eF-site ID 5vrn-F PDB Code 5vrn Chain F 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 F:  GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFD RLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAI GAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHI SAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMT VAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAI VGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTV CALLSDWLPATTGDIIYADGGAHTQLL Description Functional site 1) chain F residue 14 type sequence G description binding site for residue 9JM F 300 source : AC6 2) chain F residue 15 type sequence I description binding site for residue 9JM F 300 source : AC6 3) chain F residue 16 type sequence I description binding site for residue 9JM F 300 source : AC6 4) chain F residue 20 type sequence S description binding site for residue 9JM F 300 source : AC6 5) chain F residue 21 type sequence I description binding site for residue 9JM F 300 source : AC6 6) chain F residue 41 type sequence F description binding site for residue 9JM F 300 source : AC6 7) chain F residue 63 type sequence L description binding site for residue 9JM F 300 source : AC6 8) chain F residue 64 type sequence D description binding site for residue 9JM F 300 source : AC6 9) chain F residue 65 type sequence V description binding site for residue 9JM F 300 source : AC6 10) chain F residue 94 type sequence S description binding site for residue 9JM F 300 source : AC6 11) chain F residue 95 type sequence I description binding site for residue 9JM F 300 source : AC6 12) chain F residue 96 type sequence G description binding site for residue 9JM F 300 source : AC6 13) chain F residue 122 type sequence I description binding site for residue 9JM F 300 source : AC6 14) chain F residue 147 type sequence M description binding site for residue 9JM F 300 source : AC6 15) chain F residue 148 type sequence D description binding site for residue 9JM F 300 source : AC6 16) chain F residue 149 type sequence F description binding site for residue 9JM F 300 source : AC6 17) chain F residue 165 type sequence K description binding site for residue 9JM F 300 source : AC6 18) chain F residue 191 type sequence A description binding site for residue 9JM F 300 source : AC6 19) chain F residue 192 type sequence G description binding site for residue 9JM F 300 source : AC6 20) chain F residue 193 type sequence P description binding site for residue 9JM F 300 source : AC6 21) chain F residue 194 type sequence I description binding site for residue 9JM F 300 source : AC6 22) chain F residue 196 type sequence T description binding site for residue 9JM F 300 source : AC6 23) chain F residue 266 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326 source Swiss-Prot : SWS_FT_FI5 24) chain F 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 25) chain F 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 26) chain F 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 27) chain F 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 28) chain F 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 29) chain F residue 158 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10336454 source Swiss-Prot : SWS_FT_FI2 30) chain F 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 31) chain F residue 158 type SITE sequence Y description Transition state stabilizer => ECO:0000305|PubMed:10521269 source Swiss-Prot : SWS_FT_FI4

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