eF-site ID 3hdh-B PDB Code 3hdh Chain B 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 B:  KILVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSSISTS TDAASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTI FASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEV VKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLL VPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLD YVGLDTTKFIIDGWHEMDSQNPLFQPSPAMNKLVAENKFG KKTGEGFYKYK Description Functional site 1) chain B residue 24 type sequence G description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 2) chain B residue 25 type sequence L description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 3) chain B residue 26 type sequence M description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 4) chain B residue 45 type sequence D description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 5) chain B residue 46 type sequence Q description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 6) chain B residue 107 type sequence A description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 7) chain B residue 108 type sequence I description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 8) chain B residue 110 type sequence E description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 9) chain B residue 115 type sequence K description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 10) chain B residue 135 type sequence N description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 11) chain B residue 137 type sequence S description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 12) chain B residue 159 type sequence F description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 13) chain B residue 149 type BINDING sequence T description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 34 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 57 type BINDING sequence G description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 122 type BINDING sequence L description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 127 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 73 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 80 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 173 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 170 type SITE sequence E description Important for catalytic activity => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 80 type MOD_RES sequence F description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 206 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 87 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 25) chain B residue 136 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 185 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 192 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 28) chain B residue 202 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 29) chain B residue 212 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 30) chain B residue 241 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 31) chain B residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 125 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 33) chain B residue 179 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 34) chain B 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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