Homo sapiens · seed P02794 · 183 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P02794 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 1.20.1260.10 SCOP 8038756 SCOP 8063904 SCOP 8063908 SCOP 8063930 SCOP 8037855 SCOP 8038642 SCOP 8063914 SCOP 8041472 SCOP 8063912 SCOP 8033038 RCSB 9JQD 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.
9JQD, 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.
245 distinct constructs across 586 entries. 512 polymer entities differ from the UniProt canonical sequence in some way, 12 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 |
|---|---|---|---|---|
| 84 | 174 | 1.24 | 8B7L | residues 2-175 |
| 19 | 182 | 1.38 | 9RGH | residues 2-183 |
| 15 | 176 | 1.16 | 4LQH | matches the canonical sequence |
| 13 | 172 | 1.27 | 7RRP | residues 6-177 |
| 13 | 182 | 1.24 | 22FX | matches the canonical sequence |
| 13 | 183 | 1.34 | 4Y08 | matches the canonical sequence |
| 12 | 182 | 1.79 | 5UP7 | residues 2-183; K87Q, C91E, C103A +2 more |
| 12 | 183 | 1.15 | 7A6A | K87Q |
| 11 | 183 | 1.16 | 7O63 | residues 60-242; G60M |
| 9 | 168 | 1.65 | 4IWK | residues 62-229; P62G |
| 9 | 182 | 1.90 | 9VOF | residues 2-183; E28A, Y35A, Y55A +14 more |
| 8 | 173 | 1.58 | 7R5O | residues 5-177; K87Q |
| 7 | 172 | 1.09 | 8RQB | residues 6-177 |
| 6 | 174 | 1.50 | 7VIO | residues 2-175; R169H, L170C |
| 6 | 183 | 1.55 | 8PP3 | A19K, N26R, K87Q +7 more |
| 5 | 164 | 2.01 | 6TXN | matches the canonical sequence |
| 5 | 170 | 1.60 | 6LS2 | T158H |
| 5 | 170 | 2.00 | 6KH0 | residues 2-170; 1-residue insertion after 157; T158H |
| 5 | 173 | 1.89 | 9SJV | residues 5-177; N140S |
| 5 | 174 | 1.65 | 2Z5P | residues 2-175; L94P |
| 5 | 174 | 2.10 | 2FG4 | residues 2-175 |
| 5 | 176 | 1.10 | 5J93 | E58A, E137A, D141A |
| 4 | 169 | 1.16 | 6A4U | residues 2-170; Q88R |
| 4 | 171 | 2.03 | 8W95 | H11K, H122E |
| 4 | 172 | 1.78 | 6L55 | matches the canonical sequence |
Showing the 25 most-used of 245.
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 |
|---|---|---|---|
| 24-meric | 24 | 554 | 94.5% |
| dimeric | 2 | 12 | 2.0% |
| 48-meric | 48 | 7 | 1.2% |
| octameric | 8 | 3 | 0.5% |
| monomeric | 1 | 3 | 0.5% |
| 26-meric | 26 | 2 | 0.3% |
| trimeric | 3 | 2 | 0.3% |
| hexadecameric | 16 | 1 | 0.2% |
454 entries have the depositor's assembly corroborated by PISA, 126 carry the depositor's word alone and 6 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 1 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1Z4A.
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 |
|---|---|---|---|
| Ferritin, core subunit, four-helix bundle | CATH 1.20.1260.10 | 8–177 | 337 |
| Ferritin-like | SCOP2B 8038756 | 6–177 | 150 |
| Ferritin-like | SCOP2B 8063904 | 7–177 | 27 |
| Ferritin-like | SCOP2B 8063908 | 7–176 | 22 |
| Ferritin-like | SCOP2B 8063930 | 7–162 | 8 |
| Ferritin-like | SCOP2B 8037855 | 8–177 | 116 |
| Ferritin-like | SCOP2B 8038642 | 9–178 | 23 |
| Ferritin-like | SCOP2B 8063914 | 16–180 | 47 |
| Ferritin-like | SCOP2B 8041472 | 20–183 | 23 |
| Ferritin-like | SCOP2B 8063912 | 23–177 | 16 |
| Ferritin-like | SCOP2B 8033038 | 27–183 | 5 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| CD | ion | Cadmium Ion | 184 | 1.15 |
| FE | ion | Fe (Iii) Ion | 180 | 1.06 |
| CL | ion | Chloride Ion | 176 | 1.10 |
| MG | ion | Magnesium Ion | 155 | 1.10 |
| SO4 | ion | Sulfate Ion | 143 | 1.15 |
| EDO | cryoprotectant | 1,2-Ethanediol | 72 | 1.16 |
| GOL | cryoprotectant | Glycerol | 60 | 1.15 |
| CA | ion | Calcium Ion | 45 | 1.06 |
| NA | ion | Sodium Ion | 44 | 1.15 |
| ZN | ion | Zinc Ion | 37 | 1.09 |
| FE2 | ion | Fe (Ii) Ion | 35 | 1.10 |
| AU | ion | Gold Ion | 25 | 1.17 |
| NI | ion | Nickel (Ii) Ion | 14 | 1.70 |
| PD | ion | Palladium Ion | 12 | 1.53 |
| PLL | ligand | Palladium(Ii) Allyl Complex | 11 | 1.48 |
| OXY | solvent | Oxygen Molecule | 11 | 1.34 |
| CU | ion | Copper (Ii) Ion | 10 | 1.73 |
| LFA | ligand | Eicosane | 8 | 1.76 |
| O | ion | Oxygen Atom | 8 | 2.02 |
| CO | ion | Cobalt (Ii) Ion | 7 | 1.35 |
Parsed from the free text 480 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 487
entries that recorded anything at all.
