eF-site ID 2gmh-AB PDB Code 2gmh Chain A, B click to enlarge Title Structure of Porcine Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase in Complexed with Ubiquinone 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 52 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 2) chain A residue 282 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 3) chain A residue 283 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 4) chain B residue 52 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 5) chain B residue 282 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 283 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 566 type catalytic sequence Q description 281 source MCSA : MCSA1 8) chain A residue 92 type catalytic sequence E description 281 source MCSA : MCSA1 9) chain A residue 341 type catalytic sequence I description 281 source MCSA : MCSA1 10) chain A residue 377 type catalytic sequence A description 281 source MCSA : MCSA1 11) chain A residue 538 type catalytic sequence L description 281 source MCSA : MCSA1 12) chain A residue 563 type catalytic sequence D description 281 source MCSA : MCSA1 13) chain A residue 569 type catalytic sequence N description 281 source MCSA : MCSA1 14) chain B residue 566 type catalytic sequence Q description 281 source MCSA : MCSA2 15) chain B residue 92 type catalytic sequence E description 281 source MCSA : MCSA2 16) chain B residue 341 type catalytic sequence I description 281 source MCSA : MCSA2 17) chain B residue 377 type catalytic sequence A description 281 source MCSA : MCSA2 18) chain B residue 538 type catalytic sequence L description 281 source MCSA : MCSA2 19) chain B residue 563 type catalytic sequence D description 281 source MCSA : MCSA2 20) chain B residue 569 type catalytic sequence N description 281 source MCSA : MCSA2 21) chain A residue 86-107 type INTRAMEM sequence LDPRAFEELFPDWKEKGAPLNT description source Swiss-Prot : SWS_FT_FI1 22) chain A residue 405-424 type INTRAMEM sequence NLKNSWVWKELYSVRNIRPS description source Swiss-Prot : SWS_FT_FI1 23) chain B residue 86-107 type INTRAMEM sequence LDPRAFEELFPDWKEKGAPLNT description source Swiss-Prot : SWS_FT_FI1 24) chain B residue 405-424 type INTRAMEM sequence NLKNSWVWKELYSVRNIRPS description source Swiss-Prot : SWS_FT_FI1 25) chain A residue 538 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 26) chain A residue 563 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 27) chain A residue 566 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 28) chain A residue 569 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 29) chain B residue 538 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 30) chain B residue 563 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 31) chain B residue 566 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 32) chain B residue 569 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 33) chain A residue 200 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 334 type MOD_RES sequence N description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 73 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 109 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 200 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 334 type MOD_RES sequence N description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 39) chain A residue 73 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 40) chain A residue 109 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 528 type MOD_RES sequence C description Phosphoserine => ECO:0000250|UniProtKB:Q16134 source Swiss-Prot : SWS_FT_FI5 42) chain B residue 528 type MOD_RES sequence C description Phosphoserine => ECO:0000250|UniProtKB:Q16134 source Swiss-Prot : SWS_FT_FI5

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