADFATSQG IIRVQGNKKGIFTRERKPKMIAHSLRERWTNIPEFGYKK C:  KLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKA KGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV GVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGE TAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGV LSAGINAASPNKELAVNKDKPLGAVALKSYEEELAKDPRI AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTV DEALKDAQTNSS D:  IWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFP QVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDK LYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKT WEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYA FKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADT DYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLP TFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDE GLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGE IMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNS SS Description Functional site 1) chain A residue 363 type sequence F description binding site for residue FJV A 601 source : AC1 2) chain A residue 364 type sequence M description binding site for residue FJV A 601 source : AC1 3) chain A residue 368 type sequence F description binding site for residue FJV A 601 source : AC1 4) chain A residue 412 type sequence E description binding site for residue FJV A 601 source : AC1 5) chain A residue 447 type sequence L description binding site for residue FJV A 601 source : AC1 6) chain A residue 472 type sequence Y description binding site for residue FJV A 601 source : AC1 7) chain A residue 562 type sequence I description binding site for residue FJV A 601 source : AC1 8) chain A residue 563 type sequence R description binding site for residue FJV A 601 source : AC1 9) chain B residue 364 type sequence M description binding site for residue FJV B 601 source : AC2 10) chain B residue 368 type sequence F description binding site for residue FJV B 601 source : AC2 11) chain B residue 412 type sequence E description binding site for residue FJV B 601 source : AC2 12) chain B residue 447 type sequence L description binding site for residue FJV B 601 source : AC2 13) chain B residue 448 type sequence M description binding site for residue FJV B 601 source : AC2 14) chain B residue 472 type sequence Y description binding site for residue FJV B 601 source : AC2 15) chain C residue 109-126 type prosite sequence PIAVEALSLIYNKDLLPN description SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN source prosite : PS01037 16) chain A residue 398-412 type prosite sequence DKNHPCVVMWSVANE description GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPCVVMWSva.NE source prosite : PS00608 17) chain A residue 326-351 type prosite sequence NSFRTSHYPYSEEIMRLADREGIVVI description GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsFRTSHYPyseeIMrlaDreGIVVI source prosite : PS00719 18) chain A residue 412 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 412 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 505 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 505 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 164 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 466 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 472 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 505 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 550 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 569 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 411 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 466 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 472 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 505 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 550 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 569 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 164 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3 35) chain B residue 411 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P05804 source Swiss-Prot : SWS_FT_FI3

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