eF-site ID 1ebd-A PDB Code 1ebd Chain A click to enlarge Title DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE Classification COMPLEX (OXIDOREDUCTASE/TRANSFERASE) Compound DIHYDROLIPOAMIDE DEHYDROGENASE Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (ODP2_BACST) Sequence A:  AIETETLVVGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGV CLNVGCIPSKALISASHRYEQAKHSEEMGIKAENVTIDFA KVQEWKASVVKKLTGGVEGLLKGNKVEIVKGEAYFVDANT VRVVNGDSAQTYTFKNAIIATGSRPIELPNFKFSNRILDS TGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILE GAGEILSGFEKQMAAIIKKRLKKKGVEVVTNALAKGAEER EDGVTVTYEANGETKTIDADYVLVTVGRRPNTDELGLEQI GIKMTNRGLIEVDQQCRTSVPNIFAIGDIVPGPALAHKAS YEGKVAAEAIAGHPSAVDYVAIPAVVFSDPECASVGYFEQ QAKDEGIDVIAAKFPFAANGRALALNDTDGFLKLVVRKED GVIIGAQIIGPNASDMIAELGLAIEAGMTAEDIALTIHAH PTLGEIAMEAAEVAL Description (1)  DIHYDROLIPOAMIDE DEHYDROGENASE, DIHYDROLIPOAMIDE ACETYLTRANSFERASE, FLAVIN-ADENINE DINUCLEOTIDE Functional site 1) chain A residue 16 type sequence G description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 2) chain A residue 18 type sequence G description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 3) chain A residue 19 type sequence P description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 4) chain A residue 20 type sequence G description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 5) chain A residue 38 type sequence V description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 6) chain A residue 39 type sequence E description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 7) chain A residue 40 type sequence K description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 8) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 9) chain A residue 46 type sequence V description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 10) chain A residue 47 type sequence C description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 11) chain A residue 50 type sequence V description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 12) chain A residue 51 type sequence G description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 13) chain A residue 52 type sequence C description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 14) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 15) chain A residue 117 type sequence G description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 16) chain A residue 118 type sequence E description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 17) chain A residue 119 type sequence A description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 18) chain A residue 146 type sequence A description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 19) chain A residue 147 type sequence T description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 20) chain A residue 148 type sequence G description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 21) chain A residue 186 type sequence Y description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 22) chain A residue 187 type sequence I description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 23) chain A residue 274 type sequence R description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 24) chain A residue 313 type sequence G description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 25) chain A residue 314 type sequence D description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 26) chain A residue 320 type sequence A description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 27) chain A residue 321 type sequence L description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 28) chain A residue 322 type sequence A description BINDING SITE FOR RESIDUE FAD A 462 source : AC1 29) chain A residue 446 type sequence H description BINDING SITE FOR RESIDUE FAD B 462 source : AC2 30) chain A residue 447 type sequence P description BINDING SITE FOR RESIDUE FAD B 462 source : AC2 31) chain A residue 44-54 type prosite sequence GGVCLNVGCIP description PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP source prosite : PS00076 32) chain A residue 446 type ACT_SITE sequence H description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 39 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8805537 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 56 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8805537 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 314 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8805537 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 322 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8805537 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 119 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 183 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 206 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 271 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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