eF-site ID 2gmh-B PDB Code 2gmh Chain 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 B:  PRITTHYTIYPRDQDKRWEGVNMERFAEEADVVIVGAGPA GLSAATRLKQLAAQHEKDLRVCLVEKAAHIGAHTLSGACL DPRAFEELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVP ILPGLPMNNHGNYVVRLGHLVSWMGEQAEALGVEVYPGYA AAEILFHEDGSVKGIATNDVGIQKDGAPKTTFERGLELHA KVTIFAEGCHGHLAKQLYKKFDLRANCEPQTYGIGLKELW VIDEKKWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLL ALGFVVGLDYQNPYLSPFREFQRWKHHPSIKPTLEGGKRI AYGARALNEGGFQSIPKLTFPGGLLIGCSPGFMNVPKIKG THTAMKSGTLAAESIFNQLTSENLQSKTIGLHVTEYEDNL KNSWVWKELYSVRNIRPSCHGILGVYGGMIYTGIFYWIFR GMEPWTLKHKGSDSDQLKPAKDCTPIEYPKPDGQISFDLL SSVALSGTNHEHDQPAHLTLKDDSVPVNRNLSIYDGPEQR FCPAGVYEFVPLEQGDGFRLQINAQNCVHCKTCDIKDPSQ NINWVVPEGGGGPAYNGM Description Functional site 1) chain B residue 92 type catalytic sequence E description 281 source MCSA : MCSA2 2) chain B residue 341 type catalytic sequence I description 281 source MCSA : MCSA2 3) chain B residue 377 type catalytic sequence A description 281 source MCSA : MCSA2 4) chain B residue 538 type catalytic sequence L description 281 source MCSA : MCSA2 5) chain B residue 563 type catalytic sequence D description 281 source MCSA : MCSA2 6) chain B residue 566 type catalytic sequence Q description 281 source MCSA : MCSA2 7) chain B residue 569 type catalytic sequence N description 281 source MCSA : MCSA2 8) chain B residue 52 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 282 type BINDING sequence G description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 10) chain B residue 283 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17050691 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 538 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 12) chain B residue 563 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 13) chain B residue 566 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 14) chain B residue 569 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 15) chain B residue 73 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 16) chain B residue 109 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 17) chain B residue 200 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 18) chain B residue 334 type MOD_RES sequence N description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 19) chain B residue 528 type MOD_RES sequence C description Phosphoserine => ECO:0000250|UniProtKB:Q16134 source Swiss-Prot : SWS_FT_FI5 20) chain B residue 86-107 type INTRAMEM sequence LDPRAFEELFPDWKEKGAPLNT description source Swiss-Prot : SWS_FT_FI1 21) chain B residue 405-424 type INTRAMEM sequence NLKNSWVWKELYSVRNIRPS description source Swiss-Prot : SWS_FT_FI1

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