eF-site ID 2gge-ABCDEFGH PDB Code 2gge Chain A, B, C, D, E, F, G, H click to enlarge Title Crystal Structure of Mandelate Racemase/Muconate Lactonizing Enzyme from Bacillus Subtilis complexed with MG++ at 1.8 A Classification STRUCTURAL GENOMICS, UNKNOWN FUNCTION Compound yitF Source (O06741_BACSU) Sequence A:  LVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITE SGIDGWGECVDWLPALHVGFTKRIIPFLLGKQAGSRLSLV RTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYRE EIPVYASFQSYSDSPQWISRSVSNVEAQLKKGFEQIKVKI GGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFK WERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGG ENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQL ARYFGVRASAHAYDGSLSRLYALFAQACLPPWSKMKNDHI EPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINME IVNRYKWDGSAYE B:  ALVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIIT ESGIDGWGECVDWLPALHVGFTKRIIPFLLGKQAGSRLSL VRTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYR EEIPVYASFQSYSDSPQWISRSVSNVEAQLKKGFEQIKVK IGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAF KWERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAG GENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQ LARYFGVRASAHAYDGSLSRLYALFAQACLPPWSKMKNDH IEPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINM EIVNRYKWDGSAYE C:  ALVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIIT ESGIDGWGECVDWLPALHVGFTKRIIPFLLGKQAGSRLSL VRTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYR EEIPVYASFQSYSDSPQWISRSVSNVEAQLKKGFEQIKVK IGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAF KWERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAG GENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQ LARYFGVRASAHAYDGSLSRLYALFAQACLPPWSKMKNDH IEPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINM EIVNRYKWDGSAYE D:  ALVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIIT ESGIDGWGECVDWLPALHVGFTKRIIPFLLGKQAGSRLSL VRTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYR EEIPVYASFQSYSDSPQWISRSVSNVEAQLKKGFEQIKVK IGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAF KWERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAG GENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQ LARYFGVRASAHAYDGSLSRLYALFAQACLPPWSKMKNDH IEPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINM EIVNRYKWDGSAYEGH E:  LVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITE SGIDGWGECVDWLPALHVGFTKRIIPFLLGKQAGSRLSLV RTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYRE EIPVYASFQSYSDSPQWISRSVSNVEAQLKKGFEQIKVKI GGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFK WERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGG ENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQL ARYFGVRASAHAYDGSLSRLYALFAQACLPPWSKMKNDHI EPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINME IVNRYKWDGSAYE F:  LVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITE SGIDGWGECVDWLPALHVGFTKRIIPFLLGKQAGSRLSLV RTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYRE EIPVYASFQSYSDSPQWISRSVSNVEAQLKKGFEQIKVKI GGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFK WERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGG ENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQL ARYFGVRASAHAYDGSLSRLYALFAQACLPPWSKMKNDHI EPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINME IVNRYKWDGSAYE G:  ALVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIIT ESGIDGWGECVDWLPALHVGFTKRIIPFLLGKQAGSRLSL VRTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYR EEIPVYASFQSYSDSPQWISRSVSNVEAQLKKGFEQIKVK IGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAF KWERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAG GENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQ LARYFGVRASAHAYDGSLSRLYALFAQACLPPWSKMKNDH IEPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINM EIVNRYKWDGSAYE H:  ALVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIIT ESGIDGWGECVDWLPALHVGFTKRIIPFLLGKQAGSRLSL VRTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYR EEIPVYASFQSYSDSPQWISRSVSNVEAQLKKGFEQIKVK IGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAF KWERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAG GENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQ LARYFGVRASAHAYDGSLSRLYALFAQACLPPWSKMKNDH IEPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINM EIVNRYKWDGSAYE Description Functional site 1) chain H residue 217 type sequence E description BINDING SITE FOR RESIDUE MG H 400 source : AC1 2) chain H residue 243 type sequence E description BINDING SITE FOR RESIDUE MG H 400 source : AC1 3) chain H residue 293 type sequence H description BINDING SITE FOR RESIDUE MG H 400 source : AC1 4) chain G residue 190 type sequence D description BINDING SITE FOR RESIDUE MG G 400 source : AC2 5) chain G residue 217 type sequence E description BINDING SITE FOR RESIDUE MG G 400 source : AC2 6) chain G residue 243 type sequence E description BINDING SITE FOR RESIDUE MG G 400 source : AC2 7) chain G residue 293 type sequence H description BINDING SITE FOR RESIDUE MG G 400 source : AC2 8) chain D residue 217 type sequence E description BINDING SITE FOR RESIDUE MG D 400 source : AC3 9) chain D residue 243 type sequence E description BINDING SITE FOR RESIDUE MG D 400 source : AC3 10) chain D residue 293 type sequence H description BINDING SITE FOR RESIDUE MG D 400 source : AC3 11) chain C residue 217 type sequence E description BINDING SITE FOR RESIDUE MG C 400 source : AC4 12) chain C residue 243 type sequence E description BINDING SITE FOR RESIDUE MG C 400 source : AC4 13) chain C residue 