eF-site ID 2qq2-ABCDEFGHIJKL PDB Code 2qq2 Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7 Classification HYDROLASE Compound Cytosolic acyl coenzyme A thioester hydrolase Source null (BACH_HUMAN) Sequence A:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPVVSQKRYRAASAFFTYVSLSQEG RSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGH B:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQ EGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQ C:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPVVDSQKRYRAASAFFTYVSLSQE GRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGH D:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQ EGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKA E:  NPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDE VAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRM TFTSNKSMEIEVLVDADPVQKRYRAASAFFTYVSLSQEGR SLPVPQLVPETEDEKKRFEEGKGRYLQMKA F:  EPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVA GIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTF TSNKSMEIEVLVDADPVVQKRYRAASAFFTYVSLSQEGRS LPVPQLVPETEDEKKRFEEGKGRYLQMKA G:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPVKRYRAASAFFTYVSLSQEGRSL PVPQLVPETEDEKKRFEEGKGRYLQMKA H:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPVVDKRYRAASAFFTYVSLSQEGR SLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQ I:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQ EGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAK J:  TVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIV AARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSN KSMEIEVLVDADPVRYRAASAFFTYVSLSQEGRSLPVPQL VPETEDEKKRFEEGKGRYLQMKA K:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQ EGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQ L:  PEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEV AGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMT FTSNKSMEIEVLVDADPSQKRYRAASAFFTYVSLSQEGRS LPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGH Description Functional site 1) chain A residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 3) chain C residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 5) chain E residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 6) chain F residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 7) chain G residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 8) chain H residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 9) chain I residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 10) chain J residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 11) chain K residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain L residue 245 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 15) chain C residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 16) chain D residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 17) chain E residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 18) chain F residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 19) chain G residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 20) chain H residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 21) chain I residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 22) chain J residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 23) chain K residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 24) chain L residue 273 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2

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