eF-site ID 2v0t-ABCDEFGH PDB Code 2v0t Chain A, B, C, D, E, F, G, H click to enlarge Title The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM Classification ISOMERASE Compound TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL Source (TPIS_TRYBB) Sequence A:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWVLTPQQAQEAHALIRSWVSSKIGADVAGELR ILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIK ATQ B:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAIGTGKVLTPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ C:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWLTPQQAQEAHALIRSWVSSKIGADVAGELRI LYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKA TQ D:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAIGTGKVLTPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ E:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAVLTPQQAQEAHALIRSWVSSKIGADVAGEL RILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDII KATQ F:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWLTPQQAQEAHALIRSWVSSKIGADVAGELRI LYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKA TQ G:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAIGTGKVLTPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ H:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWLTPQQAQEAHALIRSWVSSKIGADVAGELRI LYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKA TQ Description Functional site 1) chain A residue 213 type sequence S description BINDING SITE FOR RESIDUE SO4 A1251 source : AC1 2) chain A residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 A1251 source : AC1 3) chain A residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 A1251 source : AC1 4) chain B residue 213 type sequence S description BINDING SITE FOR RESIDUE SO4 B1251 source : AC2 5) chain B residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 B1251 source : AC2 6) chain B residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 B1251 source : AC2 7) chain C residue 170 type sequence W description BINDING SITE FOR RESIDUE SO4 C1251 source : AC3 8) chain C residue 213 type sequence S description BINDING SITE FOR RESIDUE SO4 C1251 source : AC3 9) chain C residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 C1251 source : AC3 10) chain C residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 C1251 source : AC3 11) chain D residue 213 type sequence S description BINDING SITE FOR RESIDUE SO4 D1251 source : AC4 12) chain D residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 D1251 source : AC4 13) chain D residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 D1251 source : AC4 14) chain E residue 213 type sequence S description BINDING SITE FOR RESIDUE SO4 E1251 source : AC5 15) chain E residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 E1251 source : AC5 16) chain E residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 E1251 source : AC5 17) chain F residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 F1251 source : AC6 18) chain F residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 F1251 source : AC6 19) chain G residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 G1251 source : AC7 20) chain H residue 213 type sequence S description BINDING SITE FOR RESIDUE SO4 H1251 source : AC8 21) chain H residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 H1251 source : AC8 22) chain H residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 H1251 source : AC8 23) chain A residue 31 type sequence T description BINDING SITE FOR RESIDUE SO4 A1252 source : AC9 24) chain A residue 32 type sequence S description BINDING SITE FOR RESIDUE SO4 A1252 source : AC9 25) chain A residue 33 type sequence I description BINDING SITE FOR RESIDUE SO4 A1252 source : AC9 26) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE SO4 A1252 source : AC9 27) chain A residue 59 type sequence K description BINDING SITE FOR RESIDUE SO4 A1252 source : AC9 28) chain E residue 31 type sequence T description BINDING SITE FOR RESIDUE SO4 E1252 source : BC1 29) chain E residue 32 type sequence S description BINDING SITE FOR RESIDUE SO4 E1252 source : BC1 30) chain E residue 33 type sequence I description BINDING SITE FOR RESIDUE SO4 E1252 source : BC1 31) chain E residue 57 type sequence H description BINDING SITE FOR RESIDUE SO4 E1252 source : BC1 32) chain C residue 155 type sequence K description BINDING SITE FOR RESIDUE EPE C1252 source : BC2 33) chain D residue 29 type sequence N description BINDING SITE FOR RESIDUE EPE D1252 source : BC3 34) chain D residue 31 type sequence T description BINDING SITE FOR RESIDUE EPE D1252 source : BC3 35) chain D residue 32 type sequence S description BINDING SITE FOR RESIDUE EPE D1252 source : BC3 36) chain D residue 33 type sequence I description BINDING SITE FOR RESIDUE EPE D1252 source : BC3 37) chain D residue 57 type sequence H description BINDING SITE FOR RESIDUE EPE D1252 source : BC3 38) chain D residue 59 type sequence K description BINDING SITE FOR RESIDUE EPE D1252 source : BC3 39) chain A residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 40) chain E residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 41) chain F residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 42) chain F residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 43) chain G residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 44) chain G residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 45) chain H residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 46) chain H residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 47) chain A residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 48) chain B residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 49) chain B residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 50) chain C residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 51) chain C residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 52) chain D residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 53) chain D residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 54) chain E residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 55) chain A residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 56) chain B residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 57) chain C residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 58) chain D residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 59) chain E residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 60) chain F residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 61) chain G residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 62) chain H residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 63) chain A residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 64) chain B residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 65) chain C residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 66) chain D residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 67) chain E residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 68) chain F residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 69) chain G residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 70) chain H residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2

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