293 type sequence H description BINDING SITE FOR RESIDUE MG C 400 source : AC4 14) chain B residue 217 type sequence E description BINDING SITE FOR RESIDUE MG B 400 source : AC5 15) chain B residue 243 type sequence E description BINDING SITE FOR RESIDUE MG B 400 source : AC5 16) chain B residue 293 type sequence H description BINDING SITE FOR RESIDUE MG B 400 source : AC5 17) chain A residue 190 type sequence D description BINDING SITE FOR RESIDUE MG A 400 source : AC6 18) chain A residue 217 type sequence E description BINDING SITE FOR RESIDUE MG A 400 source : AC6 19) chain A residue 243 type sequence E description BINDING SITE FOR RESIDUE MG A 400 source : AC6 20) chain A residue 293 type sequence H description BINDING SITE FOR RESIDUE MG A 400 source : AC6 21) chain F residue 190 type sequence D description BINDING SITE FOR RESIDUE MG F 400 source : AC7 22) chain F residue 217 type sequence E description BINDING SITE FOR RESIDUE MG F 400 source : AC7 23) chain F residue 243 type sequence E description BINDING SITE FOR RESIDUE MG F 400 source : AC7 24) chain F residue 293 type sequence H description BINDING SITE FOR RESIDUE MG F 400 source : AC7 25) chain E residue 190 type sequence D description BINDING SITE FOR RESIDUE MG E 400 source : AC8 26) chain E residue 217 type sequence E description BINDING SITE FOR RESIDUE MG E 400 source : AC8 27) chain E residue 243 type sequence E description BINDING SITE FOR RESIDUE MG E 400 source : AC8 28) chain E residue 293 type sequence H description BINDING SITE FOR RESIDUE MG E 400 source : AC8 29) chain D residue 373 type sequence A description BINDING SITE FOR RESIDUE CL D 1801 source : AC9 30) chain D residue 376 type sequence G description BINDING SITE FOR RESIDUE CL D 1801 source : AC9 31) chain D residue 54 type sequence W description BINDING SITE FOR RESIDUE CL D 1802 source : BC1 32) chain D residue 374 type sequence Y description BINDING SITE FOR RESIDUE CL D 1802 source : BC1 33) chain G residue 193 type sequence Q description BINDING SITE FOR RESIDUE CL G 1803 source : BC2 34) chain G residue 244 type sequence N description BINDING SITE FOR RESIDUE CL G 1803 source : BC2 35) chain A residue 161 type ACT_SITE sequence K description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 293 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 161 type ACT_SITE sequence K description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 293 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 161 type ACT_SITE sequence K description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 40) chain C residue 293 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 161 type ACT_SITE sequence K description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 42) chain D residue 293 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 43) chain E residue 161 type ACT_SITE sequence K description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 44) chain E residue 293 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 45) chain F residue 161 type ACT_SITE sequence K description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 46) chain F residue 293 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 47) chain G residue 161 type ACT_SITE sequence K description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 48) chain G residue 293 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 49) chain H residue 161 type ACT_SITE sequence K description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 50) chain H residue 293 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 217 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 52) chain A residue 243 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 53) chain A residue 293 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 54) chain B residue 217 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 55) chain B residue 243 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 56) chain B residue 293 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 57) chain C residue 217 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 58) chain C residue 243 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 59) chain C residue 293 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 60) chain D residue 217 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 61) chain D residue 243 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 62) chain D residue 293 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 63) chain E residue 217 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 64) chain E residue 243 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 65) chain E residue 293 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 66) chain F residue 217 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 67) chain F residue 243 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 68) chain F residue 293 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 69) chain G residue 217 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 70) chain G residue 243 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 71) chain G residue 293 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 72) chain H residue 217 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 73) chain H residue 243 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 74) chain H residue 293 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2

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