Homo sapiens · seed P05067 · 770 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P05067 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.90.570.10 CATH 3.30.1490.140 CATH 4.10.410.10 CATH 1.20.120.770 CATH 2.40.10.10 CATH 2.60.40.10 CATH 4.10.230.10 CATH 2.30.29.30 SCOP 8037154 SCOP 8041099 SCOP 8038485 SCOP 8038452 SCOP 8036274 SCOP 8038527 SCOP 8038557 SCOP 8070111 SCOP 8070121 SCOP 8072399 SCOP 8038977 RCSB 1CA0 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.
1CA0, 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.
178 distinct constructs across 380 entries. 364 polymer entities differ from the UniProt canonical sequence in some way, 6 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 |
|---|---|---|---|---|
| 53 | 40 | 1.50 | 3IFN | residues 672-711 |
| 42 | 42 | 2.50 | 7Q4B | residues 672-713 |
| 42 | 58 | 1.00 | 5PTI | residues 36-93 |
| 8 | 770 | 3.00 | 8KF4 | matches the canonical sequence |
| 5 | 36 | 3.20 | 9FH1 | residues 672-713; 1 internal deletion |
| 5 | 58 | 1.30 | 4Y11 | residues 36-93 |
| 5 | 59 | 0.85 | 2FMA | residues 131-189; D131E, K132A |
| 5 | 65 | 1.55 | 1F7Z | residues 36-100 |
| 4 | 28 | 1.59 | 3BAE | residues 672-699 |
| 4 | 34 | 2.60 | 9CZN | residues 680-713 |
| 4 | 40 | 3.10 | 9UMH | residues 672-711; D678N |
| 4 | 42 | 2.80 | 8BFZ | residues 672-713; E693G |
| 4 | 58 | 0.95 | 1KTH | residues 3108-3165 |
| 3 | 42 | 3.30 | 8OLN | residues 672-713; E693Q, D694N |
| 3 | 58 | 0.86 | 1G6X | residues 36-93; T46A, P48A, K50R +1 more |
| 3 | 58 | 1.65 | 1P2I | residues 36-93; K50G, M87L |
| 3 | 59 | 1.63 | 3BYB | residues 25-83 |
| 3 | 71 | 1.75 | 35UI | residues 116-180; 6-residue insertion after 177 |
| 3 | 211 | 2.00 | 3UMH | residues 369-579; A369M, V576I, L577E +2 more |
| 3 | 214 | 2.20 | 3Q7L | residues 281-494; V281G, G282S, K283H +1 more |
| 2 | 40 | 1.99 | 8BG0 | residues 672-711; E693G |
| 2 | 43 | residues 684-726; H684G, H685S | ||
| 2 | 55 | 2.10 | 4WXV | residues 36-90 |
| 2 | 58 | 1.35 | 1P2J | residues 36-93; K50L, M87L |
| 2 | 58 | 1.37 | 4Y0Z | residues 36-93; K50A |
Showing the 25 most-used of 178.
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 | 122 | 32.1% |
| monomeric | 1 | 99 | 26.1% |
| decameric | 10 | 39 | 10.3% |
| trimeric | 3 | 24 | 6.3% |
| dodecameric | 12 | 19 | 5.0% |
| hexameric | 6 | 18 | 4.7% |
| pentameric | 5 | 12 | 3.2% |
| tetrameric | 4 | 11 | 2.9% |
181 entries have the depositor's assembly corroborated by PISA, 185 carry the depositor's word alone and 12 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 39 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1CBW, 1G6X, 1MTN, 1P2J, 1P2M, 1P2N, 1P2O, 1P2Q, 1T7C, 1T8L, 1T8M, 1T8N, 1T8O, 1TPA, 2FI3, 2FI4, 2FI5, 2FTL, 2FTM, 2HEX.
