eF-site ID 1cwu-A PDB Code 1cwu Chain A click to enlarge Title BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE Classification OXIDOREDUCTASE Compound ENOYL ACP REDUCTASE Source Brassica napus (Rape) (FABI_BRANA) Sequence A:  LPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGT WVPALNIFETSLRRGKFDQSRVLPDGSLMEIKKVYPLDAV FDNPEDVPEDVKANKRYAGSSNWTVQEAAECVRQDFGSID ILVHSLGNGPEVSKPLLETSRKGYLAAISASSYSFVSLLS HFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALES DTRVLAFEAGRKQNIRVNTISAGPLGSRAAKAIGFIDTMI EYSYNNAPIQKTLTADEVGNAAAFLVSPLASAITGATIYV DNGLNSMGVALDSPVF Description Functional site 1) chain A residue 25 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 2) chain A residue 26 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 3) chain A residue 31 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 4) chain A residue 32 type sequence Y description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 5) chain A residue 52 type sequence W description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 6) chain A residue 89 type sequence D description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 7) chain A residue 90 type sequence A description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 8) chain A residue 91 type sequence V description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 9) chain A residue 136 type sequence S description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 10) chain A residue 137 type sequence L description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 11) chain A residue 138 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 12) chain A residue 186 type sequence L description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 13) chain A residue 187 type sequence T description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 14) chain A residue 206 type sequence K description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 15) chain A residue 233 type sequence A description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 16) chain A residue 234 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 17) chain A residue 235 type sequence P description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 18) chain A residue 236 type sequence L description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 19) chain A residue 238 type sequence S description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 20) chain A residue 240 type sequence A description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 21) chain A residue 241 type sequence A description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 22) chain A residue 247 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC1 23) chain A residue 138 type sequence G description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 24) chain A residue 139 type sequence N description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 25) chain A residue 140 type sequence G description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 26) chain A residue 188 type sequence Y description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 27) chain A residue 198 type sequence Y description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 28) chain A residue 202 type sequence M description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 29) chain A residue 206 type sequence K description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 30) chain A residue 240 type sequence A description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 31) chain A residue 241 type sequence A description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 32) chain A residue 244 type sequence I description BINDING SITE FOR RESIDUE TDB A 502 source : AC2 33) chain A residue 188 type ACT_SITE sequence Y description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 198 type ACT_SITE sequence Y description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 25 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 32 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 136 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 186 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 236 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786 source Swiss-Prot : SWS_FT_FI2

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