eF-site ID 1pu0-G PDB Code 1pu0 Chain G click to enlarge Title Structure of Human Cu,Zn Superoxide Dismutase Classification OXIDOREDUCTASE Compound Superoxide dismutase [Cu-Zn] Source Homo sapiens (Human) (SODC_HUMAN) Sequence G:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ Description Functional site 1) chain G residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 G 200 source : BC4 2) chain G residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 G 200 source : BC4 3) chain G residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 G 200 source : BC4 4) chain G residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 G 200 source : BC4 5) chain G residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 6) chain G residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 7) chain G residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 8) chain G residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 9) chain G residue 136 type sequence K description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 10) chain G residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 11) chain G residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 12) chain G residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 13) chain G residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 14) chain G residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 15) chain G residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 16) chain G residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 17) chain G residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 18) chain G residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 19) chain G residue 99 type MOD_RES sequence I description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 20) chain G residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 21) chain G residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 22) chain G residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 23) chain G residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 24) chain G residue 33 type CROSSLNK sequence G description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836 source Swiss-Prot : SWS_FT_FI12 25) chain G residue 2 type MOD_RES sequence T description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3 26) chain G residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 27) chain G residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 28) chain G residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4

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