eF-site ID 1pu0-D PDB Code 1pu0 Chain D 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 D:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ Description Functional site 1) chain D residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 D 200 source : AC7 2) chain D residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 D 200 source : AC7 3) chain D residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 D 200 source : AC7 4) chain D residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 D 200 source : AC7 5) chain D residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN D 201 source : AC8 6) chain D residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN D 201 source : AC8 7) chain D residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN D 201 source : AC8 8) chain D residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN D 201 source : AC8 9) chain D residue 128 type sequence K description BINDING SITE FOR RESIDUE SO4 B 300 source : CC3 10) chain D residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 11) chain D residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 12) chain D residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 13) chain D residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 14) chain D residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 15) chain D residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 16) chain D residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 17) chain D residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 18) chain D residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 19) chain D 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 D residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 21) chain D residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 22) chain D residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 23) chain D residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 24) chain D 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 D 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 D residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 27) chain D residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 28) chain D residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4

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