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 |
|---|---|---|---|
| Amyloidogenic glycoprotein, heparin-binding domain | CATH 3.90.570.10 | 29–124 | 7 |
| Amyloidogenic glycoprotein, copper-binding domain | CATH 3.30.1490.140 | 131–189 | 10 |
| Pancreatic trypsin inhibitor Kunitz domain | CATH 4.10.410.10 | 289–346 | 101 |
| Amyloid precursor protein, E2 domain | CATH 1.20.120.770 | 384–578 | 16 |
| Trypsin-like serine proteases | CATH 2.40.10.10 | 391–498 | 18 |
| Immunoglobulins | CATH 2.60.40.10 | 598–723 | 10 |
| Amyloidogenic glycoprotein, amyloid-beta peptide | CATH 4.10.230.10 | 672–713 | 4 |
| Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) | CATH 2.30.29.30 | 749–770 | 3 |
| A heparin-binding domain | SCOP2B 8037154 | 29–124 | 4 |
| Amyloid beta a4 protein copper binding domain (domain 2) | SCOP2B 8041099 | 133–189 | 8 |
| BPTI-like | SCOP2B 8038485 | 289–346 | 56 |
| BPTI-like | SCOP2B 8038452 | 289–346 | 3 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| SO4 | ion | Sulfate Ion | 83 | 0.86 |
| CA | ion | Calcium Ion | 63 | 1.18 |
| GOL | cryoprotectant | Glycerol | 23 | 0.85 |
| PO4 | ion | Phosphate Ion | 14 | 0.95 |
| EDO | cryoprotectant | 1,2-Ethanediol | 12 | 0.86 |
| ZN | ion | Zinc Ion | 11 | 2.20 |
| NAG | cofactor | 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose | 9 | 1.65 |
| ACT | cryoprotectant | Acetate Ion | 8 | 1.70 |
| NA | ion | Sodium Ion | 6 | 1.58 |
| CU | ion | Copper (Ii) Ion | 6 | 1.60 |
| PG4 | cryoprotectant | Tetraethylene Glycol | 5 | 1.46 |
| CL | ion | Chloride Ion | 4 | 1.06 |
| CD | ion | Cadmium Ion | 4 | 2.00 |
| PC1 | lipid/detergent | 1,2-Diacyl-Sn-Glycero-3-Phosphocholine | 4 | 2.60 |
| CLR | lipid/detergent | Cholesterol | 4 | 2.60 |
| VAL | ligand | Valine | 3 | 1.90 |
| PGE | cryoprotectant | Triethylene Glycol | 3 | 1.80 |
| GSH | ligand | Glutathione | 3 | 2.01 |
| MG | ion | Magnesium Ion | 3 | 2.20 |
| UNX | ion | Unknown Atom Or Ion | 3 | 1.00 |
Parsed from the free text 149 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 166
entries that recorded anything at all.
Median pH 7.5
(range 3.3 to 9.0).
374 entries carry a wwPDB validation report: 191 clean, 83 worth a check and 100 with something to explain. Median clashscore 6.17, median RSRZ outliers 2.86%, median R-free minus R-work 0.035. 345 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 214 | 0.85 | 16 | 100% |
| Bos taurus | 109 | 0.86 | 4 | 7% |
| Unknown | 10 | 1.00 | 1 | 17% |
| Mus musculus | 10 | 2.20 | 1 | 61% |
| Dendroaspis angusticeps | 5 | 1.06 | 0 | 7% |
| Stichodactyla helianthus | 5 | 1.70 | 0 | 7% |
| Pseudonaja textilis textilis | 4 | 1.63 | 1 | 7% |
| Macaca fascicularis | 3 | 1.75 | 0 | 7% |
| Caenorhabditis elegans | 3 | 2.70 | 1 | 30% |
| Gallus gallus | 2 | 2.05 | 0 | 24% |
| Danio rerio | 2 | 2.46 | 0 | 23% |
| Equus caballus | 1 | 2.00 | 0 | 6% |
770 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 | Discovery and optimization of marstacimab, a human monoclonal antibody targeting tissue factor pathway inhibitor for the treatment of hemophilia A and B. Mabs doi:10.1080/19420862.2026.2685362 |
| 2026 | Distinct amyloid-beta filament fold in individuals with APP Flemish mutation. Nat.Struct.Mol.Biol. doi:10.1038/s41594-026-01855-y |
| 2026 | Polymorphic structures of rapidly twisting 40-residue amyloid-beta fibrils. Biorxiv doi:10.64898/2026.04.10.717728 |
| 2026 | De novo design of metalloproteases for targeted amyloid-beta cleavage Vita doi:10.15302/vita.2026.07.0055 |
| 2026 | High-resolution structure of monomorphic A beta 1-40 fibrils. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2603575123 |
| 2025 | Inactive structures of the vasopressin V2 receptor reveal distinct binding modes for Tolvaptan and Mambaquaretin toxin. Nat Commun doi:10.1038/s41467-025-59114-5 |
| 2025 | Impacts of D-aspartate on the Aggregation Kinetics and Structural Polymorphism of Amyloid beta Peptide 1-42. J.Mol.Biol. doi:10.1016/j.jmb.2025.169092 |
| 2025 | An O-glycopeptide participates in the formation of distinct A beta 42 fibril structures and attenuates A beta 42 neurotoxicity. Nat Commun doi:10.1038/s41467-025-60978-w |
| 2025 | Anle138b binds predominantly to the central cavity in lipidic A beta 40 fibrils and modulates fibril formation. Nat Commun doi:10.1038/s41467-025-64443-6 |
| 2025 | Microgravity-Assisted Exploration of the Conformational Space of Amyloid beta Affected by Tottori-Type Familial Mutation D7N. Acs Chem Neurosci doi:10.1021/acschemneuro.5c00217 |
| 2025 | Cryo-EM studies of amyloid-beta fibrils from human and murine brains carrying the Uppsala APP mutation ( Delta 690-695). Acta Neuropathol Commun doi:10.1186/s40478-025-02120-x |
