eF-site ID 1lsj-AB PDB Code 1lsj Chain A, B click to enlarge Title Crystal Structure of the E110Q Mutant of L-3-Hydroxyacyl-CoA Dehydrogenase in Complex with NAD Classification OXIDOREDUCTASE Compound 3-HYDROXYACYL-COA DEHYDROGENASE Source null (HCDH_HUMAN) Sequence A:  KIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSTIATS TDAASVVHSTDLVVEAIVQNLKVKNELFKRLDKFAAEHTI FASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEV IKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLL VPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLD YVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFG KKTGEGFYKYK B:  KIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSTIATS TDAASVVHSTDLVVEAIVQNLKVKNELFKRLDKFAAEHTI FASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEV IKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLL VPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLD YVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFG KKTGEGFYKYK Description Functional site 1) chain A residue 24 type sequence G description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 2) chain A residue 25 type sequence L description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 3) chain A residue 26 type sequence M description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 4) chain A residue 45 type sequence D description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 5) chain A residue 46 type sequence Q description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 6) chain A residue 107 type sequence A description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 7) chain A residue 108 type sequence I description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 8) chain A residue 110 type sequence Q description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 9) chain A residue 135 type sequence N description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 10) chain A residue 137 type sequence S description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 11) chain A residue 161 type sequence N description BINDING SITE FOR RESIDUE NAD A 350 source : AC1 12) chain B residue 24 type sequence G description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 13) chain B residue 25 type sequence L description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 14) chain B residue 26 type sequence M description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 15) chain B residue 45 type sequence D description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 16) chain B residue 46 type sequence Q description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 17) chain B residue 107 type sequence A description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 18) chain B residue 108 type sequence I description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 19) chain B residue 109 type sequence V description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 20) chain B residue 110 type sequence Q description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 21) chain B residue 115 type sequence K description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 22) chain B residue 135 type sequence N description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 23) chain B residue 137 type sequence S description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 24) chain A residue 143 type catalytic sequence S description 336 source MCSA : MCSA1 25) chain A residue 164 type catalytic sequence P description 336 source MCSA : MCSA1 26) chain A residue 176 type catalytic sequence M description 336 source MCSA : MCSA1 27) chain A residue 214 type catalytic sequence Y description 336 source MCSA : MCSA1 28) chain B residue 143 type catalytic sequence S description 336 source MCSA : MCSA2 29) chain B residue 164 type catalytic sequence P description 336 source MCSA : MCSA2 30) chain B residue 176 type catalytic sequence M description 336 source MCSA : MCSA2 31) chain B residue 214 type catalytic sequence Y description 336 source MCSA : MCSA2 32) chain A residue 28 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 51 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 116 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 121 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 143 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 167 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 299 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 116 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 121 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 143 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 167 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 299 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 28 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 51 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 67 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 74 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 67 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 74 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 164 type SITE sequence P description Important for catalytic activity => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 164 type SITE sequence P description Important for catalytic activity => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 74 type MOD_RES sequence P description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 54) chain B residue 74 type MOD_RES sequence P description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 55) chain B residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 75 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 57) chain A residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 59) chain B residue 130 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 60) chain B residue 179 type MOD_RES sequence Q description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 186 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 62) chain B residue 196 type MOD_RES sequence P description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 63) chain B residue 206 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 64) chain B residue 235 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 65) chain A residue 186 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 66) chain A residue 196 type MOD_RES sequence P description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 67) chain A residue 206 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 68) chain A residue 235 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 69) chain B residue 75 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 70) chain A residue 130 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 71) chain A residue 179 type MOD_RES sequence Q description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 72) chain A residue 119 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 73) chain A residue 173 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 74) chain B residue 119 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 75) chain B residue 173 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 76) chain A residue 121 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 77) chain B residue 121 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 78) chain A residue 201-225 type prosite sequence DTPGFIVNRLLVPYLMEAIRLYERG description 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DtpGFIvNRllvPYLmeair.LYerG source prosite : PS00067

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