eF-site ID 4bcy-A PDB Code 4bcy Chain A click to enlarge Title Monomeric Human Cu,Zn Superoxide dismutase, mutation H43F Classification OXIDOREDUCTASE Compound SUPEROXIDE DISMUTASE [CU-ZN] Source (SODC_HUMAN) Sequence A:  ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLFGFHVHEEEDAGPHFNPLSRKHGGPKDEERHVGDLGNV TADKDGVADVSIEDSVISLSGDHAIIGRTLVVHEKADDLG KGGNEESTKTGNAGSRLACGVIGIAQ Description Functional site 1) chain A residue 46 type sequence H description BINDING SITE FOR RESIDUE CU A 1153 source : AC1 2) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE CU A 1153 source : AC1 3) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE CU A 1153 source : AC1 4) chain A residue 120 type sequence H description BINDING SITE FOR RESIDUE CU A 1153 source : AC1 5) chain A residue 46 type sequence H description BINDING SITE FOR RESIDUE CU A 1154 source : AC2 6) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE CU A 1154 source : AC2 7) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE CU A 1154 source : AC2 8) chain A residue 120 type sequence H description BINDING SITE FOR RESIDUE CU A 1154 source : AC2 9) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN A 1155 source : AC3 10) chain A residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN A 1155 source : AC3 11) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 1155 source : AC3 12) chain A residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN A 1155 source : AC3 13) chain A residue 1 type sequence A description BINDING SITE FOR RESIDUE CD A 1156 source : AC4 14) chain A residue 51 type sequence E description BINDING SITE FOR RESIDUE CD A 1156 source : AC4 15) chain A residue 96 type sequence D description BINDING SITE FOR RESIDUE CD A 1156 source : AC4 16) chain A residue 78 type sequence E description BINDING SITE FOR RESIDUE CD A 1157 source : AC5 17) chain A residue 121 type sequence E description BINDING SITE FOR RESIDUE CD A 1157 source : AC5 18) chain A residue 50 type sequence E description BINDING SITE FOR RESIDUE CD A 1158 source : AC6 19) chain A residue 52 type sequence D description BINDING SITE FOR RESIDUE CD A 1158 source : AC6 20) chain A residue 90 type sequence D description BINDING SITE FOR RESIDUE CD A 1158 source : AC6 21) chain A residue 92 type sequence D description BINDING SITE FOR RESIDUE CD A 1158 source : AC6 22) chain A residue 52 type sequence D description BINDING SITE FOR RESIDUE CD A 1159 source : AC7 23) chain A residue 90 type sequence D description BINDING SITE FOR RESIDUE CD A 1159 source : AC7 24) chain A residue 110 type sequence H description BINDING SITE FOR RESIDUE CD A 1160 source : AC8 25) chain A residue 153 type sequence Q description BINDING SITE FOR RESIDUE CD A 1160 source : AC8 26) chain A residue 109 type sequence D description BINDING SITE FOR RESIDUE CD A 1161 source : AC9 27) chain A residue 110 type sequence H description BINDING SITE FOR RESIDUE CD A 1161 source : AC9 28) chain A residue 153 type sequence Q description BINDING SITE FOR RESIDUE CD A 1161 source : AC9 29) chain A residue 67 type sequence L description BINDING SITE FOR RESIDUE CL A 1162 source : BC1 30) chain A residue 68 type sequence S description BINDING SITE FOR RESIDUE CL A 1162 source : BC1 31) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE CL A 1162 source : BC1 32) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 1162 source : BC1 33) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE CL A 1163 source : BC2 34) chain A residue 50 type sequence E description BINDING SITE FOR RESIDUE CL A 1163 source : BC2 35) chain A residue 61 type sequence G description BINDING SITE FOR RESIDUE CL A 1163 source : BC2 36) chain A residue 136 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 37) chain A residue 6 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 38) chain A residue 32 type CROSSLNK sequence W description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836 source Swiss-Prot : SWS_FT_FI12 39) chain A residue 3 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 40) chain A residue 9 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 91 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 42) chain A residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 102 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 44) chain A residue 105 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 45) chain A residue 107 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 46) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 47) chain A residue 138-149 type prosite sequence GNAGSRLACGVI description SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI source prosite : PS00332 48) chain A residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 48 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 120 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 63 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 71 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 80 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 83 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3

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