eF-site ID 1pu0-ABCDEFGHIJ PDB Code 1pu0 Chain A, B, C, D, E, F, G, H, I, J 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 A:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ B:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ C:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ D:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ E:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ F:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ G:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ H:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ I:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ J:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ Description Functional site 1) chain A residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 A 200 source : AC1 2) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 A 200 source : AC1 3) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 A 200 source : AC1 4) chain A residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 A 200 source : AC1 5) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN A 201 source : AC2 6) chain A residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN A 201 source : AC2 7) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 201 source : AC2 8) chain A residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN A 201 source : AC2 9) chain B residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 B 200 source : AC3 10) chain B residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 B 200 source : AC3 11) chain B residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 B 200 source : AC3 12) chain B residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 B 200 source : AC3 13) chain B residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN B 201 source : AC4 14) chain B residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN B 201 source : AC4 15) chain B residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN B 201 source : AC4 16) chain B residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN B 201 source : AC4 17) chain C residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 C 200 source : AC5 18) chain C residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 C 200 source : AC5 19) chain C residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 C 200 source : AC5 20) chain C residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 C 200 source : AC5 21) chain C residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN C 201 source : AC6 22) chain C residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN C 201 source : AC6 23) chain C residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN C 201 source : AC6 24) chain C residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN C 201 source : AC6 25) chain D residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 D 200 source : AC7 26) chain D residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 D 200 source : AC7 27) chain D residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 D 200 source : AC7 28) chain D residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 D 200 source : AC7 29) chain D residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN D 201 source : AC8 30) chain D residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN D 201 source : AC8 31) chain D residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN D 201 source : AC8 32) chain D residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN D 201 source : AC8 33) chain E residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 E 200 source : AC9 34) chain E residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 E 200 source : AC9 35) chain E residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 E 200 source : AC9 36) chain E residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 E 200 source : AC9 37) chain E residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN E 201 source : BC1 38) chain E residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN E 201 source : BC1 39) chain E residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN E 201 source : BC1 40) chain E residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN E 201 source : BC1 41) chain F residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 F 200 source : BC2 42) chain F residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 F 200 source : BC2 43) chain F residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 F 200 source : BC2 44) chain F residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 F 200 source : BC2 45) chain F residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN F 201 source : BC3 46) chain F residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN F 201 source : BC3 47) chain F residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN F 201 source : BC3 48) chain F residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN F 201 source : BC3 49) chain G residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 G 200 source : BC4 50) chain G residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 G 200 source : BC4 51) chain G residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 G 200 source : BC4 52) chain G residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 G 200 source : BC4 53) chain G residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 54) chain G residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 55) chain G residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 56) chain G residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 57) chain G residue 136 type sequence K description BINDING SITE FOR RESIDUE ZN G 201 source : BC5 58) chain H residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 H 200 source : BC6 59) chain H residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 H 200 source : BC6 60) chain H residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 H 200 source : BC6 61) chain H residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 H 200 source : BC6 62) chain H residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN H 201 source : BC7 63) chain H residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN H 201 source : BC7 64) chain H residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN H 201 source : BC7 65) chain H residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN H 201 source : BC7 66) chain I residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 I 200 source : BC8 67) chain I residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 I 200 source : BC8 68) chain I residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 I 200 source : BC8 69) chain I residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 I 200 source : BC8 70) chain I residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN I 201 source : BC9 71) chain I residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN I 201 source : BC9 72) chain I residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN I 201 source : BC9 73) chain I residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN I 201 source : BC9 74) chain J residue 46 type sequence H description BINDING SITE FOR RESIDUE CU1 J 200 source : CC1 75) chain J residue 48 type sequence H description BINDING SITE FOR RESIDUE CU1 J 200 source : CC1 76) chain J residue 63 type sequence H description BINDING SITE FOR RESIDUE CU1 J 200 source : CC1 77) chain J residue 120 type sequence H description BINDING SITE FOR RESIDUE CU1 J 200 source : CC1 78) chain J residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN J 201 source : CC2 79) chain J residue 71 type sequence H description BINDING SITE FOR RESIDUE ZN J 201 source : CC2 80) chain J residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN J 201 source : CC2 81) chain J residue 83 type sequence D description BINDING SITE FOR RESIDUE ZN J 201 source : CC2 82) chain B residue 75 type sequence K description BINDING SITE FOR RESIDUE SO4 B 300 source : CC3 83) chain D residue 128 type sequence K description BINDING SITE FOR RESIDUE SO4 B 300 source : CC3 84) chain E residue 128 type sequence K description BINDING SITE FOR RESIDUE SO4 J 301 source : CC4 85) chain H residue 75 type sequence K description BINDING SITE FOR RESIDUE SO4 J 301 source : CC4 86) chain H residue 128 type sequence K description BINDING SITE FOR RESIDUE SO4 J 301 source : CC4 87) chain J residue 128 type sequence K description BINDING SITE FOR RESIDUE SO4 J 301 source : CC4 88) chain J residue 39 type sequence T description BINDING SITE FOR RESIDUE SO4 J 302 source : CC5 89) chain J residue 40 type sequence E description BINDING SITE FOR RESIDUE SO4 J 302 source : CC5 90) chain A residue 44-54 type prosite sequence GFHVHEFGDNT description SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHVHEfGDnT source prosite : PS00087 91) chain A residue 138-149 type prosite sequence GNAGSRLACGVI description SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI source prosite : PS00332 92) chain A residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 93) chain D residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 94) chain D residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 95) chain D residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 96) chain E residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 97) chain E residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 98) chain E residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 99) chain F residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 100) chain F residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 101) chain F residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 102) chain G residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 103) chain A residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 104) chain G residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 105) chain G residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 106) chain H residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 107) chain H residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 108) chain H residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 109) chain I residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 110) chain I residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 111) chain I residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 112) chain J residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 113) chain J residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 114) chain A residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 115) chain J residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 116) chain B residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 117) chain B residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 118) chain B residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 119) chain C residue 47 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 120) chain C residue 49 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 121) chain C residue 121 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 122) chain A residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 123) chain J residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 124) chain B residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 125) chain C residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 126) chain D residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 127) chain E residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 128) chain F residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 129) chain G residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 130) chain H residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 131) chain I residue 137 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI10 132) chain A residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 133) chain J residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 134) chain B residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 135) chain C residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 136) chain D residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 137) chain E residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 138) chain F residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 139) chain G residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 140) chain H residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 141) chain I residue 7 type LIPID sequence V description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 142) chain A 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 143) chain F 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 144) 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 145) chain H 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 146) 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 147) chain J 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 148) chain B 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 149) 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 150) 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 151) chain E 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 152) chain A residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 153) chain C residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 154) chain C residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 155) chain C residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 156) chain D residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 157) chain D residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 158) chain D residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 159) chain D residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 160) chain E residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 161) chain E residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 162) chain E residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 163) chain A residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 164) chain E residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 165) chain F residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 166) chain F residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 167) chain F residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 168) chain F residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 169) chain G residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 170) chain G residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 171) chain G residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 172) chain G residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 173) chain H residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 174) chain A residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 175) chain H residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 176) chain H residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 177) chain H residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 178) chain I residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 179) chain I residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 180) chain I residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 181) chain I residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 182) chain J residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 183) chain J residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 184) chain J residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 185) chain A residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 186) chain J residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 187) chain B residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 188) chain B residue 72 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 189) chain B residue 81 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 190) chain B residue 84 type BINDING sequence L description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 191) chain C residue 64 type BINDING sequence F description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 192) chain A 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 193) chain J 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 194) chain B 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 195) 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 196) 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 197) chain E 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 198) chain F 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 199) 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 200) chain H 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 201) 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 202) chain A residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 203) chain D residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 204) chain D residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 205) chain D residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 206) chain E residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 207) chain E residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 208) chain E residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 209) chain F residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 210) chain F residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 211) chain F residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 212) chain G residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 213) chain A residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 214) chain G residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 215) chain G residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 216) chain H residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 217) chain H residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 218) chain H residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 219) chain I residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 220) chain I residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 221) chain I residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 222) chain J residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 223) chain J residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 224) chain A residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 225) chain J residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 226) chain B residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 227) chain B residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 228) chain B residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 229) chain C residue 4 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 230) chain C residue 10 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 231) chain C residue 92 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 232) chain A 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 233) chain J 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 234) chain B 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 235) 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 236) 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 237) chain E 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 238) chain F 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 239) 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 240) chain H 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 241) 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 242) chain A residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 243) chain J residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 244) chain B residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 245) chain C residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 246) chain D residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 247) chain E residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 248) chain F residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 249) chain G residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 250) chain H residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 251) chain I residue 103 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 252) chain A residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 253) chain J residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 254) chain B residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 255) chain C residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 256) chain D residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 257) chain E residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 258) chain F residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 259) chain G residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 260) chain H residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 261) chain I residue 106 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 262) chain A residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 263) chain J residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 264) chain B residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 265) chain C residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 266) chain D residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 267) chain E residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 268) chain F residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 269) chain G residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 270) chain H residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 271) chain I residue 108 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 272) chain A residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 273) chain J residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 274) chain B residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 275) chain C residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 276) chain D residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 277) chain E residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 278) chain F residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 279) chain G residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 280) chain H residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 281) chain I residue 123 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links