eF-site ID 4x2a-AB PDB Code 4x2a Chain A, B click to enlarge Title Crystal structure of mouse glyoxalase I complexed with baicalein Classification LYASE/LYASE INHIBITOR Compound Lactoylglutathione lyase Source (LGUL_MOUSE) Sequence A:  TAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLG LTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFS RKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPD VYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEI LNPNKIA B:  SSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLD FYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSE KTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGH IGIAVPDVYSACKRFEELGVKFVKKPDDGMKGLAFIQDPD GYWIEILNPNKIATI Description Functional site 1) chain A residue 127 type sequence H description binding site for residue ZN A 201 source : AC1 2) chain A residue 173 type sequence E description binding site for residue ZN A 201 source : AC1 3) chain B residue 34 type sequence Q description binding site for residue ZN A 201 source : AC1 4) chain B residue 100 type sequence E description binding site for residue ZN A 201 source : AC1 5) chain A residue 34 type sequence Q description binding site for residue ZN A 202 source : AC2 6) chain A residue 100 type sequence E description binding site for residue ZN A 202 source : AC2 7) chain B residue 127 type sequence H description binding site for residue ZN A 202 source : AC2 8) chain B residue 173 type sequence E description binding site for residue ZN A 202 source : AC2 9) chain A residue 127 type sequence H description binding site for residue 3WL A 203 source : AC3 10) chain A residue 158 type sequence M description binding site for residue 3WL A 203 source : AC3 11) chain A residue 173 type sequence E description binding site for residue 3WL A 203 source : AC3 12) chain A residue 180 type sequence I description binding site for residue 3WL A 203 source : AC3 13) chain A residue 181 type sequence A description binding site for residue 3WL A 203 source : AC3 14) chain B residue 34 type sequence Q description binding site for residue 3WL A 203 source : AC3 15) chain B residue 61 type sequence L description binding site for residue 3WL A 203 source : AC3 16) chain B residue 63 type sequence F description binding site for residue 3WL A 203 source : AC3 17) chain B residue 68 type sequence F description binding site for residue 3WL A 203 source : AC3 18) chain B residue 70 type sequence L description binding site for residue 3WL A 203 source : AC3 19) chain B residue 100 type sequence E description binding site for residue 3WL A 203 source : AC3 20) chain A residue 34 type sequence Q description binding site for residue 3WL B 201 source : AC4 21) chain A residue 63 type sequence F description binding site for residue 3WL B 201 source : AC4 22) chain A residue 68 type sequence F description binding site for residue 3WL B 201 source : AC4 23) chain A residue 70 type sequence L description binding site for residue 3WL B 201 source : AC4 24) chain A residue 93 type sequence F description binding site for residue 3WL B 201 source : AC4 25) chain A residue 100 type sequence E description binding site for residue 3WL B 201 source : AC4 26) chain B residue 127 type sequence H description binding site for residue 3WL B 201 source : AC4 27) chain B residue 158 type sequence M description binding site for residue 3WL B 201 source : AC4 28) chain B residue 173 type sequence E description binding site for residue 3WL B 201 source : AC4 29) chain B residue 180 type sequence I description binding site for residue 3WL B 201 source : AC4 30) chain B residue 183 type sequence I description binding site for residue 3WL B 201 source : AC4 31) chain A residue 34 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI2 32) chain A residue 100 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI2 33) chain B residue 34 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI2 34) chain B residue 100 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI2 35) chain A residue 38 type BINDING sequence R description BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI3 36) chain A residue 104 type BINDING sequence N description BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI3 37) chain B residue 38 type BINDING sequence R description BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI3 38) chain B residue 104 type BINDING sequence N description BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI3 39) chain A residue 127 type BINDING sequence H description in other chain => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI5 40) chain A residue 173 type BINDING sequence E description in other chain => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI5 41) chain B residue 127 type BINDING sequence H description in other chain => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI5 42) chain B residue 173 type BINDING sequence E description in other chain => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI5 43) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q04760 source Swiss-Prot : SWS_FT_FI8 44) chain B residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q04760 source Swiss-Prot : SWS_FT_FI8 45) chain A residue 139 type MOD_RES sequence C description S-glutathionyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 46) chain B residue 139 type MOD_RES sequence C description S-glutathionyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 47) chain A residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI10 48) chain B residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI10 49) chain A residue 123 type BINDING sequence R description in other chain => ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI4 50) chain A residue 157 type BINDING sequence K description in other chain => ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI4 51) chain B residue 123 type BINDING sequence R description in other chain => ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI4 52) chain A residue 88 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI7 53) chain B residue 88 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI7 54) chain A residue 173 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 173 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 34-55 type prosite sequence QTMLRIKDPKKSLDFYTRVLGL description GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrIkdpkKSldFYtrvLGL source prosite : PS00934 57) chain A residue 118-134 type prosite sequence GNSDPRGFGHIGIAVPD description GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD source prosite : PS00935

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