eF-site ID 1qg6-D PDB Code 1qg6 Chain D 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 Escherichia coli (strain K12) (FABI_ECOLI) Sequence D:  GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQN DKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKV WPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISS YSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGL AKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIK DFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGIS GEVVHVDGGFSIAAMNE Description Functional site 1) chain D residue 13 type sequence G description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 2) chain D residue 14 type sequence V description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 3) chain D residue 15 type sequence A description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 4) chain D residue 19 type sequence S description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 5) chain D residue 20 type sequence I description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 6) chain D residue 40 type sequence Q description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 7) chain D residue 44 type sequence L description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 8) chain D residue 63 type sequence C description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 9) chain D residue 64 type sequence D description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 10) chain D residue 65 type sequence V description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 11) chain D residue 91 type sequence S description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 12) chain D residue 92 type sequence I description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 13) chain D residue 93 type sequence G description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 14) chain D residue 144 type sequence L description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 15) chain D residue 145 type sequence S description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 16) chain D residue 163 type sequence K description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 17) chain D residue 189 type sequence A description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 18) chain D residue 190 type sequence G description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 19) chain D residue 191 type sequence P description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 20) chain D residue 192 type sequence I description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 21) chain D residue 194 type sequence T description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 22) chain D residue 196 type sequence A description BINDING SITE FOR RESIDUE NAD D 504 source : AC7 23) chain D residue 93 type sequence G description BINDING SITE FOR RESIDUE TCL D 604 source : AC8 24) chain D residue 95 type sequence A description BINDING SITE FOR RESIDUE TCL D 604 source : AC8 25) chain D residue 100 type sequence L description BINDING SITE FOR RESIDUE TCL D 604 source : AC8 26) chain D residue 146 type sequence Y description BINDING SITE FOR RESIDUE TCL D 604 source : AC8 27) chain D residue 156 type sequence Y description BINDING SITE FOR RESIDUE TCL D 604 source : AC8 28) chain D residue 196 type sequence A description BINDING SITE FOR RESIDUE TCL D 604 source : AC8 29) chain D residue 200 type sequence I description BINDING SITE FOR RESIDUE TCL D 604 source : AC8 30) chain D residue 157 type catalytic sequence N description 606 source MCSA : MCSA4 31) chain D residue 164 type catalytic sequence A description 606 source MCSA : MCSA4 32) chain D residue 147 type ACT_SITE sequence L description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 157 type ACT_SITE sequence N description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 34) chain D 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 35) chain D 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 36) chain D 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 37) chain D 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 38) chain D 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 39) chain D 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 40) chain D 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 41) chain D residue 96 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 42) chain D residue 202 type SITE sequence D description Involved in acyl-ACP binding source Swiss-Prot : SWS_FT_FI4 43) chain D residue 205 type SITE sequence K description Involved in acyl-ACP binding source Swiss-Prot : SWS_FT_FI4 44) chain D residue 206 type SITE sequence M description Involved in acyl-ACP binding source Swiss-Prot : SWS_FT_FI4

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