eF-site ID 2gmj-AB PDB Code 2gmj Chain A, B click to enlarge Title Structure of Porcine Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase Classification OXIDOREDUCTASE Compound Electron transfer flavoprotein-ubiquinone oxidoreductase Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  CKVPRITTHYTIYPRDQDKRWEGVNMERFAEEADVVIVGA GPAGLSAATRLKQLAAQHEKDLRVCLVEKAAHIGAHTLSG ACLDPRAFEELFPDWKEKGAPLNTPVTEDRFGILTEKYRI PVPILPGLPMNNHGNYVVRLGHLVSWMGEQAEALGVEVYP GYAAAEILFHEDGSVKGIATNDVGIQKDGAPKTTFERGLE LHAKVTIFAEGCHGHLAKQLYKKFDLRANCEPQTYGIGLK ELWVIDEKKWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGE PLLALGFVVGLDYQNPYLSPFREFQRWKHHPSIKPTLEGG KRIAYGARALNEGGFQSIPKLTFPGGLLIGCSPGFMNVPK IKGTHTAMKSGTLAAESIFNQLTSENLQSKTIGLHVTEYE DNLKNSWVWKELYSVRNIRPSCHGILGVYGGMIYTGIFYW IFRGMEPWTLKHKGSDSDQLKPAKDCTPIEYPKPDGQISF DLLSSVALSGTNHEHDQPAHLTLKDDSVPVNRNLSIYDGP EQRFCPAGVYEFVPLEQGDGFRLQINAQNCVHCKTCDIKD PSQNINWVVPEGGGGPAYNGM B:  PRITTHYTIYPRDQDKRWEGVNMERFAEEADVVIVGAGPA GLSAATRLKQLAAQHEKDLRVCLVEKAAHIGAHTLSGACL DPRAFEELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVP ILPGLPMNNHGNYVVRLGHLVSWMGEQAEALGVEVYPGYA AAEILFHEDGSVKGIATNDVGIQKDGAPKTTFERGLELHA KVTIFAEGCHGHLAKQLYKKFDLRANCEPQTYGIGLKELW VIDEKKWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLL ALGFVVGLDYQNPYLSPFREFQRWKHHPSIKPTLEGGKRI AYGARALNEGGFQSIPKLTFPGGLLIGCSPGFMNVPKIKG THTAMKSGTLAAESIFNQLTSENLQSKTIGLHVTEYEDNL KNSWVWKELYSVRNIRPSCHGILGVYGGMIYTGIFYWIFR GMEPWTLKHKGSDSDQLKPAKDCTPIEYPKPDGQISFDLL SSVALSGTNHEHDQPAHLTLKDDSVPVNRNLSIYDGPEQR FCPAGVYEFVPLEQGDGFRLQINAQNCVHCKTCDIKDPSQ NINWVVPEGGGGPAYNGM Description Functional site 1) chain A residue 504 type sequence L description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 2) chain A residue 528 type sequence C description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 3) chain A residue 529 type sequence P description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 4) chain A residue 553 type sequence C description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 5) chain A residue 554 type sequence V description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 6) chain A residue 556 type sequence C description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 7) chain A residue 557 type sequence K description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 8) chain A residue 559 type sequence C description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 9) chain A residue 570 type sequence W description BINDING SITE FOR RESIDUE SF4 A 610 source : AC1 10) chain A residue 42 type sequence G description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 11) chain A residue 44 type sequence G description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 12) chain A residue 45 type sequence P description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 13) chain A residue 46 type sequence A description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 14) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 15) chain A residue 72 type sequence K description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 16) chain A residue 79 type sequence H description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 17) chain A residue 82 type sequence S description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 18) chain A residue 83 type sequence G description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 19) chain A residue 84 type sequence A description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 20) chain A residue 85 type sequence C description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 21) chain A residue 167 type sequence A description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 22) chain A residue 212 type sequence A description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 23) chain A residue 213 type sequence E description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 24) chain A residue 214 type sequence G description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 25) chain A residue 218 type sequence H description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 26) chain A residue 275 type sequence F description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 27) chain A residue 333 type sequence L description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 28) chain A residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 29) chain A residue 354 type sequence C description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 30) chain A residue 364 type sequence I description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 31) chain A residue 365 type sequence K description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 32) chain A residue 366 type sequence G description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 33) chain A residue 367 type sequence T description BINDING SITE FOR RESIDUE FAD A 611 source : AC2 34) chain B residue 504 type sequence L description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 35) chain B residue 528 type sequence C description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 36) chain B residue 529 type sequence P description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 37) chain B residue 532 type sequence V description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 38) chain B residue 553 type sequence C description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 39) chain B residue 554 type sequence V description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 40) chain B residue 556 type sequence C description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 41) chain B residue 557 type sequence K description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 42) chain B residue 559 type sequence C description BINDING SITE FOR RESIDUE SF4 B 612 source : AC3 43) chain B residue 42 type sequence G description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 44) chain B residue 44 type sequence G description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 45) chain B residue 45 type sequence P description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 46) chain B residue 46 type sequence A description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 47) chain B residue 71 type sequence E description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 48) chain B residue 72 type sequence K description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 49) chain B residue 79 