eF-site ID 5vrn-C PDB Code 5vrn Chain C 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 C:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI GAGNKLDGVVHSIGFMPQPFFDAPYADVSKGIHISAYSYA SMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSAL ESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALG EEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSD WLPATTGDIIYADGGAHTQLL Description Functional site 1) chain C residue 14 type sequence G description binding site for residue 9JM C 300 source : AC3 2) chain C residue 15 type sequence I description binding site for residue 9JM C 300 source : AC3 3) chain C residue 16 type sequence I description binding site for residue 9JM C 300 source : AC3 4) chain C residue 20 type sequence S description binding site for residue 9JM C 300 source : AC3 5) chain C residue 21 type sequence I description binding site for residue 9JM C 300 source : AC3 6) chain C residue 41 type sequence F description binding site for residue 9JM C 300 source : AC3 7) chain C residue 63 type sequence L description binding site for residue 9JM C 300 source : AC3 8) chain C residue 64 type sequence D description binding site for residue 9JM C 300 source : AC3 9) chain C residue 65 type sequence V description binding site for residue 9JM C 300 source : AC3 10) chain C residue 94 type sequence S description binding site for residue 9JM C 300 source : AC3 11) chain C residue 95 type sequence I description binding site for residue 9JM C 300 source : AC3 12) chain C residue 96 type sequence G description binding site for residue 9JM C 300 source : AC3 13) chain C residue 122 type sequence I description binding site for residue 9JM C 300 source : AC3 14) chain C residue 147 type sequence M description binding site for residue 9JM C 300 source : AC3 15) chain C residue 148 type sequence D description binding site for residue 9JM C 300 source : AC3 16) chain C residue 149 type sequence F description binding site for residue 9JM C 300 source : AC3 17) chain C residue 158 type sequence Y description binding site for residue 9JM C 300 source : AC3 18) chain C residue 161 type sequence M description binding site for residue 9JM C 300 source : AC3 19) chain C residue 165 type sequence K description binding site for residue 9JM C 300 source : AC3 20) chain C residue 191 type sequence A description binding site for residue 9JM C 300 source : AC3 21) chain C residue 193 type sequence P description binding site for residue 9JM C 300 source : AC3 22) chain C residue 194 type sequence I description binding site for residue 9JM C 300 source : AC3 23) chain C residue 196 type sequence T description binding site for residue 9JM C 300 source : AC3 24) chain C residue 199 type sequence M description binding site for residue 9JM C 300 source : AC3 25) chain C residue 215 type sequence I description binding site for residue 9JM C 300 source : AC3 26) chain C residue 218 type sequence L description binding site for residue 9JM C 300 source : AC3 27) chain C residue 219 type sequence E description binding site for residue 9JM C 300 source : AC3 28) 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 29) 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 30) 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 31) 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 32) 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 33) 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 34) chain C residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 35) 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 36) chain C residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4

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