eF-site ID 3hdh-C PDB Code 3hdh Chain C 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 C:  KILVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSSISTS TDAASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTI FASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEV VKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLL VPYLIEAVRLYEKEDIDTAMKLGAGPFELLDYVGLDTTKF IIDGWHESPAMNKLVAENKFGKKTG Description Functional site 1) chain C residue 22 type sequence G description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 2) chain C residue 25 type sequence L description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 3) chain C residue 26 type sequence M description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 4) chain C residue 45 type sequence D description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 5) chain C residue 46 type sequence Q description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 6) chain C residue 107 type sequence A description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 7) chain C residue 108 type sequence I description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 8) chain C residue 110 type sequence E description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 9) chain C residue 115 type sequence K description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 10) chain C residue 118 type sequence L description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 11) chain C residue 135 type sequence N description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 12) chain C residue 136 type sequence T description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 13) chain C residue 137 type sequence S description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 14) chain C residue 158 type sequence H description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 15) chain C residue 159 type sequence F description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 16) chain C residue 161 type sequence N description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 17) chain C residue 34 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 57 type BINDING sequence G description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 122 type BINDING sequence L description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 127 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 149 type BINDING sequence T description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 73 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 80 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 173 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 170 type SITE sequence E description Important for catalytic activity => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI3 26) chain C residue 80 type MOD_RES sequence F description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 27) chain C residue 206 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 28) chain C residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 29) chain C residue 87 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 30) chain C residue 136 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 31) chain C residue 185 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 32) chain C residue 192 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 33) chain C residue 202 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 34) chain C residue 212 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 35) chain C residue 125 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 36) chain C residue 179 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 37) chain C 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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