eF-site ID 1pu0-I PDB Code 1pu0 Chain I 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 I:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ Description Functional site 1) chain I residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 I 200 source : BC8 2) chain I residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 I 200 source : BC8 3) chain I residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 I 200 source : BC8 4) chain I residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 I 200 source : BC8 5) chain I residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN I 201 source : BC9 6) chain I residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN I 201 source : BC9 7) chain I residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN I 201 source : BC9 8) chain I residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN I 201 source : BC9 9) chain I residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 10) chain I residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 11) chain I residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 12) chain I residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 13) chain I residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 14) chain I 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 15) chain I residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 16) chain I residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 17) chain I residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 18) chain I residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 19) chain I 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 20) chain I residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 21) chain I residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 22) chain I residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 23) chain I 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 24) chain I residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 25) chain I residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 26) chain I residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 27) chain I residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9

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