Median pH 8.0
(range 4.5 to 9.5).
586 entries carry a wwPDB validation report: 358 clean, 158 worth a check and 70 with something to explain. Median clashscore 4.32, median RSRZ outliers 3.51%, median R-free minus R-work 0.032. 570 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 209 | 1.06 | 31 | 100% |
| Equus caballus | 173 | 1.15 | 40 | 93% |
| Aquarana catesbeiana | 54 | 1.10 | 5 | 94% |
| Mus musculus | 31 | 1.09 | 0 | 100% |
| Penaeus japonicus | 23 | 1.16 | 0 | 91% |
| Pseudo-nitzschia multiseries | 16 | 1.65 | 0 | 70% |
| Thermotoga maritima MSB8 | 16 | 1.76 | 8 | 76% |
| Thermotoga maritima | 8 | 1.84 | 0 | 76% |
| Asterias forbesi | 6 | 1.91 | 0 | 93% |
| Azumapecten farreri | 5 | 2.03 | 1 | 93% |
| Tegillarca granosa | 4 | 1.78 | 0 | 92% |
| Glycine max | 4 | 1.80 | 0 | 94% |
183 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 | Atomic resolution cryo-EM at 200 keV. Iucrj doi:10.1107/S2052252526004100 |
| 2026 | Gradual Modification of Ferritin 4-Fold Pore Promotes Cage Instability, Fe 2+ Exit, and Iron-Induced Protein Precipitation. Biochemistry doi:10.1021/acs.biochem.5c00744 |
| 2026 | Ferritin iron uptake and oxidation are dynamically modulated by nucleotide phosphate architecture via electrostatic gating. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2026.151118 |
| 2026 | Design of a flexible aromatic gate to immobilize C 60 in a ferritin cage. Chem.Commun.(Camb.) doi:10.1039/d6cc02237e |
| 2026 | Granzyme B-mimetic nanozyme for nanovesicle targeted anticancer applications. Nat Commun doi:10.1038/s41467-026-68773-x |
| 2026 | Impact of the three-fold channel substitution D131N on kinetics of translocation of Fe 2+ across the protein coat is more severe for human cytosolic H-chain ferritin than for human mitochondrial ferritin. Dalton Trans doi:10.1039/d5dt02739j |
| 2026 | Ferritin Iron Mineralisation: Route of Fe 3+ Transfer From the Ferroxidase Centre to the Inner Cavity of Human H-Chain Ferritin. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.1203843 |
| 2026 | Post-acquisition super resolution for cryo-electron microscopy. Iucrj doi:10.1107/S2052252526005348 |
| 2026 | Direct evidence of acid-driven protein desolvation. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2525949123 |
| 2026 | Redesign of the Ferritin Ferroxidase Center for Universal Molecular Binding or Specific Recognition. Small doi:10.1002/smll.73922 |
| 2026 | Subtomogram averaging by cryo electron tomography using CRYO ARMTM 300 II for purified and cellular samples AIMS Biophysics doi:10.3934/biophy.2026008 |
| 2026 | Separating the effects of temperature and absorbed X-ray dose on unit-cell volume. Acta Crystallogr D Struct Biol doi:10.1107/S2059798326008612 |
| 2026 | Identification, functional characterization, and cryo-EM structural analysis of novel ferritin subunits in Turbo sazae. Febs J. doi:10.1111/febs.70601 |
| 2025 | Observation of the Assembly of the Nascent Mineral Core at the Nucleation Site of Human Mitochondrial Ferritin. J.Am.Chem.Soc. doi:10.1021/jacs.5c01337 |
| 2025 | Spherical mixed-valence pentadecavanadate binding to human H-chain ferritin Inorg Chem Front doi:10.1039/D5QI01694K |
| 2025 | An Artificial Metal-Free Peroxidase Designed Using a Ferritin Cage for Bioinspired Catalysis. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202504608 |
| 2025 | Design of Aromatic Interaction Networks in a Protein Cage Modulated by Fluorescent Ligand Binding. Adv Sci doi:10.1002/advs.202417030 |
