eF-site ID 1lsj-A PDB Code 1lsj Chain A 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 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 A residue 143 type catalytic sequence S description 336 source MCSA : MCSA1 13) chain A residue 164 type catalytic sequence P description 336 source MCSA : MCSA1 14) chain A residue 176 type catalytic sequence M description 336 source MCSA : MCSA1 15) chain A residue 214 type catalytic sequence Y description 336 source MCSA : MCSA1 16) chain A residue 28 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 51 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 116 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 121 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 143 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 167 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 299 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 67 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 74 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 164 type SITE sequence P description Important for catalytic activity => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 74 type MOD_RES sequence P description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 75 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 186 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 196 type MOD_RES sequence P description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 206 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 235 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 130 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 179 type MOD_RES sequence Q description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 119 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 37) chain A residue 173 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 38) chain A residue 121 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7 39) 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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