eF-site ID 1yrl-ABCD PDB Code 1yrl Chain A, B, C, D click to enlarge Title Escherichia coli ketol-acid reductoisomerase Classification OXIDOREDUCTASE Compound Ketol-acid reductoisomerase Source Escherichia coli (strain K12) (ILVC_ECOLI) Sequence A:  NYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVI VGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKA TENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQPLM KDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVR EEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHR AGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVE EGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAK LRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWAN DDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMI AMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIA RKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPG DLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGYMT DMKRIAV B:  NYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQYEELIP QADLVINLTPDKQHSDVVRTVQPLMKDGAALGYSHGFNIV EVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAV HPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSD LMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFG WETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMA PLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKT AFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMV DSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTA EYGNYLFSYACVPLLKPFMAELQPGDLGKAIPEGAVDNGQ LRDVNEAIRSHAIEQVGKKLRGYMTDMKRIA C:  NYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVI VGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKA TENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQPLM KDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVR EEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHR AGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVE EGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAK LRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWAN DDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMI AMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIA RKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPG DLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGYMT DMKRIAV D:  NYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVI VLNQGLNMRDSGLDISYALRKEAIAEGFKVGTYEELIPQA DLVINLTPDKQHSDVVRTVQPLMKDGAALGYSHGFNIVEV GEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHP ENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLM GEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWE TITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPL FQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAF ETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVDS GIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEY GNYLFSYACVPLLKPFMAELQPGDLGKAIPEGAVDNGQLR DVNEAIRSHAIEQVGKKLRGYMTDMKRIAV Description Functional site 1) chain A residue 3 type sequence N description BINDING SITE FOR RESIDUE SO4 A 4121 source : AC1 2) chain A residue 6 type sequence N description BINDING SITE FOR RESIDUE SO4 A 4121 source : AC1 3) chain A residue 11 type sequence R description BINDING SITE FOR RESIDUE SO4 A 4122 source : AC2 4) chain A residue 12 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 4122 source : AC2 5) chain D residue 3 type sequence N description BINDING SITE FOR RESIDUE SO4 D 4123 source : AC3 6) chain D residue 6 type sequence N description BINDING SITE FOR RESIDUE SO4 D 4123 source : AC3 7) chain A residue 301 type sequence Q description BINDING SITE FOR RESIDUE SO4 D 4124 source : AC4 8) chain D residue 11 type sequence R description BINDING SITE FOR RESIDUE SO4 D 4124 source : AC4 9) chain D residue 12 type sequence Q description BINDING SITE FOR RESIDUE SO4 D 4124 source : AC4 10) chain C residue 11 type sequence R description BINDING SITE FOR RESIDUE SO4 C 4125 source : AC5 11) chain C residue 12 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 4125 source : AC5 12) chain B residue 11 type sequence R description BINDING SITE FOR RESIDUE SO4 B 4126 source : AC6 13) chain B residue 12 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 4126 source : AC6 14) chain A residue 71 type sequence A description BINDING SITE FOR RESIDUE SO4 A 4127 source : AC7 15) chain A residue 76 type sequence R description BINDING SITE FOR RESIDUE SO4 A 4127 source : AC7 16) chain A residue 78 type sequence S description BINDING SITE FOR RESIDUE SO4 A 4127 source : AC7 17) chain A residue 201 type sequence H description BINDING SITE FOR RESIDUE SO4 A 4128 source : AC8 18) chain A residue 202 type sequence R description BINDING SITE FOR RESIDUE SO4 A 4128 source : AC8 19) chain D residue 201 type sequence H description BINDING SITE FOR RESIDUE SO4 D 4129 source : AC9 20) chain D residue 202 type sequence R description BINDING SITE FOR RESIDUE SO4 D 4129 source : AC9 21) chain A residue 159 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 22) chain D residue 159 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 23) chain D residue 222 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 24) chain D residue 415 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 222 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 415 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 159 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 28) chain B residue 222 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 29) chain B residue 415 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 30) chain C residue 159 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 31) chain C residue 222 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 32) chain C residue 415 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 77 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858, ECO:0000305|PubMed:9015391 source Swiss-Prot : SWS_FT_FI4 34) chain C residue 77 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858, ECO:0000305|PubMed:9015391 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 133 type ACT_SITE sequence G description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 133 type ACT_SITE sequence G description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI1 37) chain C residue 133 type ACT_SITE sequence G description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI1 38) chain D residue 133 type ACT_SITE sequence G description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00435 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 46 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 218 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 390 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 394 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 43) chain C residue 46 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 44) chain C residue 79 type BINDING sequence W description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 45) chain C residue 109 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 46) chain C residue 218 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 47) chain C residue 390 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 48) chain C residue 394 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 79 type BINDING sequence W description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 50) chain D residue 109 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 51) chain D residue 218 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 52) chain D residue 390 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 53) chain D residue 394 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 109 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 218 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 390 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 394 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 109 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 69 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:9015391 source Swiss-Prot : SWS_FT_FI3 60) chain C residue 69 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:9015391 source Swiss-Prot : SWS_FT_FI3 61) chain D residue 69 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:9015391 source Swiss-Prot : SWS_FT_FI3

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