eF-site ID 5vrm-ABCD PDB Code 5vrm Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURE OF THE INHA FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AN12855, EBSI 4333. Classification OXIDOREDUCTASE Compound Enoyl-[acyl-carrier-protein] reductase [NADH] Source (INHA_MYCTO) Sequence A:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI GAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHI SAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMT VAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAG AQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPA TTGDIIYADGGAHTQLL B:  TGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGF DRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEA IGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIH ISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWM TVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMQL LEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDI IYADGGAHTQLL C:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI GAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHI SAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMT VAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAI QLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTG DIIYADGGAHTQLL D:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI GAGNKLDGVVHSIGFMPQPFFDAPYADVSKGIHISAYSYA SMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSAL ESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIEAGAQI QLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTG DIIYADGGAHTQLL Description Functional site 1) chain A residue 14 type sequence G description binding site for residue 9JJ A 300 source : AC1 2) chain A residue 15 type sequence I description binding site for residue 9JJ A 300 source : AC1 3) chain A residue 16 type sequence I description binding site for residue 9JJ A 300 source : AC1 4) chain A residue 20 type sequence S description binding site for residue 9JJ A 300 source : AC1 5) chain A residue 21 type sequence I description binding site for residue 9JJ A 300 source : AC1 6) chain A residue 41 type sequence F description binding site for residue 9JJ A 300 source : AC1 7) chain A residue 63 type sequence L description binding site for residue 9JJ A 300 source : AC1 8) chain A residue 64 type sequence D description binding site for residue 9JJ A 300 source : AC1 9) chain A residue 65 type sequence V description binding site for residue 9JJ A 300 source : AC1 10) chain A residue 94 type sequence S description binding site for residue 9JJ A 300 source : AC1 11) chain A residue 95 type sequence I description binding site for residue 9JJ A 300 source : AC1 12) chain A residue 96 type sequence G description binding site for residue 9JJ A 300 source : AC1 13) chain A residue 122 type sequence I description binding site for residue 9JJ A 300 source : AC1 14) chain A residue 147 type sequence M description binding site for residue 9JJ A 300 source : AC1 15) chain A residue 148 type sequence D description binding site for residue 9JJ A 300 source : AC1 16) chain A residue 149 type sequence F description binding site for residue 9JJ A 300 source : AC1 17) chain A residue 165 type sequence K description binding site for residue 9JJ A 300 source : AC1 18) chain A residue 192 type sequence G description binding site for residue 9JJ A 300 source : AC1 19) chain A residue 193 type sequence P description binding site for residue 9JJ A 300 source : AC1 20) chain A residue 194 type sequence I description binding site for residue 9JJ A 300 source : AC1 21) chain A residue 196 type sequence T description binding site for residue 9JJ A 300 source : AC1 22) chain A residue 198 type sequence A description binding site for residue 9JJ A 300 source : AC1 23) chain A residue 199 type sequence M description binding site for residue 9JJ A 300 source : AC1 24) chain B residue 14 type sequence G description binding site for residue 9JJ B 300 source : AC2 25) chain B residue 15 type sequence I description binding site for residue 9JJ B 300 source : AC2 26) chain B residue 16 type sequence I description binding site for residue 9JJ B 300 source : AC2 27) chain B residue 20 type sequence S description binding site for residue 9JJ B 300 source : AC2 28) chain B residue 21 type sequence I description binding site for residue 9JJ B 300 source : AC2 29) chain B residue 41 type sequence F description binding site for residue 9JJ B 300 source : AC2 30) chain B residue 63 type sequence L description binding site for residue 9JJ B 300 source : AC2 31) chain B residue 64 type sequence D description binding site for residue 9JJ B 300 source : AC2 32) chain B residue 65 type sequence V description binding site for residue 9JJ B 300 source : AC2 33) chain B residue 94 type sequence S description binding site for residue 9JJ B 300 source : AC2 34) chain B residue 95 type sequence I description binding site for residue 9JJ B 300 source : AC2 35) chain B residue 96 type sequence G description