eF-site ID 4u0k-A PDB Code 4u0k Chain A click to enlarge Title Crystal structure of Mycobacterium tuberculosis enoyl reductase complexed with N-(5-chloro-2-methylphenyl)-1-cyclohexyl-5-oxopyrrolidine-3-carboxamide Classification OXIDOREDUCTASE Compound Enoyl-[acyl-carrier-protein] reductase [NADH] Source (INHA_MYCTU) Sequence A:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI GAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHI SAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMT VAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAI VGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTV CALLSDWLPATTGDIIYADGGAHTQLL Description Functional site 1) chain A residue 14 type sequence G description binding site for residue NAD A 500 source : AC1 2) chain A residue 15 type sequence I description binding site for residue NAD A 500 source : AC1 3) chain A residue 16 type sequence I description binding site for residue NAD A 500 source : AC1 4) chain A residue 20 type sequence S description binding site for residue NAD A 500 source : AC1 5) chain A residue 21 type sequence I description binding site for residue NAD A 500 source : AC1 6) chain A residue 41 type sequence F description binding site for residue NAD A 500 source : AC1 7) chain A residue 63 type sequence L description binding site for residue NAD A 500 source : AC1 8) chain A residue 64 type sequence D description binding site for residue NAD A 500 source : AC1 9) chain A residue 65 type sequence V description binding site for residue NAD A 500 source : AC1 10) chain A residue 94 type sequence S description binding site for residue NAD A 500 source : AC1 11) chain A residue 95 type sequence I description binding site for residue NAD A 500 source : AC1 12) chain A residue 96 type sequence G description binding site for residue NAD A 500 source : AC1 13) chain A residue 122 type sequence I description binding site for residue NAD A 500 source : AC1 14) chain A residue 147 type sequence M description binding site for residue NAD A 500 source : AC1 15) chain A residue 148 type sequence D description binding site for residue NAD A 500 source : AC1 16) chain A residue 149 type sequence F description binding site for residue NAD A 500 source : AC1 17) chain A residue 165 type sequence K description binding site for residue NAD A 500 source : AC1 18) chain A residue 192 type sequence G description binding site for residue NAD A 500 source : AC1 19) chain A residue 193 type sequence P description binding site for residue NAD A 500 source : AC1 20) chain A residue 194 type sequence I description binding site for residue NAD A 500 source : AC1 21) chain A residue 196 type sequence T description binding site for residue NAD A 500 source : AC1 22) chain A residue 96 type sequence G description binding site for residue 744 A 501 source : AC2 23) chain A residue 103 type sequence M description binding site for residue 744 A 501 source : AC2 24) chain A residue 149 type sequence F description binding site for residue 744 A 501 source : AC2 25) chain A residue 156 type sequence P description binding site for residue 744 A 501 source : AC2 26) chain A residue 157 type sequence A description binding site for residue 744 A 501 source : AC2 27) chain A residue 158 type sequence Y description binding site for residue 744 A 501 source : AC2 28) chain A residue 161 type sequence M description binding site for residue 744 A 501 source : AC2 29) chain A residue 199 type sequence M description binding site for residue 744 A 501 source : AC2 30) chain A residue 215 type sequence I description binding site for residue 744 A 501 source : AC2 31) chain A residue 218 type sequence L description binding site for residue 744 A 501 source : AC2 32) 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 33) 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 34) 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 35) 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 36) 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 37) chain A residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 38) 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 39) chain A residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4 40) 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

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