Homo sapiens · seed P00441 · 154 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P00441 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 2.60.40.200 CATH 3.30.70.100 SCOP 8055253 SCOP 8055251 SCOP 8055259 SCOP 8062177 SCOP 8062205 SCOP 8062209 SCOP 8055265 SCOP 8062203 SCOP 8055277 RCSB 1HL4 PDBe
CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.
Every figure here is counted over the whole family rather than quoted from one entry.
1HL4, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.
How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.
142 distinct constructs across 252 entries. 236 polymer entities differ from the UniProt canonical sequence in some way, 11 carry a recognised expression tag and 0 carry a fusion partner.
"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.
| Entities | Length | Best (Å) | Best entry | What was made |
|---|---|---|---|---|
| 23 | 153 | 1.07 | 2C9V | residues 2-154 |
| 17 | 151 | 1.45 | 2ZOW | residues 2-152 |
| 14 | 153 | 1.25 | 6Z3V | residues 2-154; A5V |
| 8 | 153 | 0.98 | 4A7U | residues 2-154; I114T |
| 8 | 154 | 1.67 | 8CCX | matches the canonical sequence |
| 6 | 153 | 1.35 | 7T8G | residues 2-154; G94A |
| 6 | 153 | 1.55 | 1JCV | residues 2-154 |
| 6 | 154 | 1.80 | 3PU7 | residues 64-217 |
| 4 | 153 | 1.00 | 2WYT | residues 2-154; L39V |
| 4 | 153 | 1.02 | 1MFM | residues 2-154; C7A, F51E, G52E +2 more |
| 4 | 153 | 2.00 | 6FOI | residues 2-154; C58A, C147A |
| 3 | 152 | 1.15 | 1Q0E | matches the canonical sequence |
| 3 | 153 | 1.30 | 2VR6 | residues 2-154; G86R |
| 3 | 153 | 1.40 | 7WX0 | E40K, E51G, X53N |
| 3 | 153 | 1.75 | 3K91 | residues 2-154; H47R, H49Q |
| 3 | 153 | residues 2-154; C7A, C112S | ||
| 3 | 154 | 1.97 | 2WKO | G94A |
| 3 | 165 | 1.60 | 6D52 | His6; residues 21-177 |
| 3 | 180 | 1.90 | 5YTO | His6; TEV site |
| 2 | 110 | residues 2-154; 3 internal deletions; C7A, H47W, E50G +4 more | ||
| 2 | 152 | 0.99 | 3F7L | residues 2-153 |
| 2 | 153 | 1.41 | 7B4O | no UniProt reference for this entity, so it cannot be diffed against a canonical sequence |
| 2 | 153 | 2.00 | 2GBU | residues 2-154; C7A, C58A, C112A +1 more |
| 2 | 153 | 2.15 | 1OEZ | residues 2-154; H47R |
| 2 | 153 | 2.20 | 4MCM | residues 2-154; C58S |
Showing the 25 most-used of 142.
Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".
| Oligomeric state | Chains | Entries | Share |
|---|---|---|---|
| dimeric | 2 | 199 | 79.0% |
| monomeric | 1 | 28 | 11.1% |
| tetrameric | 4 | 8 | 3.2% |
| trimeric | 3 | 8 | 3.2% |
| hexameric | 6 | 5 | 2.0% |
| 24-meric | 24 | 2 | 0.8% |
| octameric | 8 | 1 | 0.4% |
| dodecameric | 12 | 1 | 0.4% |
176 entries have the depositor's assembly corroborated by PISA, 71 carry the depositor's word alone and 5 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 12 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1DO5, 1JK9, 1TO5, 1XTL, 1XTM, 2AQN, 2AQP, 2AQQ, 2AQR, 2AQT, 3HFF, 7FB9.
Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.
