eF-site ID 6h23-F PDB Code 6h23 Chain F click to enlarge Title Crystal structure of the hClpP Y118A mutant with an activating small molecule Classification HYDROLASE Compound ATP-dependent Clp protease proteolytic subunit, mitochondrial Source (CLPP_HUMAN) Sequence F:  DIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKK PIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAAS MGSLLLAAGTPGMRHSLPNSRIMIHQPDIAIQAEEIMKLK KQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILD KVLVHP Description (1)  ATP-dependent Clp protease proteolytic subunit, mitochondrial (E.C.3.4.21.92) Functional site 1) chain F residue 78 type sequence R description binding site for residue FJT E 301 source : AC6 2) chain F residue 79 type sequence L description binding site for residue FJT E 301 source : AC6 3) chain F residue 82 type sequence E description binding site for residue FJT E 301 source : AC6 4) chain F residue 84 type sequence I description binding site for residue FJT E 301 source : AC6 5) chain F residue 146 type sequence W description binding site for residue FJT E 301 source : AC6 6) chain F residue 148 type sequence V description binding site for residue FJT E 301 source : AC6 7) chain F residue 101 type sequence A description binding site for residue FJT F 301 source : AC8 8) chain F residue 104 type sequence L description binding site for residue FJT F 301 source : AC8 9) chain F residue 105 type sequence F description binding site for residue FJT F 301 source : AC8 10) chain F residue 108 type sequence S description binding site for residue FJT F 301 source : AC8 11) chain F residue 138 type sequence Y description binding site for residue FJT F 301 source : AC8 12) chain F residue 179 type sequence Q description binding site for residue EDO F 302 source : AC9 13) chain F residue 198 type sequence I description binding site for residue EDO F 302 source : AC9 14) chain F residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 15) chain F residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 16) chain F residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 17) chain F residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4

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