eF-site ID 6h23-ABCDEFGHIJKLMN PDB Code 6h23 Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N 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 A:  DIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKK PIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAAS MGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLKK QLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDK VLVHP B:  DIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKK PIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAAS MGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLKK QLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDK VLVHPP C:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLK KQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILD KVLVHP D:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPIQAEEIMKLKKQ LYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKV LVHP E:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLK KQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILD KVLVHP F:  DIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKK PIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAAS MGSLLLAAGTPGMRHSLPNSRIMIHQPDIAIQAEEIMKLK KQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILD KVLVHP G:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPSDIAIQAEEIMK LKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGI LDKVLVHPP H:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPDIAIQAEEIMKL KKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGIL DKVLVHP I:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPDIAIQAEEIMKL KKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGIL DKVLVHP J:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLK KQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILD KVLVHP K:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLK KQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILD KVLVHP L:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLK KQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILD KVLVHP M:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPIAIQAEEIMKLK KQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILD KVLVHP N:  YDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNK KPIHMAINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAA SMGSLLLAAGTPGMRHSLPNSRIMIHQPSIAIQAEEIMKL KKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGIL DKVLVHPP Description (1)  ATP-dependent Clp protease proteolytic subunit, mitochondrial (E.C.3.4.21.92) Functional site 1) chain A residue 101 type sequence A description binding site for residue FJT A 301 source : AC1 2) chain A residue 104 type sequence L description binding site for residue FJT A 301 source : AC1 3) chain A residue 105 type sequence F description binding site for residue FJT A 301 source : AC1 4) chain A residue 108 type sequence S description binding site for residue FJT A 301 source : AC1 5) chain A residue 138 type sequence Y description binding site for residue FJT A 301 source : AC1 6) chain B residue 79 type sequence L description binding site for residue FJT A 301 source : AC1 7) chain B residue 82 type sequence E description binding site for residue FJT A 301 source : AC1 8) chain B residue 84 type sequence I description binding site for residue FJT A 301 source : AC1 9) chain B residue 146 type sequence W description binding site for residue FJT A 301 source : AC1 10) chain B residue 148 type sequence V description binding site for residue FJT A 301 source : AC1 11) chain A residue 194 type sequence Q description binding site for residue EDO A 302 source : AC2 12) chain A residue 195 type sequence A description binding site for residue EDO A 302 source : AC2 13) chain H residue 179 type sequence Q description binding site for residue EDO A 302 source : AC2 14) chain H residue 202 type sequence K description binding site for residue EDO A 302 source : AC2 15) chain B residue 100 type sequence I description binding site for residue FJT B 301 source : AC3 16) chain B residue 101 type sequence A description binding site for residue FJT B 301 source : AC3 17) chain B residue 104 type sequence L description binding site for residue FJT B 301 source : AC3 18) chain B residue 105 type sequence F description binding site for residue FJT B 301 source : AC3 19) chain B residue 107 type sequence Q description binding site for residue FJT B 301 source : AC3 20) chain B residue 108 type sequence S description binding site for residue FJT B 301 source : AC3 21) chain B residue 135 type sequence T description binding site for residue FJT B 301 source : AC3 22) chain B residue 138 type sequence Y description binding site for residue FJT B 301 source : AC3 23) chain C residue 78 type sequence R description binding site for residue FJT B 301 source : AC3 24) chain C residue 79 type sequence L description binding site for residue FJT B 301 source : AC3 25) chain C residue 82 type sequence E description binding site for residue FJT B 301 source : AC3 26) chain C residue 84 type sequence I description binding site for residue FJT B 301 source : AC3 27) chain C residue 146 type sequence W description binding site for residue FJT B 301 source : AC3 28) chain C residue 148 type sequence V description binding site for residue FJT B 301 source : AC3 29) chain C residue 100 type sequence I description binding site for residue FJT D 301 source : AC4 30) chain C residue 101 type sequence A description binding site for residue FJT D 301 source : AC4 31) chain C residue 104 type sequence L description binding site for residue FJT D 301 source : AC4 32) chain C residue 105 type sequence F description binding site for residue FJT D 301 source : AC4 33) chain C residue 108 type sequence S description binding site for residue FJT D 301 source : AC4 34) chain C residue 138 type sequence Y description binding site for residue FJT D 301 source : AC4 