eF-site ID 1vdc-A PDB Code 1vdc Chain A click to enlarge Title STRUCTURE OF NADPH DEPENDENT THIOREDOXIN REDUCTASE Classification OXIDOREDUCTASE Compound NADPH DEPENDENT THIOREDOXIN REDUCTASE Source null (TRXB1_ARATH) Sequence A:  LETHNTRLCIVGSGPAAHTAAIYAARAELKPLLFEGWMAN DIAPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERF GTTIFTETVTKVDFSSKPFKLFTDSKAILADAVILAIGAV AKRLSFVGSGEVLGGFWNRGISACAVCDGAAPIFRNKPLA VIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQR ALSNPKIDVIWNSSVVEAYGDGERDVLGGLKVKNVVTGDV SDLKVSGLFFAIGHEPATKFLDGGVELDSDGYVVTKPGTT QTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALDAEHYLQ EI Description Functional site 1) chain A residue 135 type sequence C description ACTIVE SITE. source : ACT 2) chain A residue 138 type sequence C description ACTIVE SITE. source : ACT 3) chain A residue 136 type sequence A description ACTIVE SITE. source : ACT 4) chain A residue 139 type sequence D description ACTIVE SITE. source : ACT 5) chain A residue 140 type sequence G description ACTIVE SITE. source : ACT 6) chain A residue 159 type sequence E description ACTIVE SITE. source : ACT 7) chain A residue 12 type sequence G description FAD BINDING SITE. source : FAD 8) chain A residue 13 type sequence S description FAD BINDING SITE. source : FAD 9) chain A residue 14 type sequence G description FAD BINDING SITE. source : FAD 10) chain A residue 15 type sequence P description FAD BINDING SITE. source : FAD 11) chain A residue 16 type sequence A description FAD BINDING SITE. source : FAD 12) chain A residue 36 type sequence G description FAD BINDING SITE. source : FAD 13) chain A residue 41 type sequence G description FAD BINDING SITE. source : FAD 14) chain A residue 46 type sequence T description FAD BINDING SITE. source : FAD 15) chain A residue 50 type sequence E description FAD BINDING SITE. source : FAD 16) chain A residue 51 type sequence N description FAD BINDING SITE. source : FAD 17) chain A residue 61 type sequence G description FAD BINDING SITE. source : FAD 18) chain A residue 113 type sequence G description FAD BINDING SITE. source : FAD 19) chain A residue 133 type sequence S description FAD BINDING SITE. source : FAD 20) chain A residue 139 type sequence D description FAD BINDING SITE. source : FAD 21) chain A residue 285 type sequence G description FAD BINDING SITE. source : FAD 22) chain A residue 286 type sequence D description FAD BINDING SITE. source : FAD 23) chain A residue 56 type sequence P description BINDING SITE FOR RESIDUE SO4 A 440 source : AC1 24) chain A residue 57 type sequence E description BINDING SITE FOR RESIDUE SO4 A 440 source : AC1 25) chain A residue 67 type sequence K description BINDING SITE FOR RESIDUE SO4 A 440 source : AC1 26) chain A residue 70 type sequence K description BINDING SITE FOR RESIDUE SO4 A 440 source : AC1 27) chain A residue 11 type sequence V description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 28) chain A residue 12 type sequence G description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 29) chain A residue 13 type sequence S description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 30) chain A residue 14 type sequence G description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 31) chain A residue 15 type sequence P description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 32) chain A residue 16 type sequence A description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 33) chain A residue 34 type sequence F description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 34) chain A residue 35 type sequence E description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 35) chain A residue 36 type sequence G description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 36) chain A residue 37 type sequence I description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 37) chain A residue 38 type sequence A description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 38) chain A residue 41 type sequence G description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 39) chain A residue 42 type sequence Q description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 40) chain A residue 43 type sequence L description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 41) chain A residue 49 type sequence V description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 42) chain A residue 51 type sequence N description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 43) chain A residue 84 type sequence V description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 44) chain A residue 111 type sequence A description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 45) chain A residue 112 type sequence I description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 46) chain A residue 113 type sequence G description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 47) chain A residue 138 type sequence C description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 48) chain A residue 285 type sequence G description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 49) chain A residue 286 type sequence D description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 50) chain A residue 293 type sequence R description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 51) chain A residue 294 type sequence Q description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 52) chain A residue 295 type sequence A description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 53) chain A residue 298 type sequence A description BINDING SITE FOR RESIDUE FAD A 400 source : AC2 54) chain A residue 50 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9000629 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 71 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:9000629 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 79 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9000629 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 93 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9000629 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 126 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9000629 source Swiss-Prot : SWS_FT_FI1 59) chain A residue 178 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9000629 source Swiss-Prot : SWS_FT_FI1 60) chain A residue 135-155 type prosite sequence CAVCDGAAPIFRNKPLAVIGGGD description PYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CavCDGaapiFrnkpLaVIGGGD source prosite : PS00573

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