| 2025 | Elucidating the Unique J-Shaped Protomer Structure of Amyloid-beta (1-40) Fibril with Cryo-Electron Microscopy. Int J Mol Sci doi:10.3390/ijms26031179 |
| 2025 | Cryo-EM structure of the tissue factor/factor VIIa complex with a factor X mimetic reveals a novel allosteric mechanism. Blood doi:10.1182/blood.2025029430 |
| 2025 | Collagen VI microfibril structure reveals mechanism for molecular assembly and clustering of inherited pathogenic mutations. Nat Commun doi:10.1038/s41467-025-62923-3 |
| 2025 | Transient interactions between the fuzzy coat and the cross-beta core of brain-derived amyloid-beta 42 filaments Sci Adv doi:10.1126/sciadv.adr7008 |
| 2024 | Fusion of amyloid beta with ferritin yields an isolated oligomeric beta-sheet-rich aggregate inside the ferritin cage. Biomater Sci doi:10.1039/d4bm00173g |
| 2024 | E22G A beta 40 fibril structure and kinetics illuminate how A beta 40 rather than A beta 42 triggers familial Alzheimer's. Nat Commun doi:10.1038/s41467-024-51294-w |
| 2024 | Cryo-EM structures of cotton wool plaques' amyloid beta and of tau filaments in dominantly inherited Alzheimer disease. Acta Neuropathol doi:10.1007/s00401-024-02786-y |
| 2024 | An electrostatic cluster guides A beta 40 fibril formation in sporadic and Dutch-type cerebral amyloid angiopathy. J.Struct.Biol. doi:10.1016/j.jsb.2024.108092 |
| 2024 | Cryo-EM structures of lipidic fibrils of amyloid-beta (1-40). Nat Commun doi:10.1038/s41467-023-43822-x |
| 2024 | Molecular mechanism of substrate recognition and cleavage by human gamma-secretase. Science doi:10.1126/science.adn5820 |
| 2024 | Cryo-EM structures of amyloid-beta and tau filaments in Down syndrome. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01252-3 |
| 2024 | Sea Anemone Kunitz Peptide HCIQ2c1: Structure, Modulation of TRPA1 Channel, and Suppression of Nociceptive Reaction In Vivo. Mar Drugs doi:10.3390/md22120542 |
| 2023 | Cryo-EM structures of amyloid-beta filaments with the Arctic mutation (E22G) from human and mouse brains. Acta Neuropathol doi:10.1007/s00401-022-02533-1 |
| 2023 | Cryo-EM structures of A beta 40 filaments from the leptomeninges of individuals with Alzheimer's disease and cerebral amyloid angiopathy. Acta Neuropathol Commun doi:10.1186/s40478-023-01694-8 |
| 2023 | Cryo-EM Analysis of the Effect of Seeding with Brain-derived A beta Amyloid Fibrils. J.Mol.Biol. doi:10.1016/j.jmb.2023.168422 |
| 2023 | Structures of brain-derived 42-residue amyloid-beta fibril polymorphs with unusual molecular conformations and intermolecular interactions. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2218831120 |
| 2023 | Abundant A beta fibrils in ultracentrifugal supernatants of aqueous extracts from Alzheimer's disease brains. Neuron doi:10.1016/j.neuron.2023.04.007 |
| 2023 | The in-tissue molecular architecture of beta-amyloid pathology in the mammalian brain. Nat Commun doi:10.1038/s41467-023-38495-5 |
| 2023 | Cryo-EM of A beta fibrils from mouse models find tg-APP ArcSwe fibrils resemble those found in patients with sporadic Alzheimer's disease. Nat.Neurosci. doi:10.1038/s41593-023-01484-4 |
| 2023 | Tau filaments from amyotrophic lateral sclerosis/parkinsonism-dementia complex adopt the CTE fold. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2306767120 |
| 2023 | The Double-Layered Structure of Amyloid-beta Assemblage on GM1-Containing Membranes Catalytically Promotes Fibrillization. Acs Chem Neurosci doi:10.1021/acschemneuro.3c00192 |
| 2022 | Water Network in the Binding Pocket of Fluorinated BPTI-Trypsin Complexes─Insights from Simulation and Experiment. J.Phys.Chem.B doi:10.1021/acs.jpcb.2c05496 |
| 2022 | Fluorine-induced polarity increases inhibitory activity of BPTI towards chymotrypsin. Rsc Chem Biol doi:10.1039/d2cb00018k |
| 2022 | Cryo-EM structures of amyloid-beta 42 filaments from human brains. Science doi:10.1126/science.abm7285 |
| 2022 | Structural basis of FPR2 in recognition of A beta 42 and neuroprotection by humanin. Nat Commun doi:10.1038/s41467-022-29361-x |
| 2022 | TFPI is a colonic crypt receptor for TcdB from hypervirulent clade 2 C. difficile. Cell doi:10.1016/j.cell.2022.02.010 |
| 2022 | Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition. Nat Commun doi:10.1038/s41467-022-29322-4 |
| 2022 | Molecular Structure of Cu(II)-Bound Amyloid-beta Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer's Disease. Jacs Au doi:10.1021/jacsau.2c00438 |
| 2021 | Members of the vertebrate contactin and amyloid precursor protein families interact through a conserved interface. J.Biol.Chem. doi:10.1016/j.jbc.2021.101541 |