eF-site ID 3hdh-A PDB Code 3hdh Chain A click to enlarge Title PIG HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE REVISITED: SEQUENCE ANALYSIS AND CRYSTAL STRUCTURE DETERMINATION Classification OXIDOREDUCTASE Compound PROTEIN (L-3-HYDROXYACYL COA DEHYDROGENASE) Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  KILVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSSISTS TDAASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTI FASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEV VKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLL VPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLD YVGLDTTKFIIDGWHEMDSQNPLFQPSPAMNKLVAENKFG KKTGEGFYKYK Description Functional site 1) chain A residue 25 type sequence L description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 2) chain A residue 26 type sequence M description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 3) chain A residue 45 type sequence D description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 4) chain A residue 46 type sequence Q description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 5) chain A residue 107 type sequence A description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 6) chain A residue 108 type sequence I description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 7) chain A residue 109 type sequence V description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 8) chain A residue 110 type sequence E description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 9) chain A residue 114 type sequence V description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 10) chain A residue 115 type sequence K description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 11) chain A residue 135 type sequence N description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 12) chain A residue 137 type sequence S description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 13) chain A residue 158 type sequence H description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 14) chain A residue 159 type sequence F description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 15) chain A residue 34 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 57 type BINDING sequence G description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 122 type BINDING sequence L description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 127 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 149 type BINDING sequence T description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 73 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 80 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 173 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 201-225 type prosite sequence DTPGFIVNRLLVPYLIEAVRLYERG description 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DtpGFIvNRllvPYLieavr.LYerG source prosite : PS00067 24) chain A residue 170 type SITE sequence E description Important for catalytic activity => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 80 type MOD_RES sequence F description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 206 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 87 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 136 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 185 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 192 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 202 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 212 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 241 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 125 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 36) chain A residue 179 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 37) chain A residue 127 type MOD_RES sequence A description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI7

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