eF-site ID 5vrm-D PDB Code 5vrm Chain 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 D:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI GAGNKLDGVVHSIGFMPQPFFDAPYADVSKGIHISAYSYA SMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSAL ESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIEAGAQI QLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTG DIIYADGGAHTQLL Description Functional site 1) chain D residue 14 type sequence G description binding site for residue 9JJ D 300 source : AC4 2) chain D residue 15 type sequence I description binding site for residue 9JJ D 300 source : AC4 3) chain D residue 16 type sequence I description binding site for residue 9JJ D 300 source : AC4 4) chain D residue 20 type sequence S description binding site for residue 9JJ D 300 source : AC4 5) chain D residue 21 type sequence I description binding site for residue 9JJ D 300 source : AC4 6) chain D residue 41 type sequence F description binding site for residue 9JJ D 300 source : AC4 7) chain D residue 63 type sequence L description binding site for residue 9JJ D 300 source : AC4 8) chain D residue 64 type sequence D description binding site for residue 9JJ D 300 source : AC4 9) chain D residue 65 type sequence V description binding site for residue 9JJ D 300 source : AC4 10) chain D residue 95 type sequence I description binding site for residue 9JJ D 300 source : AC4 11) chain D residue 96 type sequence G description binding site for residue 9JJ D 300 source : AC4 12) chain D residue 97 type sequence F description binding site for residue 9JJ D 300 source : AC4 13) chain D residue 98 type sequence M description binding site for residue 9JJ D 300 source : AC4 14) chain D residue 99 type sequence P description binding site for residue 9JJ D 300 source : AC4 15) chain D residue 100 type sequence Q description binding site for residue 9JJ D 300 source : AC4 16) chain D residue 122 type sequence I description binding site for residue 9JJ D 300 source : AC4 17) chain D residue 147 type sequence M description binding site for residue 9JJ D 300 source : AC4 18) chain D residue 148 type sequence D description binding site for residue 9JJ D 300 source : AC4 19) chain D residue 157 type sequence A description binding site for residue 9JJ D 300 source : AC4 20) chain D residue 158 type sequence Y description binding site for residue 9JJ D 300 source : AC4 21) chain D residue 159 type sequence N description binding site for residue 9JJ D 300 source : AC4 22) chain D residue 161 type sequence M description binding site for residue 9JJ D 300 source : AC4 23) chain D residue 165 type sequence K description binding site for residue 9JJ D 300 source : AC4 24) chain D residue 191 type sequence A description binding site for residue 9JJ D 300 source : AC4 25) chain D residue 193 type sequence P description binding site for residue 9JJ D 300 source : AC4 26) chain D residue 194 type sequence I description binding site for residue 9JJ D 300 source : AC4 27) chain D residue 196 type sequence T description binding site for residue 9JJ D 300 source : AC4 28) 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 29) 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 30) 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 31) 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 32) 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 33) chain D residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 34) 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 35) chain D residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4 36) 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

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