eF-site ID 1ml1-ACEGIK PDB Code 1ml1 Chain A, C, E, G, I, K click to enlarge Title PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATE ISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OF A SEVEN RESIDUE LOOP Classification ISOMERASE Compound TRIOSEPHOSPHATE ISOMERASE Source null (TPIS_TRYBB) Sequence A:  SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVA STFVHLAMTKERLSHPKFVIAAQNAGNADALASLKDFGVN WIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGE TLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPV WAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRIL YGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKAT Q C:  SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVA STFVHLAMTKERLSHPKFVIAAQNAGNADALASLKDFGVN WIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGE TLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPV WAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRIL YGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKAT Q E:  SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVA STFVHLAMTKERLSHPKFVIAAQNAGNADALASLKDFGVN WIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGE TLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPV WAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRIL YGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKAT Q G:  SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVA STFVHLAMTKERLSHPKFVIAAQNAGNADALASLKDFGVN WIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGE TLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPV WAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRIL YGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKAT Q I:  SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVA STFVHLAMTKERLSHPKFVIAAQNAGNADALASLKDFGVN WIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGE TLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPV WAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRIL YGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKAT Q K:  SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVA STFVHLAMTKERLSHPKFVIAAQNAGNADALASLKDFGVN WIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGE TLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPV WAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRIL YGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKAT Q Description Functional site 1) chain A residue 11 type sequence N description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 2) chain A residue 13 type sequence K description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 3) chain A residue 95 type sequence H description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 4) chain A residue 167 type sequence E description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 5) chain A residue 172 type sequence I description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 6) chain A residue 173 type sequence G description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 7) chain A residue 213 type sequence S description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 8) chain A residue 234 type sequence G description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 9) chain A residue 235 type sequence G description BINDING SITE FOR RESIDUE PGA A 600 source : AC1 10) chain C residue 11 type sequence N description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 11) chain C residue 13 type sequence K description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 12) chain C residue 95 type sequence H description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 13) chain C residue 167 type sequence E description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 14) chain C residue 172 type sequence I description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 15) chain C residue 173 type sequence G description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 16) chain C residue 213 type sequence S description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 17) chain C residue 234 type sequence G description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 18) chain C residue 235 type sequence G description BINDING SITE FOR RESIDUE PGA C 600 source : AC2 19) chain E residue 11 type sequence N description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 20) chain E residue 13 type sequence K description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 21) chain E residue 95 type sequence H description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 22) chain E residue 167 type sequence E description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 23) chain E residue 172 type sequence I description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 24) chain E residue 173 type sequence G description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 25) chain E residue 213 type sequence S description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 26) chain E residue 234 type sequence G description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 27) chain E residue 235 type sequence G description BINDING SITE FOR RESIDUE PGA E 600 source : AC3 28) chain G residue 11 type sequence N description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 29) chain G residue 13 type sequence K description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 30) chain G residue 95 type sequence H description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 31) chain G residue 167 type sequence E description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 32) chain G residue 172 type sequence I description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 33) chain G residue 173 type sequence G description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 34) chain G residue 213 type sequence S description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 35) chain G residue 234 type sequence G description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 36) chain G residue 235 type sequence G description BINDING SITE FOR RESIDUE PGA G 600 source : AC4 37) chain I residue 11 type sequence N description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 38) chain I residue 13 type sequence K description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 39) chain I residue 95 type sequence H description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 40) chain I residue 167 type sequence E description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 41) chain I residue 172 type sequence I description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 42) chain I residue 173 type sequence G description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 43) chain I residue 213 type sequence S description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 44) chain I residue 234 type sequence G description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 45) chain I residue 235 type sequence G description BINDING SITE FOR RESIDUE PGA I 600 source : AC5 46) chain K residue 11 type sequence N description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 47) chain K residue 13 type sequence K description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 48) chain K residue 95 type sequence H description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 49) chain K residue 167 type sequence E description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 50) chain K residue 172 type sequence I description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 51) chain K residue 173 type sequence G description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 52) chain K residue 213 type sequence S description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 53) chain K residue 234 type sequence G description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 54) chain K residue 235 type sequence G description BINDING SITE FOR RESIDUE PGA K 600 source : AC6 55) chain A residue 165-175 type prosite sequence AYEPVWAIGTG description TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG source prosite : PS00171 56) chain C residue 102 type ACT_SITE sequence Y description Electrophile source Swiss-Prot : SWS_FT_FI1 57) chain E residue 102 type ACT_SITE sequence Y description Electrophile source Swiss-Prot : SWS_FT_FI1 58) chain G residue 102 type ACT_SITE sequence Y description Electrophile source Swiss-Prot : SWS_FT_FI1 59) chain I residue 102 type ACT_SITE sequence Y description Electrophile source Swiss-Prot : SWS_FT_FI1 60) chain K residue 102 type ACT_SITE sequence Y description Electrophile source Swiss-Prot : SWS_FT_FI1 61) chain A residue 102 type ACT_SITE sequence Y description Electrophile source Swiss-Prot : SWS_FT_FI1 62) chain C residue 174 type ACT_SITE sequence T description Proton acceptor source Swiss-Prot : SWS_FT_FI2 63) chain E residue 174 type ACT_SITE sequence T description Proton acceptor source Swiss-Prot : SWS_FT_FI2 64) chain G residue 174 type ACT_SITE sequence T description Proton acceptor source Swiss-Prot : SWS_FT_FI2 65) chain I residue 174 type ACT_SITE sequence T description Proton acceptor source Swiss-Prot : SWS_FT_FI2 66) chain K residue 174 type ACT_SITE sequence T description Proton acceptor source Swiss-Prot : SWS_FT_FI2 67) chain A residue 174 type ACT_SITE sequence T description Proton acceptor source Swiss-Prot : SWS_FT_FI2 68) chain C residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 69) chain C residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 70) chain E residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 71) chain E residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 72) chain G residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 73) chain G residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 74) chain I residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 75) chain I residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 76) chain K residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 77) chain K residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 78) chain A residue 11 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 79) chain A residue 13 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3

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