eF-site ID 2r27-AB PDB Code 2r27 Chain A, B click to enlarge Title Constitutively zinc-deficient mutant of human superoxide dismutase (SOD), C6A, H80S, H83S, C111S Classification OXIDOREDUCTASE Compound Superoxide dismutase [Cu-Zn] Source null (SODC_HUMAN) Sequence A:  ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLRSVGSLGNVTADK DGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGN AGSRLACGVIGIAQ B:  ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLRSVGSLGNVTADK DGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGN AGSRLACGVIGIAQ Description Functional site 1) chain A residue 6 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 2) chain B residue 6 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 3) chain A residue 32 type CROSSLNK sequence W description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836 source Swiss-Prot : SWS_FT_FI12 4) chain B residue 32 type CROSSLNK sequence W description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836 source Swiss-Prot : SWS_FT_FI12 5) chain A residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 6) chain A residue 48 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 7) chain B residue 48 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 8) chain B residue 120 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 9) chain A residue 120 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 10) chain B residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 63 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 63 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 80 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 83 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 80 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 83 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 91 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 20) chain B residue 3 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 9 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 91 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 3 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 9 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 102 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 28) chain A residue 102 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 29) chain A residue 105 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 30) chain B residue 105 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 31) chain A residue 107 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 32) chain B residue 107 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 33) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 34) chain B residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9 35) chain A residue 44-54 type prosite sequence GFHVHEFGDNT description SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHVHEfGDnT source prosite : PS00087

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