eF-site ID 5i3k-ABCD PDB Code 5i3k 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 VVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFAVGGASLKPE FVDIIKATQ B:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFAVGGASLKPE FVDIIKATQ C:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFAVGGASLKPE FVDIIKATQ D:  SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVV ASTFVHLAMTKERLSHPKFVIAAQNAIAKSGAFTGEVSLP ILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASGF MVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAK VVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGAD VAGELRILYGGSVNGKNARTLYQQRDVNGFAVGGASLKPE FVDIIKATQ Description Functional site 1) chain A residue 160 type sequence A description binding site for residue NA A 301 source : AC1 2) chain B residue 13 type sequence K description binding site for residue PGA B 301 source : AC3 3) chain B residue 167 type sequence E description binding site for residue PGA B 301 source : AC3 4) chain B residue 171 type sequence A description binding site for residue PGA B 301 source : AC3 5) chain B residue 172 type sequence I description binding site for residue PGA B 301 source : AC3 6) chain B residue 173 type sequence G description binding site for residue PGA B 301 source : AC3 7) chain B residue 234 type sequence G description binding site for residue PGA B 301 source : AC3 8) chain B residue 235 type sequence G description binding site for residue PGA B 301 source : AC3 9) chain C residue 13 type sequence K description binding site for residue PGA C 301 source : AC4 10) chain C residue 167 type sequence E description binding site for residue PGA C 301 source : AC4 11) chain C residue 171 type sequence A description binding site for residue PGA C 301 source : AC4 12) chain C residue 172 type sequence I description binding site for residue PGA C 301 source : AC4 13) chain C residue 173 type sequence G description binding site for residue PGA C 301 source : AC4 14) chain C residue 212 type sequence G description binding site for residue PGA C 301 source : AC4 15) chain C residue 214 type sequence V description binding site for residue PGA C 301 source : AC4 16) chain C residue 232 type sequence A description binding site for residue PGA C 301 source : AC4 17) chain C residue 234 type sequence G description binding site for residue PGA C 301 source : AC4 18) chain C residue 235 type sequence G description binding site for residue PGA C 301 source : AC4 19) chain C residue 74 type sequence F description binding site for residue NA C 302 source : AC5 20) chain D residue 13 type sequence K description binding site for residue PGA D 301 source : AC6 21) chain D residue 167 type sequence E description binding site for residue PGA D 301 source : AC6 22) chain D residue 172 type sequence I description binding site for residue PGA D 301 source : AC6 23) chain D residue 173 type sequence G description binding site for residue PGA D 301 source : AC6 24) chain D residue 212 type sequence G description binding site for residue PGA D 301 source : AC6 25) chain D residue 232 type sequence A description binding site for residue PGA D 301 source : AC6 26) chain D residue 234 type sequence G description binding site for residue PGA D 301 source : AC6 27) chain D residue 235 type sequence G description binding site for residue PGA D 301 source : AC6 28) chain A residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 29) chain B residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 30) chain C residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 31) chain D residue 95 type ACT_SITE sequence H description Electrophile source Swiss-Prot : SWS_FT_FI1 32) chain A residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 33) chain A residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 34) chain B residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 35) chain B residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 36) chain C residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 37) chain C residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 38) chain D residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 39) chain D residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 40) chain A residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 41) chain B residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 42) chain C residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 43) chain D residue 167 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 44) chain A residue 165-175 type prosite sequence AYEPVWAIGTG description TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG source prosite : PS00171

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