| Domain | Source | Span (seed) | Chains |
|---|---|---|---|
| Superoxide dismutase, copper/zinc binding domain | CATH 2.60.40.200 | 2–154 | 185 |
| 3.30.70.100 | CATH | 16–83 | 2 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8055253 | 2–154 | 118 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8055251 | 2–152 | 27 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8055259 | 4–154 | 11 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8062177 | 5–154 | 5 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8062205 | 24–154 | 2 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8062209 | 34–154 | 3 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8055265 | 37–154 | 2 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8062203 | 49–154 | 2 |
| Cu,Zn superoxide dismutase-like | SCOP2B 8055277 | 81–154 | 4 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| ZN | cofactor | Zinc Ion | 205 | 0.98 |
| CU | cofactor | Copper (Ii) Ion | 130 | 0.98 |
| SO4 | ion | Sulfate Ion | 72 | 0.98 |
| GOL | cryoprotectant | Glycerol | 25 | 1.25 |
| CU1 | ion | Copper (I) Ion | 23 | 0.99 |
| ACT | cryoprotectant | Acetate Ion | 19 | 0.98 |
| CL | ion | Chloride Ion | 15 | 1.00 |
| DMS | cryoprotectant | Dimethyl Sulfoxide | 8 | 1.65 |
| CA | ion | Calcium Ion | 7 | 1.80 |
| NA | ion | Sodium Ion | 6 | 0.99 |
| SCN | ion | Thiocyanate Ion | 5 | 1.30 |
| AZI | ion | Azide Ion | 4 | 1.55 |
| MLI | buffer | Malonate Ion | 4 | 1.55 |
| 9JT | ligand | N-Phenyl-2-Selanylbenzamide | 4 | 1.40 |
| HEM | cofactor | Protoporphyrin Ix Containing Fe | 3 | 1.50 |
| EDO | cryoprotectant | 1,2-Ethanediol | 3 | 1.30 |
| MES | buffer | 2-(N-Morpholino)-Ethanesulfonic Acid | 3 | 1.45 |
| S4P | ligand | Dihydrogen Tetrasulfide | 3 | 1.90 |
| PO4 | ion | Phosphate Ion | 2 | 1.35 |
| CD | ion | Cadmium Ion | 2 | 1.02 |
Parsed from the free text 203 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 215
entries that recorded anything at all.
Median pH 6.5
(range 3.8 to 9.0).
251 entries carry a wwPDB validation report: 124 clean, 84 worth a check and 43 with something to explain. Median clashscore 5.32, median RSRZ outliers 3.05%, median R-free minus R-work 0.039. 229 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 150 | 0.98 | 130 | 100% |
| Bos taurus | 25 | 1.15 | 28 | 100% |
| Saccharomyces cerevisiae | 11 | 1.35 | 11 | 97% |
| Canis lupus familiaris | 8 | 1.40 | 5 | 100% |
| Neisseria meningitidis | 6 | 1.30 | 6 | 82% |
| Solanum lycopersicum | 6 | 1.80 | 5 | 97% |
| Bombyx mori | 4 | 1.80 | 4 | 100% |
| Salmonella enterica subsp. enterica serovar Typhimurium | 3 | 1.70 | 3 | 75% |
| Alvinella pompejana | 2 | 0.99 | 2 | 98% |
| Caenorhabditis elegans | 2 | 1.10 | 1 | 99% |
| Bacteroidetes bacterium GWA2_30_7 | 2 | 1.41 | 2 | 97% |
| [Haemophilus] ducreyi | 2 | 1.50 | 2 | 73% |
154 residues, numbered every ten. Every identity figure in this document is measured against this sequence.
active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions
Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.
One record per paper, not per entry.
| Year | Citation |
|---|---|
| 2026 | The Mycobacterium abscessus cytochrome bcc:aa 3 oxidase structure paves the way for an agent targeting subunit QcrB. Nat Commun doi:10.1038/s41467-026-70805-5 |
| 2026 | Structural analysis of Cu/Zn-superoxide dismutase linked to neurodegenerative disease by antibody-guided cryo-EM. Protein Sci. doi:10.1002/pro.70615 |
| 2025 | Cu/Zn-superoxide dismutase naturally fused with a beta-propeller lactonase in Deinococcus radiodurans. J.Biol.Chem. doi:10.1016/j.jbc.2025.110499 |
| 2025 | Structural mechanisms and insights on multiple nanobodies binding diverse SOD1 epitopes. Commun Biol doi:10.1038/s42003-025-09293-0 |
| 2025 | Temperature-Dependent Structural Dynamics of SOD1 Revealed by Serial Synchrotron Crystallography Abant Med J doi:10.47493/abantmedj.1817591 |
| 2025 | Structural Insights into the Dynamics of Water in SOD1 Catalysis and Drug Interactions. Int J Mol Sci doi:10.3390/ijms26094228 |
| 2025 | Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N. Embo Rep. doi:10.1038/s44319-025-00557-8 |
| 2025 | Structural insights into the role of reduced cysteine residues in SOD1 amyloid filament formation. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2408582122 |
| 2024 | Ebselen analogues delay disease onset and its course in fALS by on-target SOD-1 engagement. Sci Rep doi:10.1038/s41598-024-62903-5 |
| 2024 | Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS. Plos Biol. doi:10.1371/journal.pbio.3002462 |
