eF-site ID 2r27-A PDB Code 2r27 Chain A 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 Homo sapiens (Human) (SODC_HUMAN) Sequence A:  ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSAGPHFNPLRSVGSLGNVTADK DGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGN AGSRLACGVIGIAQ Description Functional site 1) chain A residue 44-54 type prosite sequence GFHVHEFGDNT description SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHVHEfGDnT source prosite : PS00087 2) chain A residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 3) chain A residue 48 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 4) chain A residue 120 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 6 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122 source Swiss-Prot : SWS_FT_FI11 6) 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 7) chain A residue 63 type BINDING sequence H description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 8) chain A residue 80 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 83 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20727846 source Swiss-Prot : SWS_FT_FI2 10) 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 11) chain A residue 3 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 9 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 91 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI4 14) 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 15) chain A residue 102 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 16) chain A residue 105 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P07632 source Swiss-Prot : SWS_FT_FI7 17) chain A residue 107 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08228 source Swiss-Prot : SWS_FT_FI8 18) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062 source Swiss-Prot : SWS_FT_FI9

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