binding site for residue 9JJ B 300 source : AC2 36) chain B residue 122 type sequence I description binding site for residue 9JJ B 300 source : AC2 37) chain B residue 147 type sequence M description binding site for residue 9JJ B 300 source : AC2 38) chain B residue 148 type sequence D description binding site for residue 9JJ B 300 source : AC2 39) chain B residue 149 type sequence F description binding site for residue 9JJ B 300 source : AC2 40) chain B residue 158 type sequence Y description binding site for residue 9JJ B 300 source : AC2 41) chain B residue 161 type sequence M description binding site for residue 9JJ B 300 source : AC2 42) chain B residue 165 type sequence K description binding site for residue 9JJ B 300 source : AC2 43) chain B residue 192 type sequence G description binding site for residue 9JJ B 300 source : AC2 44) chain B residue 193 type sequence P description binding site for residue 9JJ B 300 source : AC2 45) chain B residue 194 type sequence I description binding site for residue 9JJ B 300 source : AC2 46) chain B residue 196 type sequence T description binding site for residue 9JJ B 300 source : AC2 47) chain B residue 198 type sequence A description binding site for residue 9JJ B 300 source : AC2 48) chain B residue 199 type sequence M description binding site for residue 9JJ B 300 source : AC2 49) chain C residue 14 type sequence G description binding site for residue 9JJ C 300 source : AC3 50) chain C residue 15 type sequence I description binding site for residue 9JJ C 300 source : AC3 51) chain C residue 16 type sequence I description binding site for residue 9JJ C 300 source : AC3 52) chain C residue 20 type sequence S description binding site for residue 9JJ C 300 source : AC3 53) chain C residue 21 type sequence I description binding site for residue 9JJ C 300 source : AC3 54) chain C residue 41 type sequence F description binding site for residue 9JJ C 300 source : AC3 55) chain C residue 63 type sequence L description binding site for residue 9JJ C 300 source : AC3 56) chain C residue 64 type sequence D description binding site for residue 9JJ C 300 source : AC3 57) chain C residue 65 type sequence V description binding site for residue 9JJ C 300 source : AC3 58) chain C residue 94 type sequence S description binding site for residue 9JJ C 300 source : AC3 59) chain C residue 95 type sequence I description binding site for residue 9JJ C 300 source : AC3 60) chain C residue 96 type sequence G description binding site for residue 9JJ C 300 source : AC3 61) chain C residue 122 type sequence I description binding site for residue 9JJ C 300 source : AC3 62) chain C residue 147 type sequence M description binding site for residue 9JJ C 300 source : AC3 63) chain C residue 148 type sequence D description binding site for residue 9JJ C 300 source : AC3 64) chain C residue 149 type sequence F description binding site for residue 9JJ C 300 source : AC3 65) chain C residue 156 type sequence P description binding site for residue 9JJ C 300 source : AC3 66) chain C residue 158 type sequence Y description binding site for residue 9JJ C 300 source : AC3 67) chain C residue 161 type sequence M description binding site for residue 9JJ C 300 source : AC3 68) chain C residue 165 type sequence K description binding site for residue 9JJ C 300 source : AC3 69) chain C residue 191 type sequence A description binding site for residue 9JJ C 300 source : AC3 70) chain C residue 192 type sequence G description binding site for residue 9JJ C 300 source : AC3 71) chain C residue 193 type sequence P description binding site for residue 9JJ C 300 source : AC3 72) chain C residue 194 type sequence I description binding site for residue 9JJ C 300 source : AC3 73) chain C residue 196 type sequence T description binding site for residue 9JJ C 300 source : AC3 74) chain C residue 198 type sequence A description binding site for residue 9JJ C 300 source : AC3 75) chain C residue 202 type sequence I description binding site for residue 9JJ C 300 source : AC3 76) chain D residue 14 type sequence G description binding site for residue 9JJ D 300 source : AC4 77) chain D residue 15 type sequence I description binding site for residue 9JJ D 300 source : AC4 78) chain D residue 16 type sequence I description binding site for residue 9JJ D 300 source : AC4 79) chain D residue 20 type sequence S description binding site for residue 9JJ D 300 source : AC4 80) chain D residue 21 type sequence I description binding site for residue 9JJ D 300 source : AC4 81) chain D residue 41 type sequence F description binding site for residue 9JJ D 300 source : AC4 82) chain D residue 63 type sequence L description binding site for residue 9JJ D 300 source : AC4 83) chain D residue 64 type sequence D description binding site for residue 9JJ D 300 source : AC4 84) chain D residue 65 type sequence V description binding site for residue 9JJ D 300 source : AC4 85) chain D residue 95 type sequence I description binding site for residue 