type sequence H description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 50) chain B residue 82 type sequence S description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 51) chain B residue 83 type sequence G description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 52) chain B residue 84 type sequence A description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 53) chain B residue 85 type sequence C description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 54) chain B residue 167 type sequence A description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 55) chain B residue 213 type sequence E description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 56) chain B residue 214 type sequence G description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 57) chain B residue 218 type sequence H description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 58) chain B residue 275 type sequence F description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 59) chain B residue 277 type sequence Y description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 60) chain B residue 331 type sequence R description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 61) chain B residue 333 type sequence L description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 62) chain B residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 63) chain B residue 354 type sequence C description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 64) chain B residue 364 type sequence I description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 65) chain B residue 365 type sequence K description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 66) chain B residue 366 type sequence G description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 67) chain B residue 367 type sequence T description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 68) chain B residue 572 type sequence V description BINDING SITE FOR RESIDUE FAD B 613 source : AC4 69) chain A residue 364 type sequence I description BINDING SITE FOR RESIDUE TBU A 621 source : AC5 70) chain A residue 271 type sequence Y description BINDING SITE FOR RESIDUE TBU A 622 source : AC6 71) chain A residue 438 type sequence T description BINDING SITE FOR RESIDUE TBU A 622 source : AC6 72) chain A residue 131 type sequence L description BINDING SITE FOR RESIDUE TBU A 623 source : AC7 73) chain A residue 324 type sequence K description BINDING SITE FOR RESIDUE TBU A 624 source : AC8 74) chain A residue 491 type sequence L description BINDING SITE FOR RESIDUE TBU A 624 source : AC8 75) chain B residue 273 type sequence G description BINDING SITE FOR RESIDUE TBU B 626 source : BC1 76) chain A residue 92 type catalytic sequence E description 281 source MCSA : MCSA1 77) chain A residue 341 type catalytic sequence I description 281 source MCSA : MCSA1 78) chain A residue 377 type catalytic sequence A description 281 source MCSA : MCSA1 79) chain A residue 538 type catalytic sequence L description 281 source MCSA : MCSA1 80) chain A residue 563 type catalytic sequence D description 281 source MCSA : MCSA1 81) chain A residue 566 type catalytic sequence Q description 281 source MCSA : MCSA1 82) chain A residue 569 type catalytic sequence N description 281 source MCSA : MCSA1 83) chain B residue 92 type catalytic sequence E description 281 source MCSA : MCSA2 84) chain B residue 341 type catalytic sequence I description 281 source MCSA : MCSA2 85) chain B residue 377 type catalytic sequence A description 281 source MCSA : MCSA2 86) chain B residue 538 type catalytic sequence L description 281 source MCSA : MCSA2 87) chain B residue 563 type catalytic sequence D description 281 source MCSA : MCSA2 88) chain B residue 566 type catalytic sequence Q description 281 source MCSA : MCSA2 89) chain B residue 569 type catalytic sequence N description 281 source MCSA : MCSA2 90) chain A residue 52 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 91) chain A residue 282 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 92) chain A residue 283 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 93) chain B residue 52 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 94) chain B residue 282 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 95) chain B residue 283 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 96) chain A residue 538 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 97) chain A residue 563 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 98) chain A residue 566 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 99) chain A residue 569 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 100) chain B residue 538 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 101) chain B residue 563 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 102) chain B residue 566 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 103) chain B residue 569 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 104) chain A residue 73 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 105) chain A residue 109 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 106) chain A residue 200 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 107) chain A residue 334 type MOD_RES sequence N description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 108) chain B residue 73 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 109) chain B residue 109 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 110) chain B residue 200 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 111) chain B residue 334 type MOD_RES sequence N description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 112) chain A residue 528 type MOD_RES sequence C description Phosphoserine => ECO:0000250|UniProtKB:Q16134 source Swiss-Prot : SWS_FT_FI5 113) chain B residue 528 type MOD_RES sequence C description Phosphoserine => ECO:0000250|UniProtKB:Q16134 source Swiss-Prot : SWS_FT_FI5 114) chain A residue 86-107 type INTRAMEM sequence LDPRAFEELFPDWKEKGAPLNT description source Swiss-Prot : SWS_FT_FI1 115) chain A residue 405-424 type INTRAMEM sequence NLKNSWVWKELYSVRNIRPS description source Swiss-Prot : SWS_FT_FI1 116) chain B residue 86-107 type INTRAMEM sequence LDPRAFEELFPDWKEKGAPLNT description source Swiss-Prot : SWS_FT_FI1 117) chain B residue 405-424 type INTRAMEM sequence NLKNSWVWKELYSVRNIRPS description source Swiss-Prot : SWS_FT_FI1

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