eF-site ID 1pu0-C PDB Code 1pu0 Chain C 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 C:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ Description Functional site 1) chain C residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 C 200 source : AC5 2) chain C residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 C 200 source : AC5 3) chain C residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 C 200 source : AC5 4) chain C residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 C 200 source : AC5 5) chain C residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN C 201 source : AC6 6) chain C residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN C 201 source : AC6 7) chain C residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN C 201 source : AC6 8) chain C residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN C 201 source : AC6 9) chain C residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 10) chain C residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 11) chain C residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 12) chain C residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 13) chain C residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 14) chain C residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 15) chain C residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 16) chain C residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 17) chain C residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 18) chain C 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 19) chain C residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 20) chain C residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 21) chain C residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 22) chain C residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 23) chain C 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 24) chain C 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 25) chain C residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 26) chain C residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 27) chain C residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links