9JJ D 300 source : AC4 86) chain D residue 96 type sequence G description binding site for residue 9JJ D 300 source : AC4 87) chain D residue 97 type sequence F description binding site for residue 9JJ D 300 source : AC4 88) chain D residue 98 type sequence M description binding site for residue 9JJ D 300 source : AC4 89) chain D residue 99 type sequence P description binding site for residue 9JJ D 300 source : AC4 90) chain D residue 100 type sequence Q description binding site for residue 9JJ D 300 source : AC4 91) chain D residue 122 type sequence I description binding site for residue 9JJ D 300 source : AC4 92) chain D residue 147 type sequence M description binding site for residue 9JJ D 300 source : AC4 93) chain D residue 148 type sequence D description binding site for residue 9JJ D 300 source : AC4 94) chain D residue 157 type sequence A description binding site for residue 9JJ D 300 source : AC4 95) chain D residue 158 type sequence Y description binding site for residue 9JJ D 300 source : AC4 96) chain D residue 159 type sequence N description binding site for residue 9JJ D 300 source : AC4 97) chain D residue 161 type sequence M description binding site for residue 9JJ D 300 source : AC4 98) chain D residue 165 type sequence K description binding site for residue 9JJ D 300 source : AC4 99) chain D residue 191 type sequence A description binding site for residue 9JJ D 300 source : AC4 100) chain D residue 193 type sequence P description binding site for residue 9JJ D 300 source : AC4 101) chain D residue 194 type sequence I description binding site for residue 9JJ D 300 source : AC4 102) chain D residue 196 type sequence T description binding site for residue 9JJ D 300 source : AC4 103) chain A residue 266 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326 source Swiss-Prot : SWS_FT_FI5 104) chain B residue 266 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326 source Swiss-Prot : SWS_FT_FI5 105) chain C residue 266 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326 source Swiss-Prot : SWS_FT_FI5 106) chain D residue 266 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326 source Swiss-Prot : SWS_FT_FI5 107) chain A residue 20 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 108) chain B residue 194 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 109) chain C residue 20 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 110) chain C residue 64 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 111) chain C residue 95 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 112) chain C residue 165 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 113) chain C residue 194 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 114) chain D residue 20 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 115) chain D residue 64 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 116) chain D residue 95 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 117) chain D residue 165 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 118) chain A residue 64 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 119) chain D residue 194 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 120) chain A residue 95 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 121) chain A residue 165 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 122) chain A residue 194 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 123) chain B residue 20 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 124) chain B residue 64 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 125) chain B residue 95 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 126) chain B residue 165 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 source Swiss-Prot : SWS_FT_FI1 127) chain A residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 128) chain B residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 129) chain C residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 130) chain D residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 131) chain A residue 149 type SITE sequence F description May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454 source Swiss-Prot : SWS_FT_FI3 132) chain B residue 149 type SITE sequence F description May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454 source Swiss-Prot : SWS_FT_FI3 133) chain C residue 149 type SITE sequence F description May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454 source Swiss-Prot : SWS_FT_FI3 134) chain D residue 149 type SITE sequence F description May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454 source Swiss-Prot : SWS_FT_FI3 135) chain A residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4 136) chain B residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4 137) chain C residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4 138) chain D residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4

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