eF-site ID 2gmh-A PDB Code 2gmh Chain A 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 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 A residue 566 type catalytic sequence Q description 281 source MCSA : MCSA1 5) chain A residue 92 type catalytic sequence E description 281 source MCSA : MCSA1 6) chain A residue 341 type catalytic sequence I description 281 source MCSA : MCSA1 7) chain A residue 377 type catalytic sequence A description 281 source MCSA : MCSA1 8) chain A residue 538 type catalytic sequence L description 281 source MCSA : MCSA1 9) chain A residue 563 type catalytic sequence D description 281 source MCSA : MCSA1 10) chain A residue 569 type catalytic sequence N description 281 source MCSA : MCSA1 11) chain A residue 86-107 type INTRAMEM sequence LDPRAFEELFPDWKEKGAPLNT description source Swiss-Prot : SWS_FT_FI1 12) chain A residue 405-424 type INTRAMEM sequence NLKNSWVWKELYSVRNIRPS description source Swiss-Prot : SWS_FT_FI1 13) chain A residue 538 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 14) chain A residue 563 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 15) chain A residue 566 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 16) chain A residue 569 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 17) chain A residue 200 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 334 type MOD_RES sequence N description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 73 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 20) chain A residue 109 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:Q921G7 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 528 type MOD_RES sequence C description Phosphoserine => ECO:0000250|UniProtKB:Q16134 source Swiss-Prot : SWS_FT_FI5

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