eF-site ID 1lx6-AB PDB Code 1lx6 Chain A, B click to enlarge Title Crystal Structure of E. Coli Enoyl Reductase-NAD+ with a Bound Benzamide Inhibitor Classification OXIDOREDUCTASE Compound Enoyl-[acyl-carrier-protein] reductase [NADH] Source Escherichia coli (strain K12) (FABI_ECOLI) Sequence A:  GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQN DKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKV WPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISS YSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGL AKASLEANVRYMANAMGPEGVRVNAISAGPIMLAHCEAVT PIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIA AMN B:  GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQN DKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKV WPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISS YSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGL AKASLEANVRYMANAMGPEGVRVNAISAGPIMLAHCEAVT PIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIA AMN Description Functional site 1) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 2) chain A residue 19 type sequence S description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 3) chain A residue 20 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 4) chain A residue 40 type sequence Q description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 5) chain A residue 63 type sequence C description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 6) chain A residue 64 type sequence D description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 7) chain A residue 65 type sequence V description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 8) chain A residue 91 type sequence S description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 9) chain A residue 92 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 10) chain A residue 93 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 11) chain A residue 119 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 12) chain A residue 144 type sequence L description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 13) chain A residue 145 type sequence S description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 14) chain A residue 163 type sequence K description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 15) chain A residue 189 type sequence A description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 16) chain A residue 190 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 17) chain A residue 191 type sequence P description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 18) chain A residue 192 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 19) chain A residue 93 type sequence G description BINDING SITE FOR RESIDUE ZAM A 502 source : AC2 20) chain A residue 94 type sequence F description BINDING SITE FOR RESIDUE ZAM A 502 source : AC2 21) chain A residue 146 type sequence Y description BINDING SITE FOR RESIDUE ZAM A 502 source : AC2 22) chain A residue 155 type sequence N description BINDING SITE FOR RESIDUE ZAM A 502 source : AC2 23) chain A residue 156 type sequence Y description BINDING SITE FOR RESIDUE ZAM A 502 source : AC2 24) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 25) chain B residue 15 type sequence A description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 26) chain B residue 19 type sequence S description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 27) chain B residue 20 type sequence I description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 28) chain B residue 40 type sequence Q description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 29) chain B residue 63 type sequence C description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 30) chain B residue 64 type sequence D description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 31) chain B residue 65 type sequence V description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 32) chain B residue 91 type sequence S description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 33) chain B residue 92 type sequence I description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 34) chain B residue 119 type sequence I description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 35) chain B residue 145 type sequence S description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 36) chain B residue 163 type sequence K description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 37) chain B residue 189 type sequence A description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 38) chain B residue 190 type sequence G description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 39) chain B residue 191 type sequence P description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 40) chain B residue 192 type sequence I description BINDING SITE FOR RESIDUE NAD B 503 source : AC3 41) chain B residue 93 type sequence G description BINDING SITE FOR RESIDUE ZAM B 504 source : AC4 42) chain B residue 94 type sequence F description BINDING SITE FOR RESIDUE ZAM B 504 source : AC4 43) chain B residue 95 type sequence A description BINDING SITE FOR RESIDUE ZAM B 504 source : AC4 44) chain B residue 146 type sequence Y description BINDING SITE FOR RESIDUE ZAM B 504 source : AC4 45) chain B residue 155 type sequence N description BINDING SITE FOR RESIDUE ZAM B 504 source : AC4 46) chain B residue 156 type sequence Y description BINDING SITE FOR RESIDUE ZAM B 504 source : AC4 47) chain B residue 206 type sequence M description BINDING SITE FOR RESIDUE ZAM B 504 source : AC4 48) chain A residue 157 type catalytic sequence N description 606 source MCSA : MCSA1 49) chain A residue 164 type catalytic sequence A description 606 source MCSA : MCSA1 50) chain B residue 157 type catalytic sequence N description 606 source MCSA : MCSA2 51) chain B residue 164 type catalytic sequence A description 606 source MCSA : MCSA2 52) chain A residue 147 type ACT_SITE sequence L description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 157 type ACT_SITE sequence N description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 147 type ACT_SITE sequence L description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 157 type ACT_SITE sequence N description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 14 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 41 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 65 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 59) chain B residue 93 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 60) chain B residue 164 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 20 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 62) chain A residue 41 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 65 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 64) chain A residue 93 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 65) chain A residue 164 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 66) chain B residue 14 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 67) chain B residue 20 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 source Swiss-Prot : SWS_FT_FI2 68) chain A residue 96 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 69) chain B residue 96 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 70) chain A residue 206 type SITE sequence M description Involved in acyl-ACP binding source Swiss-Prot : SWS_FT_FI4 71) chain B residue 206 type SITE sequence M description Involved in acyl-ACP binding source Swiss-Prot : SWS_FT_FI4

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