35) chain D residue 79 type sequence L description binding site for residue FJT D 301 source : AC4 36) chain D residue 82 type sequence E description binding site for residue FJT D 301 source : AC4 37) chain D residue 84 type sequence I description binding site for residue FJT D 301 source : AC4 38) chain D residue 146 type sequence W description binding site for residue FJT D 301 source : AC4 39) chain D residue 148 type sequence V description binding site for residue FJT D 301 source : AC4 40) chain D residue 100 type sequence I description binding site for residue FJT D 302 source : AC5 41) chain D residue 101 type sequence A description binding site for residue FJT D 302 source : AC5 42) chain D residue 104 type sequence L description binding site for residue FJT D 302 source : AC5 43) chain D residue 105 type sequence F description binding site for residue FJT D 302 source : AC5 44) chain D residue 108 type sequence S description binding site for residue FJT D 302 source : AC5 45) chain D residue 138 type sequence Y description binding site for residue FJT D 302 source : AC5 46) chain E residue 78 type sequence R description binding site for residue FJT D 302 source : AC5 47) chain E residue 79 type sequence L description binding site for residue FJT D 302 source : AC5 48) chain E residue 82 type sequence E description binding site for residue FJT D 302 source : AC5 49) chain E residue 146 type sequence W description binding site for residue FJT D 302 source : AC5 50) chain E residue 100 type sequence I description binding site for residue FJT E 301 source : AC6 51) chain E residue 101 type sequence A description binding site for residue FJT E 301 source : AC6 52) chain E residue 104 type sequence L description binding site for residue FJT E 301 source : AC6 53) chain E residue 105 type sequence F description binding site for residue FJT E 301 source : AC6 54) chain E residue 108 type sequence S description binding site for residue FJT E 301 source : AC6 55) chain E residue 138 type sequence Y description binding site for residue FJT E 301 source : AC6 56) chain F residue 78 type sequence R description binding site for residue FJT E 301 source : AC6 57) chain F residue 79 type sequence L description binding site for residue FJT E 301 source : AC6 58) chain F residue 82 type sequence E description binding site for residue FJT E 301 source : AC6 59) chain F residue 84 type sequence I description binding site for residue FJT E 301 source : AC6 60) chain F residue 146 type sequence W description binding site for residue FJT E 301 source : AC6 61) chain F residue 148 type sequence V description binding site for residue FJT E 301 source : AC6 62) chain E residue 202 type sequence K description binding site for residue EDO E 302 source : AC7 63) chain F residue 101 type sequence A description binding site for residue FJT F 301 source : AC8 64) chain F residue 104 type sequence L description binding site for residue FJT F 301 source : AC8 65) chain F residue 105 type sequence F description binding site for residue FJT F 301 source : AC8 66) chain F residue 108 type sequence S description binding site for residue FJT F 301 source : AC8 67) chain F residue 138 type sequence Y description binding site for residue FJT F 301 source : AC8 68) chain G residue 79 type sequence L description binding site for residue FJT F 301 source : AC8 69) chain G residue 82 type sequence E description binding site for residue FJT F 301 source : AC8 70) chain G residue 84 type sequence I description binding site for residue FJT F 301 source : AC8 71) chain G residue 146 type sequence W description binding site for residue FJT F 301 source : AC8 72) chain G residue 148 type sequence V description binding site for residue FJT F 301 source : AC8 73) chain F residue 179 type sequence Q description binding site for residue EDO F 302 source : AC9 74) chain F residue 198 type sequence I description binding site for residue EDO F 302 source : AC9 75) chain A residue 79 type sequence L description binding site for residue FJT G 301 source : AD1 76) chain A residue 82 type sequence E description binding site for residue FJT G 301 source : AD1 77) chain A residue 84 type sequence I description binding site for residue FJT G 301 source : AD1 78) chain A residue 146 type sequence W description binding site for residue FJT G 301 source : AD1 79) chain G residue 100 type sequence I description binding site for residue FJT G 301 source : AD1 80) chain G residue 101 type sequence A description binding site for residue FJT G 301 source : AD1 81) chain G residue 104 type sequence L description binding site for residue FJT G 301 source : AD1 82) chain G residue 105 type sequence F description binding site for residue FJT G 301 source : AD1 83) chain G residue 108 type sequence S description binding site for residue FJT G 301 source : AD1 84) chain G residue 138 type sequence Y description binding site for residue FJT G 301 source : AD1 85) chain H residue 78 type sequence R description binding site for residue FJT H 301 source : AD2 86) chain H residue 79 type sequence L description binding site for residue FJT H 301 source : AD2 87) chain H residue 82 type sequence E description binding site for residue FJT H 301 source : AD2 88) chain H residue 146 type sequence W description binding site for residue FJT H 301 source : AD2 89) chain H residue 148 type sequence V description binding site for residue FJT H 301 source : AD2 90) chain N residue 100 type sequence I description binding site for residue FJT H 301 source : AD2 91) chain N residue 101 type sequence A description binding site for residue FJT H 301 source : AD2 92) chain N residue 104 type sequence L description binding site for residue FJT H 301 source : AD2 93) chain N residue 105 type sequence F description binding site for residue FJT H 301 source : AD2 94) chain N residue 