eF-site ID 5vrn-A PDB Code 5vrn Chain A 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:  TGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGF DRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEA IGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIH ISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWM TVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSA IVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKT VCALLSDWLPATTGDIIYADGGAHTQLL Description Functional site 1) chain A residue 14 type sequence G description binding site for residue 9JM A 300 source : AC1 2) chain A residue 15 type sequence I description binding site for residue 9JM A 300 source : AC1 3) chain A residue 16 type sequence I description binding site for residue 9JM A 300 source : AC1 4) chain A residue 20 type sequence S description binding site for residue 9JM A 300 source : AC1 5) chain A residue 21 type sequence I description binding site for residue 9JM A 300 source : AC1 6) chain A residue 41 type sequence F description binding site for residue 9JM A 300 source : AC1 7) chain A residue 63 type sequence L description binding site for residue 9JM A 300 source : AC1 8) chain A residue 64 type sequence D description binding site for residue 9JM A 300 source : AC1 9) chain A residue 65 type sequence V description binding site for residue 9JM A 300 source : AC1 10) chain A residue 94 type sequence S description binding site for residue 9JM A 300 source : AC1 11) chain A residue 95 type sequence I description binding site for residue 9JM A 300 source : AC1 12) chain A residue 96 type sequence G description binding site for residue 9JM A 300 source : AC1 13) chain A residue 122 type sequence I description binding site for residue 9JM A 300 source : AC1 14) chain A residue 147 type sequence M description binding site for residue 9JM A 300 source : AC1 15) chain A residue 148 type sequence D description binding site for residue 9JM A 300 source : AC1 16) chain A residue 149 type sequence F description binding site for residue 9JM A 300 source : AC1 17) chain A residue 158 type sequence Y description binding site for residue 9JM A 300 source : AC1 18) chain A residue 165 type sequence K description binding site for residue 9JM A 300 source : AC1 19) chain A residue 191 type sequence A description binding site for residue 9JM A 300 source : AC1 20) chain A residue 193 type sequence P description binding site for residue 9JM A 300 source : AC1 21) chain A residue 194 type sequence I description binding site for residue 9JM A 300 source : AC1 22) chain A residue 196 type sequence T description binding site for residue 9JM A 300 source : AC1 23) chain A residue 199 type sequence M description binding site for residue 9JM A 300 source : AC1 24) chain A residue 218 type sequence L description binding site for residue 9JM A 300 source : AC1 25) chain A residue 219 type sequence E description binding site for residue 9JM A 300 source : AC1 26) 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 27) 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 28) 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 29) 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 30) 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 31) 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 32) chain A residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 33) 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 34) chain A residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4

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