| 2024 | Structural insights into the modulation Of SOD1 aggregation By a fungal metabolite Phialomustin-B: Therapeutic potential in ALS. Plos One doi:10.1371/journal.pone.0298196 |
| 2024 | Disulfide-mediated oligomerization of mutant Cu/Zn-superoxide dismutase associated with canine degenerative myelopathy. Protein Sci. doi:10.1002/pro.5210 |
| 2024 | Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations. Sci Adv |
| 2023 | Intrinsic structural vulnerability in the hydrophobic core induces species-specific aggregation of canine SOD1 with degenerative myelopathy-linked E40K mutation. J.Biol.Chem. doi:10.1016/j.jbc.2023.104798 |
| 2023 | Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in Paenibacillus lautus missing a conserved disulfide bond. J.Biol.Chem. doi:10.1016/j.jbc.2023.105040 |
| 2023 | Hydrogen sulfide functions as a micro-modulator bound at the copper active site of Cu/Zn-SOD to regulate the catalytic activity of the enzyme. Cell Rep doi:10.1016/j.celrep.2023.112750 |
| 2023 | Direct relationship between dimeric form and activity in the acidic copper-zinc superoxide dismutase from lemon. Acta Crystallogr.,Sect.F doi:10.1107/S2053230X23010646 |
| 2023 | Structure-based discovery of an antipsychotic drug, paliperidone, as a modulator of human superoxide dismutase 1: a potential therapeutic target in amyotrophic lateral sclerosis. Acta Crystallogr D Struct Biol doi:10.1107/S2059798323003649 |
| 2023 | Structure of a superoxide dismutase from a tardigrade: Ramazzottius varieornatus strain YOKOZUNA-1. Acta Crystallogr.,Sect.F doi:10.1107/S2053230X2300523X |
| 2022 | Structural analysis of the overoxidized Cu/Zn-superoxide dismutase in ROS-induced ALS filament formation. Commun Biol doi:10.1038/s42003-022-04017-0 |
| 2022 | Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion. Nat Commun doi:10.1038/s41467-022-31240-4 |
| 2021 | Bacterial Evolutionary Precursors of Eukaryotic Copper-Zinc Superoxide Dismutases. Mol.Biol.Evol. doi:10.1093/molbev/msab157 |
| 2021 | Crystal Structure of a Cu,Zn Superoxide Dismutase From the Thermophilic Fungus Chaetomium thermophilum. Protein Pept.Lett. doi:10.2174/0929866528666210316104919 |
| 2021 | Transient Diffusive Interactions with a Protein Crowder Affect Aggregation Processes of Superoxide Dismutase 1 beta-Barrel. J.Phys.Chem.B doi:10.1021/acs.jpcb.0c11162 |
| 2020 | Novel Selenium-based compounds with therapeutic potential for SOD1-linked amyotrophic lateral sclerosis. Ebiomedicine doi:10.1016/j.ebiom.2020.102980 |
| 2020 | Ebselen as template for stabilization of A4V mutant dimer for motor neuron disease therapy. Commun Biol doi:10.1038/s42003-020-0826-3 |
| 2019 | Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS. Plos Biol. doi:10.1371/journal.pbio.3000141 |
| 2019 | Rational discovery of a SOD1 tryptophan oxidation inhibitor with therapeutic potential for amyotrophic lateral sclerosis. J.Biomol.Struct.Dyn. doi:10.1080/07391102.2018.1531787 |
| 2018 | The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation. Nat Commun doi:10.1038/s41467-018-04114-x |
| 2018 | The Cost of Long Catalytic Loops in Folding and Stability of the ALS-Associated Protein SOD1. J.Am.Chem.Soc. doi:10.1021/jacs.8b08141 |
| 2018 | Assessment of ligand binding at a site relevant to SOD1 oxidation and aggregation FEBS Lett. doi:10.1002/1873-3468.13055 |
| 2018 | Interaction of Half Oxa-/Halfcis-Platin Complex with Human Superoxide Dismutase and Induced Reduction of Neurotoxicity. ACS Med Chem Lett doi:10.1021/acsmedchemlett.8b00199 |
| 2017 | Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site. J. Biol. Chem. doi:10.1074/jbc.M117.775981 |
| 2016 | Tricking a Protein To Swap Strands. J. Am. Chem. Soc. doi:10.1021/jacs.6b05151 |
| 2016 | A Phosphomimetic Mutation Stabilizes SOD1 and Rescues Cell Viability in the Context of an ALS-Associated Mutation. Structure doi:10.1016/j.str.2016.08.011 |
| 2016 | SALS-linked WT-SOD1 adopts a highly similar helical conformation as FALS-causing L126Z-SOD1 in a membrane environment Biochim.Biophys.Acta doi:10.1016/j.bbamem.2016.06.027 |
| 2015 | Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase. J.Biol.Chem. doi:10.1074/jbc.M114.588798 |
| 2015 | The megavirus chilensis cu,zn-superoxide dismutase: the first viral structure of a typical cellular copper chaperone-independent hyperstable dimeric enzyme. J.Virol. doi:10.1128/JVI.02588-14 |
| 2015 | Thermodynamics of protein destabilization in live cells. Proc. Natl. Acad. Sci. U.S.A. doi:10.1073/pnas.1511308112 |
| 2015 | Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutations Biochim.Biophys.Acta doi:10.1016/j.bbamem.2014.10.002 |