eF-site ID 5i3i-ABCD PDB Code 5i3i Chain A, B, C, D click to enlarge Title Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Classification ISOMERASE Compound Triosephosphate isomerase, glycosomal Source Trypanosoma brucei brucei (TPIS_TRYBB) Sequence A:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAAGTGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ B:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAAGTGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ C:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAAGTGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ D:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAAGTGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPE FVDIIKATQ Description Functional site 1) chain A residue 11 type sequence N description binding site for residue PGA A 301 source : AC1 2) chain A residue 13 type sequence K description binding site for residue PGA A 301 source : AC1 3) chain A residue 95 type sequence H description binding site for residue PGA A 301 source : AC1 4) chain A residue 167 type sequence E description binding site for residue PGA A 301 source : AC1 5) chain A residue 171 type sequence A description binding site for residue PGA A 301 source : AC1 6) chain A residue 173 type sequence G description binding site for residue PGA A 301 source : AC1 7) chain A residue 212 type sequence G description binding site for residue PGA A 301 source : AC1 8) chain A residue 213 type sequence S description binding site for residue PGA A 301 source : AC1 9) chain A residue 234 type sequence G description binding site for residue PGA A 301 source : AC1 10) chain A residue 235 type sequence G description binding site for residue PGA A 301 source : AC1 11) chain B residue 11 type sequence N description binding site for residue PGA B 301 source : AC2 12) chain B residue 13 type sequence K description binding site for residue PGA B 301 source : AC2 13) chain B residue 95 type sequence H description binding site for residue PGA B 301 source : AC2 14) chain B residue 167 type sequence E description binding site for residue PGA B 301 source : AC2 15) chain B residue 171 type sequence A description binding site for residue PGA B 301 source : AC2 16) chain B residue 172 type sequence A description binding site for residue PGA B 301 source : AC2 17) chain B residue 173 type sequence G description binding site for residue PGA B 301 source : AC2 18) chain B residue 212 type sequence G description binding site for residue PGA B 301 source : AC2 19) chain B residue 213 type sequence S description binding site for residue PGA B 301 source : AC2 20) chain B residue 234 type sequence G description binding site for residue PGA B 301 source : AC2 21) chain B residue 235 type sequence G description binding site for residue PGA B 301 source : AC2 22) chain C residue 11 type sequence N description binding site for residue PGA C 301 source : AC3 23) chain C residue 13 type sequence K description binding site for residue PGA C 301 source : AC3 24) chain C residue 95 type sequence H description binding site for residue PGA C 301 source : AC3 25) chain C residue 167 type sequence E description binding site for residue PGA C 301 source : AC3 26) chain C residue 171 type sequence A description binding site for residue PGA C 301 source : AC3 27) chain C residue 173 type sequence G description binding site for residue PGA C 301 source : AC3 28) chain C residue 212 type sequence G description binding site for residue PGA C 301 source : AC3 29) chain C residue 213 type sequence S description binding site for residue PGA C 301 source : AC3 30) chain C residue 234 type sequence G description binding site for residue PGA C 301 source : AC3 31) chain C residue 235 type sequence G description binding site for residue PGA C 301 source : AC3 32) chain D residue 11 type sequence N description binding site for residue PGA D 301 source : AC4 33) chain D residue 13 type sequence K description binding site for residue PGA D 301 source : AC4 34) chain D residue 95 type sequence H description binding site for residue PGA D 301 source : AC4 35) chain D residue 167 type sequence E description binding site for residue PGA D 301 source : AC4 36) chain D residue 171 type sequence A description binding site for residue PGA D 301 source : AC4 37) chain D residue 172 type sequence A description binding site for residue PGA D 301 source : AC4 38) chain D residue 173 type sequence G description binding site for residue PGA D 301 source : AC4 39) chain D residue 212 type sequence G description binding site for residue PGA D 301 source : AC4 40) chain D residue 213 type sequence S description binding site for residue PGA D 301 source : AC4 41) chain D residue 234 type sequence G description binding site for residue PGA D 301 source : AC4 42) chain D residue 235 type sequence G description binding site for residue PGA D 301 source : AC4 43) chain B residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 44) chain C residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 45) chain D residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 46) chain A residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 47) chain B residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 48) chain C residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 49) chain D residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 50) chain A residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 51) chain B residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 52) chain B residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 53) chain C residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 54) chain C residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 55) chain D residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 56) chain D residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 57) chain A residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 58) chain A residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3

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