eF-site ID 3hdh-ABC PDB Code 3hdh Chain A, B, 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 A:  KILVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSSISTS TDAASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTI FASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEV VKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLL VPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLD YVGLDTTKFIIDGWHEMDSQNPLFQPSPAMNKLVAENKFG KKTGEGFYKYK B:  KILVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSSISTS TDAASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTI FASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEV VKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLL VPYLIEAVRLYERGDASKEDIDTAMKLGAGYPMGPFELLD YVGLDTTKFIIDGWHEMDSQNPLFQPSPAMNKLVAENKFG KKTGEGFYKYK C:  KILVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSSISTS TDAASVVHSTDLVVEAIVENLKVKSELFKRLDKFAAEHTI FASNTSSLQITSLANATTRQDRFAGLHFFNPVPLMKLVEV VKTPMTSQKTLESLVDFSKTLGKHPVSCKDTPGFIVNRLL VPYLIEAVRLYEKEDIDTAMKLGAGPFELLDYVGLDTTKF IIDGWHESPAMNKLVAENKFGKKTG 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 B residue 24 type sequence G description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 16) chain B residue 25 type sequence L description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 17) chain B residue 26 type sequence M description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 18) chain B residue 45 type sequence D description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 19) chain B residue 46 type sequence Q description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 20) chain B residue 107 type sequence A description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 21) chain B residue 108 type sequence I description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 22) chain B residue 110 type sequence E description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 23) chain B residue 115 type sequence K description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 24) chain B residue 135 type sequence N description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 25) chain B residue 137 type sequence S description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 26) chain B residue 159 type sequence F description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 27) chain C residue 22 type sequence G description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 28) chain C residue 25 type sequence L description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 29) chain C residue 26 type sequence M description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 30) chain C residue 45 type sequence D description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 31) chain C residue 46 type sequence Q description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 32) chain C residue 107 type sequence A description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 33) chain C residue 108 type sequence I description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 34) chain C residue 110 type sequence E description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 35) chain C residue 115 type sequence K description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 36) chain C residue 118 type sequence L description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 37) chain C residue 135 type sequence N description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 38) chain C residue 136 type sequence T description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 39) chain C residue 137 type sequence S description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 40) chain C residue 158 type sequence H description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 41) chain C residue 159 type sequence F description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 42) chain C residue 161 type sequence N description BINDING SITE FOR RESIDUE NAD C 1150 source : AC3 43) chain A residue 34 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 57 type BINDING sequence G description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 122 type BINDING sequence L description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 149 type BINDING sequence T description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 47) chain C residue 34 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 48) chain C residue 57 type BINDING sequence G description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 49) chain C residue 122 type BINDING sequence L description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 50) chain C residue 127 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 51) chain C residue 149 type BINDING sequence T description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 127 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 149 type BINDING sequence T description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 34 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 57 type BINDING sequence G description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 122 type BINDING sequence L description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 57) chain B residue 127 type BINDING sequence A description BINDING => ECO:0000269|PubMed:3479790 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 73 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 80 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 173 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 61) chain B residue 73 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 80 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 63) chain B residue 173 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 64) chain C residue 73 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 65) chain C residue 80 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 66) chain C residue 173 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 170 type SITE sequence E description Important for catalytic activity => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI3 68) chain C residue 170 type SITE sequence E description Important for catalytic activity => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI3 69) chain B residue 170 type SITE sequence E description Important for catalytic activity => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI3 70) chain A residue 80 type MOD_RES sequence F description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 71) chain A residue 206 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 72) chain B residue 80 type MOD_RES sequence F description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 73) chain B residue 206 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 74) chain C residue 80 type MOD_RES sequence F description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 75) chain C residue 206 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 76) chain A residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 77) chain A residue 87 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 78) chain A residue 136 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 79) chain B residue 87 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 80) chain B residue 136 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 81) chain B residue 185 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 82) chain B residue 192 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 83) chain B residue 202 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 84) chain B residue 212 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 85) chain B residue 241 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 86) chain C residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 87) chain C residue 87 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 88) chain C residue 136 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 89) chain C residue 185 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 90) chain C residue 192 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 91) chain C residue 202 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 92) chain C residue 212 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 93) chain A residue 185 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 94) chain A residue 192 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 95) chain A residue 202 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 96) chain A residue 212 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 97) chain A residue 241 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 98) chain B residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 99) chain A residue 125 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 100) chain A residue 179 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 101) chain B residue 125 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 102) chain B residue 179 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 103) chain C residue 125 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 104) chain C residue 179 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 105) chain A residue 127 type MOD_RES sequence A description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI7 106) chain B residue 127 type MOD_RES sequence A description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI7 107) chain C residue 127 type MOD_RES sequence A description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:Q16836 source Swiss-Prot : SWS_FT_FI7 108) chain A residue 201-225 type prosite sequence DTPGFIVNRLLVPYLIEAVRLYERG description 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DtpGFIvNRllvPYLieavr.LYerG source prosite : PS00067

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