eF-site ID 4jeq-ABCDEFGHIJKL PDB Code 4jeq Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes Classification ISOMERASE Compound TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL Source Trypanosoma brucei brucei (TPIS_TRYBB) Sequence A:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGA DVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKP EFVDIIKATQ B:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAIATPQQAQEAHALIRSWVSSKIGADVAGE LRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDI IKATQ C:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAIGKVATPQQAQEAHALIRSWVSSKIGADV AGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEF VDIIKATQ D:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGA DVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKP EFVDIIKATQ E:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGA DVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKP EFVDIIKATQ F:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAIGGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ G:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAVATPQQAQEAHALIRSWVSSKIGADVAGE LRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDI IKATQ H:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAATPQQAQEAHALIRSWVSSKIGADVAGELR ILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIK ATQ I:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAGKVATPQQAQEAHALIRSWVSSKIGADVA GELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFV DIIKATQ J:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAIGGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ K:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAIVATPQQAQEAHALIRSWVSSKIGADVAG ELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVD IIKATQ L:  MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCV VASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSL PILKDFGVNWIVLGHSERRAYYGDTNEIVADKVAAAVASG FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWA KVVIAYEPVWAKVATPQQAQEAHALIRSWVSSKIGADVAG ELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVD IIKATQ Description Functional site 1) chain A residue 213 type sequence S description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 2) chain A residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 A 301 source : AC1 3) chain A residue 20 type sequence S description BINDING SITE FOR RESIDUE PEG A 302 source : AC2 4) chain A residue 238 type sequence L description BINDING SITE FOR RESIDUE PEG A 302 source : AC2 5) chain A residue 50 type sequence M description BINDING SITE FOR RESIDUE PEG B 301 source : AC3 6) chain B residue 49 type sequence A description BINDING SITE FOR RESIDUE PEG B 301 source : AC3 7) chain B residue 52 type sequence K description BINDING SITE FOR RESIDUE PEG B 301 source : AC3 8) chain B residue 53 type sequence E description BINDING SITE FOR RESIDUE PEG B 301 source : AC3 9) chain B residue 86 type sequence F description BINDING SITE FOR RESIDUE PEG B 301 source : AC3 10) chain B residue 3 type sequence K description BINDING SITE FOR RESIDUE PEG B 302 source : AC4 11) chain B residue 223 type sequence Y description BINDING SITE FOR RESIDUE PEG B 302 source : AC4 12) chain B residue 224 type sequence Q description BINDING SITE FOR RESIDUE PEG B 302 source : AC4 13) chain B residue 250 type sequence Q description BINDING SITE FOR RESIDUE PEG B 302 source : AC4 14) chain C residue 11 type sequence N description BINDING SITE FOR RESIDUE PEG C 301 source : AC5 15) chain C residue 13 type sequence K description BINDING SITE FOR RESIDUE PEG C 301 source : AC5 16) chain C residue 95 type sequence H description BINDING SITE FOR RESIDUE PEG C 301 source : AC5 17) chain C residue 213 type sequence S description BINDING SITE FOR RESIDUE PEG C 301 source : AC5 18) chain C residue 235 type sequence G description BINDING SITE FOR RESIDUE PEG C 301 source : AC5 19) chain I residue 193 type sequence W description BINDING SITE FOR RESIDUE SO4 D 301 source : AC6 20) chain D residue 13 type sequence K description BINDING SITE FOR RESIDUE SO4 D 302 source : AC7 21) chain D residue 171 type sequence A description BINDING SITE FOR RESIDUE SO4 D 302 source : AC7 22) chain D residue 172 type sequence I description BINDING SITE FOR RESIDUE SO4 D 302 source : AC7 23) chain D residue 173 type sequence G description BINDING SITE FOR RESIDUE SO4 D 302 source : AC7 24) chain D residue 213 type sequence S description BINDING SITE FOR RESIDUE SO4 D 302 source : AC7 25) chain D residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 D 302 source : AC7 26) chain D residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 D 302 source : AC7 27) chain E residue 192 type sequence S description BINDING SITE FOR RESIDUE PEG E 301 source : AC8 28) chain H residue 13 type sequence K description BINDING SITE FOR RESIDUE SO4 H 301 source : AC9 29) chain H residue 212 type sequence G description BINDING SITE FOR RESIDUE SO4 H 301 source : AC9 30) chain H residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 H 301 source : AC9 31) chain H residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 H 301 source : AC9 32) chain K residue 13 type sequence K description BINDING SITE FOR RESIDUE SO4 K 301 source : BC1 33) chain K residue 234 type sequence G description BINDING SITE FOR RESIDUE SO4 K 301 source : BC1 34) chain K residue 235 type sequence G description BINDING SITE FOR RESIDUE SO4 K 301 source : BC1 35) chain A residue 165-175 type prosite sequence AYEPVWAIGTG description TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG source prosite : PS00171 36) chain A residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 37) chain J residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 38) chain K residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 39) chain L residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 40) chain B residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 41) chain C residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 42) chain D residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 43) chain E residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 44) chain F residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 45) chain G residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 46) chain H residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 47) chain I residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 48) chain A residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 49) chain J residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 50) chain K residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 51) chain L residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 52) chain B residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 53) chain C residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 54) chain D residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 55) chain E residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 56) chain F residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 57) chain G residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 58) chain H residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 59) chain I residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 60) chain A residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 61) chain E residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 62) chain F residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 63) chain F residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 64) chain G residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 65) chain G residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 66) chain H residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 67) chain H residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 68) chain I residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 69) chain I residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 70) chain J residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 71) chain A residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 72) chain J residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 73) chain K residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 74) chain K residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 75) chain L residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 76) chain L residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 77) chain B residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 78) chain B residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 79) chain C residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 80) chain C residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 81) chain D residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 82) chain D residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 83) chain E residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3

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