| 2025 | Structural Insight Into a Human H Ferritin@Gold-Monocarbene Adduct: Aurophilicity Revealed in a Biological Context. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202503778 |
| 2025 | Bioengineered protein nanocarrier facilitating siRNA escape from lysosomes for targeted RNAi therapy in glioblastoma. Sci Adv doi:10.1126/sciadv.adr9266 |
| 2025 | Observation of the Protein-Inorganic Interface of Ferritin by Cryo-Electron Microscopy. J.Am.Chem.Soc. doi:10.1021/jacs.4c13873 |
| 2025 | Construction of An Artificial Photosynthesis System with A Single CdS QDs-Ferritin Hybrid Molecule. Small Methods doi:10.1002/smtd.202400915 |
| 2025 | Photoinduced NO release of [Fe2( mu-SL)2(NO)4] complexes and their protein adducts: insights from structure, cytotoxicity, and photodynamic studies Inorg Chem Front doi:10.1039/D5QI00255A |
| 2025 | Processing of Freestanding Single Supercrystal Assembled by Atomically Precise Protein-Decorated Nanoparticles. Nano Lett. doi:10.1021/acs.nanolett.5c01619 |
| 2025 | A large, general and modular DARPin-apoferritin scaffold enables the visualization of small proteins by cryo-EM. Iucrj doi:10.1107/S2052252525003021 |
| 2024 | Low-dose cryo-electron ptychography of proteins at sub-nanometer resolution. Nat Commun doi:10.1038/s41467-024-52403-5 |
| 2024 | Assembly Requirements for the Construction of Large-Scale Binary Protein Structures. Biomacromolecules doi:10.1021/acs.biomac.3c00891 |
| 2024 | Insight into the photodynamic mechanism and protein binding of a nitrosyl iron-sulfur [Fe 2 S 2 (NO) 4 ] 2- cluster. Spectrochim Acta A Mol Biomol Spectrosc doi:10.1016/j.saa.2024.124603 |
| 2024 | Site-Specific Histidine Aza-Michael Addition in Proteins Enabled by a Ferritin-Based Metalloenzyme. J.Am.Chem.Soc. doi:10.1021/jacs.4c14446 |
| 2024 | Structure-Guided Design of Ferritin-Platinum Prodrugs for Targeted Therapy of Esophageal Squamous Cell Carcinoma. Acs Nano doi:10.1021/acsnano.4c00212 |
| 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 | Engineered protein cages with enhanced extracellular drug release for elevated antitumor efficacy. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2024.131492 |
| 2024 | Self-assembling nanoparticle engineered from the ferritinophagy complex as a rabies virus vaccine candidate. Nat Commun doi:10.1038/s41467-024-52908-z |
| 2024 | Structural Insights into the Reaction between Hydrogen Peroxide and Di-iron Complexes at the Ferroxidase Center of Ferritin. Inorg.Chem. doi:10.1021/acs.inorgchem.3c03889 |
| 2024 | Structural basis for the intracellular regulation of ferritin degradation. Nat Commun doi:10.1038/s41467-024-48151-1 |
| 2023 | Measurement of charges and chemical bonding in a cryo-EM structure. Commun Chem doi:10.1038/s42004-023-00900-x |
| 2023 | Biochemical Characterization of Caenorhabditis elegans Ferritins. Biochemistry doi:10.1021/acs.biochem.3c00005 |
| 2023 | Elucidating Conformational Dynamics and Thermostability of Designed Aromatic Clusters by Using Protein Cages. Chemistry doi:10.1002/chem.202300488 |
| 2023 | Atomic-level insights into a unique semi-clathrate hydrate formed in a confined environment of porous protein crystal. Cryst.Growth Des. doi:10.1021/acs.cgd.3c00880 |
| 2023 | A new and efficient procedure to load bioactive molecules within the human heavy-chain ferritin nanocage. Front Mol Biosci doi:10.3389/fmolb.2023.1008985 |
| 2023 | Characterizing the resolution and throughput of the Apollo direct electron detector. J Struct Biol X doi:10.1016/j.yjsbx.2022.100080 |