eF-site ID 2iik-AB PDB Code 2iik Chain A, B click to enlarge Title Crystal Structure of human peroxisomal acetyl-CoA acyl transferase 1 (ACAA1) Classification TRANSFERASE Compound 3-ketoacyl-CoA thiolase, peroxisomal Source Homo sapiens (Human) (THIK_HUMAN) Sequence A:  ASAADVVVVHGRRTAICRAGRGGFKDTTPDELLSAVMTAV LKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPE TVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGVES MSLADGNITSRLMEKEKARDCLIPMGITSENVAERFGISR EKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGT KRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSS QVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDI MGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCV EKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKR RGKRAYGVVSMCIGTGMGAAAVFEYP B:  TENLYFQSMAPQASAADVVVVHGRRTAICRAGRGGFKDTT PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIM ARIAQFLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNG SYDIGMACGVESMSLAPGNITSRLMEKEKARDCLIPMGIT SENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIV PVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAF KKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVL RSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEI NEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGA RQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN Description Functional site 1) chain A residue 119-137 type prosite sequence VNRQCSSGLQAVASIAGGI description THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VNRqCSSGLqAVasiaggI source prosite : PS00098 2) chain A residue 404-417 type prosite sequence GVVSMCIGTGMGAA description THIOLASE_3 Thiolases active site. GVVSMCIGtGmGaA source prosite : PS00099 3) chain A residue 368-384 type prosite sequence NPLGGAVALGHPLGCTG description THIOLASE_2 Thiolases signature 2. NplGGaVAlGHPlGcTG source prosite : PS00737 4) chain A residue 123 type ACT_SITE sequence C description Acyl-thioester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 5) chain B residue 123 type ACT_SITE sequence C description Acyl-thioester intermediate => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 6) chain A residue 378 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 409 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 378 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 409 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020 source Swiss-Prot : SWS_FT_FI2 10) chain A residue 59 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 60 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 59 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 60 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI3

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