108 type sequence S description binding site for residue FJT H 301 source : AD2 95) chain N residue 138 type sequence Y description binding site for residue FJT H 301 source : AD2 96) chain H residue 100 type sequence I description binding site for residue FJT H 302 source : AD3 97) chain H residue 101 type sequence A description binding site for residue FJT H 302 source : AD3 98) chain H residue 104 type sequence L description binding site for residue FJT H 302 source : AD3 99) chain H residue 105 type sequence F description binding site for residue FJT H 302 source : AD3 100) chain H residue 107 type sequence Q description binding site for residue FJT H 302 source : AD3 101) chain H residue 108 type sequence S description binding site for residue FJT H 302 source : AD3 102) chain H residue 138 type sequence Y description binding site for residue FJT H 302 source : AD3 103) chain I residue 79 type sequence L description binding site for residue FJT H 302 source : AD3 104) chain I residue 82 type sequence E description binding site for residue FJT H 302 source : AD3 105) chain I residue 84 type sequence I description binding site for residue FJT H 302 source : AD3 106) chain I residue 100 type sequence I description binding site for residue FJT J 301 source : AD4 107) chain I residue 101 type sequence A description binding site for residue FJT J 301 source : AD4 108) chain I residue 104 type sequence L description binding site for residue FJT J 301 source : AD4 109) chain I residue 105 type sequence F description binding site for residue FJT J 301 source : AD4 110) chain I residue 108 type sequence S description binding site for residue FJT J 301 source : AD4 111) chain I residue 138 type sequence Y description binding site for residue FJT J 301 source : AD4 112) chain J residue 78 type sequence R description binding site for residue FJT J 301 source : AD4 113) chain J residue 79 type sequence L description binding site for residue FJT J 301 source : AD4 114) chain J residue 82 type sequence E description binding site for residue FJT J 301 source : AD4 115) chain J residue 146 type sequence W description binding site for residue FJT J 301 source : AD4 116) chain J residue 148 type sequence V description binding site for residue FJT J 301 source : AD4 117) chain J residue 101 type sequence A description binding site for residue FJT K 301 source : AD5 118) chain J residue 104 type sequence L description binding site for residue FJT K 301 source : AD5 119) chain J residue 105 type sequence F description binding site for residue FJT K 301 source : AD5 120) chain J residue 108 type sequence S description binding site for residue FJT K 301 source : AD5 121) chain J residue 138 type sequence Y description binding site for residue FJT K 301 source : AD5 122) chain K residue 78 type sequence R description binding site for residue FJT K 301 source : AD5 123) chain K residue 79 type sequence L description binding site for residue FJT K 301 source : AD5 124) chain K residue 82 type sequence E description binding site for residue FJT K 301 source : AD5 125) chain K residue 84 type sequence I description binding site for residue FJT K 301 source : AD5 126) chain K residue 116 type sequence H description binding site for residue FJT K 301 source : AD5 127) chain K residue 118 type sequence A description binding site for residue FJT K 301 source : AD5 128) chain K residue 146 type sequence W description binding site for residue FJT K 301 source : AD5 129) chain K residue 148 type sequence V description binding site for residue FJT K 301 source : AD5 130) chain K residue 104 type sequence L description binding site for residue FJT L 301 source : AD6 131) chain K residue 105 type sequence F description binding site for residue FJT L 301 source : AD6 132) chain K residue 108 type sequence S description binding site for residue FJT L 301 source : AD6 133) chain K residue 135 type sequence T description binding site for residue FJT L 301 source : AD6 134) chain K residue 138 type sequence Y description binding site for residue FJT L 301 source : AD6 135) chain L residue 78 type sequence R description binding site for residue FJT L 301 source : AD6 136) chain L residue 79 type sequence L description binding site for residue FJT L 301 source : AD6 137) chain L residue 82 type sequence E description binding site for residue FJT L 301 source : AD6 138) chain L residue 84 type sequence I description binding site for residue FJT L 301 source : AD6 139) chain L residue 118 type sequence A description binding site for residue FJT L 301 source : AD6 140) chain L residue 146 type sequence W description binding site for residue FJT L 301 source : AD6 141) chain L residue 148 type sequence V description binding site for residue FJT L 301 source : AD6 142) chain L residue 170 type sequence L description binding site for residue FJT L 301 source : AD6 143) chain L residue 100 type sequence I description binding site for residue FJT M 301 source : AD7 144) chain L residue 104 type sequence L description binding site for residue FJT M 301 source : AD7 145) chain L residue 105 type sequence F description binding site for residue FJT M 301 source : AD7 146) chain L residue 107 type sequence Q description binding site for residue FJT M 301 source : AD7 147) chain L residue 108 type sequence S description binding site for residue FJT M 301 source : AD7 148) chain M residue 79 type sequence L description binding site for residue FJT M 301 source : AD7 149) chain M residue 82 type sequence E description binding site for residue FJT M 301 source : AD7 150) chain M residue 84 type sequence I description binding site for residue FJT M 301 source : AD7 151) chain M residue 146 type sequence W description binding site for residue FJT M 301 source : AD7 152) chain M residue 148 type sequence V description binding site for residue FJT M 