eF-site ID 6h23-B PDB Code 6h23 Chain B 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 B:  DIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKK PIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAAS MGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLKK QLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDK VLVHPP Description (1)  ATP-dependent Clp protease proteolytic subunit, mitochondrial (E.C.3.4.21.92) Functional site 1) chain B residue 79 type sequence L description binding site for residue FJT A 301 source : AC1 2) chain B residue 82 type sequence E description binding site for residue FJT A 301 source : AC1 3) chain B residue 84 type sequence I description binding site for residue FJT A 301 source : AC1 4) chain B residue 146 type sequence W description binding site for residue FJT A 301 source : AC1 5) chain B residue 148 type sequence V description binding site for residue FJT A 301 source : AC1 6) chain B residue 100 type sequence I description binding site for residue FJT B 301 source : AC3 7) chain B residue 101 type sequence A description binding site for residue FJT B 301 source : AC3 8) chain B residue 104 type sequence L description binding site for residue FJT B 301 source : AC3 9) chain B residue 105 type sequence F description binding site for residue FJT B 301 source : AC3 10) chain B residue 107 type sequence Q description binding site for residue FJT B 301 source : AC3 11) chain B residue 108 type sequence S description binding site for residue FJT B 301 source : AC3 12) chain B residue 135 type sequence T description binding site for residue FJT B 301 source : AC3 13) chain B residue 138 type sequence Y description binding site for residue FJT B 301 source : AC3 14) chain B residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4

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