eF-site ID 4pv5-AB PDB Code 4pv5 Chain A, B click to enlarge Title Crystal structure of mouse glyoxalase I in complexed with 18-beta-glycyrrhetinic acid Classification LYASE/LYASE INHIBITOR Compound Lactoylglutathione lyase Source Mus musculus (Mouse) (LGUL_MOUSE) Sequence A:  DETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRV LGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWT FSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAV PDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWI EILNPNKIAT B:  EPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDP KKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIP KDKSEKTAWTFSRKATLELTHNWGTEDDETQSYHNGNSDP RGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLA FIQDPDGYWIEILNPNKIATII Description Functional site 1) chain A residue 34 type sequence Q description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 2) chain A residue 100 type sequence E description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 3) chain B residue 127 type sequence H description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 4) chain B residue 173 type sequence E description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 5) chain A residue 123 type sequence R description BINDING SITE FOR RESIDUE CBW A 202 source : AC2 6) chain A residue 151 type sequence K description BINDING SITE FOR RESIDUE CBW A 202 source : AC2 7) chain A residue 156 type sequence G description BINDING SITE FOR RESIDUE CBW A 202 source : AC2 8) chain B residue 38 type sequence R description BINDING SITE FOR RESIDUE CBW A 202 source : AC2 9) chain B residue 104 type sequence N description BINDING SITE FOR RESIDUE CBW A 202 source : AC2 10) chain A residue 127 type sequence H description BINDING SITE FOR RESIDUE ZN B 201 source : AC3 11) chain A residue 173 type sequence E description BINDING SITE FOR RESIDUE ZN B 201 source : AC3 12) chain B residue 34 type sequence Q description BINDING SITE FOR RESIDUE ZN B 201 source : AC3 13) chain B residue 100 type sequence E description BINDING SITE FOR RESIDUE ZN B 201 source : AC3 14) chain A residue 34-55 type prosite sequence QTMLRIKDPKKSLDFYTRVLGL description GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrIkdpkKSldFYtrvLGL source prosite : PS00934 15) chain B residue 173 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 173 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) 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 18) 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 19) 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 20) 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 21) chain B residue 88 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI7 22) chain A residue 88 type MOD_RES sequence K description N6-succinyllysine => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI7 23) chain B residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q04760 source Swiss-Prot : SWS_FT_FI8 24) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q04760 source Swiss-Prot : SWS_FT_FI8 25) chain B residue 139 type MOD_RES sequence C description S-glutathionyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 26) chain A residue 139 type MOD_RES sequence C description S-glutathionyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 27) chain A residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI10 28) chain B residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 source Swiss-Prot : SWS_FT_FI10 29) chain B residue 38 type BINDING sequence R description BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI3 30) chain B residue 104 type BINDING sequence N description BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI3 31) chain A residue 104 type BINDING sequence N description BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI3 32) chain A residue 38 type BINDING sequence R description BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI3 33) chain A residue 118-134 type prosite sequence GNSDPRGFGHIGIAVPD description GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD source prosite : PS00935 34) chain B residue 34 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI2 35) chain B residue 100 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI2 36) chain A residue 34 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI2 37) chain A residue 100 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI2 38) chain B residue 123 type BINDING sequence R description in other chain => ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI4 39) chain B residue 157 type BINDING sequence K description in other chain => ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI4 40) chain A residue 157 type BINDING sequence K description in other chain => ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI4 41) chain A residue 123 type BINDING sequence R description in other chain => ECO:0007744|PDB:4OPN source Swiss-Prot : SWS_FT_FI4

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