301 source : AD7 153) chain M residue 101 type sequence A description binding site for residue FJT M 302 source : AD8 154) chain M residue 104 type sequence L description binding site for residue FJT M 302 source : AD8 155) chain M residue 105 type sequence F description binding site for residue FJT M 302 source : AD8 156) chain M residue 108 type sequence S description binding site for residue FJT M 302 source : AD8 157) chain M residue 138 type sequence Y description binding site for residue FJT M 302 source : AD8 158) chain N residue 79 type sequence L description binding site for residue FJT M 302 source : AD8 159) chain N residue 82 type sequence E description binding site for residue FJT M 302 source : AD8 160) chain N residue 84 type sequence I description binding site for residue FJT M 302 source : AD8 161) chain N residue 146 type sequence W description binding site for residue FJT M 302 source : AD8 162) chain N residue 148 type sequence V description binding site for residue FJT M 302 source : AD8 163) chain N residue 179 type sequence Q description binding site for residue EDO N 301 source : AD9 164) chain N residue 198 type sequence I description binding site for residue EDO N 301 source : AD9 165) chain N residue 202 type sequence K description binding site for residue EDO N 301 source : AD9 166) chain A residue 145-156 type prosite sequence TWCVGQAASMGS description CLP_PROTEASE_SER Endopeptidase Clp serine active site. TwcVGqAASMGS source prosite : PS00381 167) chain A residue 167-180 type prosite sequence RHSLPNSRIMIHQP description CLP_PROTEASE_HIS Endopeptidase Clp histidine active site. RhslPnsrIMIHQP source prosite : PS00382 168) chain A residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 169) chain B residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 170) chain C residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 171) chain D residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 172) chain E residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 173) chain F residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 174) chain G residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 175) chain H residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 176) chain I residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 177) chain J residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 178) chain K residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 179) chain L residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 180) chain M residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 181) chain N residue 153 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:11923310 source Swiss-Prot : SWS_FT_FI1 182) chain A residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 183) chain B residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 184) chain C residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 185) chain D residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 186) chain E residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 187) chain F residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 188) chain G residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 189) chain H residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 190) chain I residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 191) chain J residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 192) chain K residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 193) chain L residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 194) chain M residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 195) chain N residue 178 type ACT_SITE sequence H description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 196) chain A residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 197) chain B residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 198) chain C residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 199) chain D residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 200) chain E residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 201) chain F residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 202) chain G residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 203) chain H residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 204) chain I residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 205) chain J residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 206) chain K residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 207) chain L residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 208) chain M residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 209) chain N residue 200 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88696 source Swiss-Prot : SWS_FT_FI3 210) chain A residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 211) chain B residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 212) chain C residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 213) chain D residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 214) chain E residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 215) chain F residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 216) chain G residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 217) chain H residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 218) chain I residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 219) chain J residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 220) chain K residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 221) chain L residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 222) chain M residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 223) chain N residue 211 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4

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