eF-site ID 1lsj-B PDB Code 1lsj Chain 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 Homo sapiens (Human) (HCDH_HUMAN) Sequence B:  KIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSTIATS TDAASVVHSTDLVVEAIVQNLKVKNELFKRLDKFAAEHTI FASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEV IKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLL VPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLD YVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFG 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 109 type sequence V description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 9) chain B residue 110 type sequence Q description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 10) chain B residue 115 type sequence K description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 11) chain B residue 135 type sequence N description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 12) chain B residue 137 type sequence S description BINDING SITE FOR RESIDUE NAD B 750 source : AC2 13) chain B residue 143 type catalytic sequence S description 336 source MCSA : MCSA2 14) chain B residue 164 type catalytic sequence P description 336 source MCSA : MCSA2 15) chain B residue 176 type catalytic sequence M description 336 source MCSA : MCSA2 16) chain B residue 214 type catalytic sequence Y description 336 source MCSA : MCSA2 17) chain B residue 116 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 121 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 143 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 167 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 299 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 28 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 51 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 67 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 74 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10840044 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 164 type SITE sequence P description Important for catalytic activity => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 74 type MOD_RES sequence P description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 81 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 30) chain B residue 130 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 31) chain B residue 179 type MOD_RES sequence Q description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 186 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 196 type MOD_RES sequence P description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 34) chain B residue 206 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 35) chain B residue 235 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 36) chain B residue 75 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI5 37) chain B residue 119 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 38) chain B residue 173 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 source Swiss-Prot : SWS_FT_FI6 39) chain B residue 121 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 source Swiss-Prot : SWS_FT_FI7

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