eF-site ID 1qg6-B PDB Code 1qg6 Chain B click to enlarge Title CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN Classification OXIDOREDUCTASE Compound PROTEIN (ENOYL-[ACYL-CARRIER PROTEIN] REDUCTASE) Source null (FABI_ECOLI) Sequence B:  GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQN DKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKV WPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISS YSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGL AKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIK DFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGIS GEVVHVDGGFSIAAMNE Description Functional site 1) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 2) chain B residue 14 type sequence V description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 3) chain B residue 15 type sequence A description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 4) chain B residue 19 type sequence S description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 5) chain B residue 20 type sequence I description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 6) chain B residue 40 type sequence Q description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 7) chain B residue 44 type sequence L description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 8) chain B residue 63 type sequence C description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 9) chain B residue 64 type sequence D description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 10) chain B residue 65 type sequence V description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 11) chain B residue 91 type sequence S description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 12) chain B residue 92 type sequence I description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 13) chain B residue 93 type sequence G description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 14) chain B residue 144 type sequence L description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 15) chain B residue 145 type sequence S description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 16) chain B residue 163 type sequence K description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 17) chain B residue 189 type sequence A description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 18) chain B residue 190 type sequence G description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 19) chain B residue 191 type sequence P description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 20) chain B residue 192 type sequence I description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 21) chain B residue 194 type sequence T description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 22) chain B residue 196 type sequence A description BINDING SITE FOR RESIDUE NAD B 502 source : AC3 23) chain B residue 93 type sequence G description BINDING SITE FOR RESIDUE TCL B 602 source : AC4 24) chain B residue 95 type sequence A description BINDING SITE FOR RESIDUE TCL B 602 source : AC4 25) chain B residue 100 type sequence L description BINDING SITE FOR RESIDUE TCL B 602 source : AC4 26) chain B residue 146 type sequence Y description BINDING SITE FOR RESIDUE TCL B 602 source : AC4 27) chain B residue 156 type sequence Y description BINDING SITE FOR RESIDUE TCL B 602 source : AC4 28) chain B residue 196 type sequence A description BINDING SITE FOR RESIDUE TCL B 602 source : AC4 29) chain B residue 200 type sequence I description BINDING SITE FOR RESIDUE TCL B 602 source : AC4 30) chain B residue 147 type ACT_SITE sequence L description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 157 type ACT_SITE sequence N description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 32) 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 33) 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 34) 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 35) 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 36) chain B residue 193 type BINDING sequence R 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 37) 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 38) 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 39) chain B residue 96 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 40) chain B residue 202 type SITE sequence D description Involved in acyl-ACP binding source Swiss-Prot : SWS_FT_FI4 41) chain B residue 205 type SITE sequence K description Involved in acyl-ACP binding source Swiss-Prot : SWS_FT_FI4 42) chain B residue 206 type SITE sequence M description Involved in acyl-ACP binding source Swiss-Prot : SWS_FT_FI4 43) chain B residue 157 type catalytic sequence N description 606 source MCSA : MCSA2 44) chain B residue 164 type catalytic sequence A description 606 source MCSA : MCSA2

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