CODSWALLOP

Ferritin heavy chain

Homo sapiens · seed P02794 · 183 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026

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.

586Entries 594Entities 245Constructs 34Organisms 85Ligand-bound
1.06 ÅBest res.
1.91 ÅMedian res.

Every figure here is counted over the whole family rather than quoted from one entry.

The reference structure

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.

Rendered structure of 9JQD
9JQD at the RCSB · open it in the 3D viewer

Which residues anyone has ever seen

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.

191183594 constructs

Constructs, most-used first

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.

EntitiesLengthBest (Å)Best entryWhat 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.

Positions people deliberately mutate

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".

H106V 69% N99D 67% N140D 66% A145L 66% T6S 66% S164A 65% F82L 65% N110S 65% Q15T 63% D90S 62% R157Q 62% K87Q 62% I134L 62% Y40F 62% H58E 62% L73M 61% M159L 61% S179D 61% S39G 61% D93E 60% E95G 60% S17V 60% N126A 60% E148K 60% T123S 59% L57R 59% K50E 59% A167G 59% L149M 59% V153L 58%

What it assembles into

Oligomeric stateChainsEntriesShare
24-meric24 554 94.5%
dimeric2 12 2.0%
48-meric48 7 1.2%
octameric8 3 0.5%
monomeric1 3 0.5%
26-meric26 2 0.3%
trimeric3 2 0.3%
hexadecameric16 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.

Domain architecture

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.

CATHFerritin, core subunit, foSCOP2BFerritin-likeFerritin-likeFerritin-likeFerritin-likeFerritin-likeFerritin-likeFerritin-likeFerritin-likeFerritin-likeFerritin-like191183
DomainSourceSpan (seed)Chains
Ferritin, core subunit, four-helix bundleCATH 1.20.1260.10 8–177 337
Ferritin-likeSCOP2B 8038756 6–177 150
Ferritin-likeSCOP2B 8063904 7–177 27
Ferritin-likeSCOP2B 8063908 7–176 22
Ferritin-likeSCOP2B 8063930 7–162 8
Ferritin-likeSCOP2B 8037855 8–177 116
Ferritin-likeSCOP2B 8038642 9–178 23
Ferritin-likeSCOP2B 8063914 16–180 47
Ferritin-likeSCOP2B 8041472 20–183 23
Ferritin-likeSCOP2B 8063912 23–177 16
Ferritin-likeSCOP2B 8033038 27–183 5

What binds it

PLL PLL11 entries LFA LFA8 entries BET BET5 entries V9Y V9Y4 entries PEO PEO4 entries A1L52 A1L524 entries RFT RFT3 entries A1JGJ A1JGJ3 entries CC9 CC93 entries DIE DIE2 entries 2MY 2MY2 entries 4LF 4LF2 entries
ComponentClassNameEntriesBest (Å)
CDion Cadmium Ion 184 1.15
FEion Fe (Iii) Ion 180 1.06
CLion Chloride Ion 176 1.10
MGion Magnesium Ion 155 1.10
SO4ion Sulfate Ion 143 1.15
EDOcryoprotectant 1,2-Ethanediol 72 1.16
GOLcryoprotectant Glycerol 60 1.15
CAion Calcium Ion 45 1.06
NAion Sodium Ion 44 1.15
ZNion Zinc Ion 37 1.09
FE2ion Fe (Ii) Ion 35 1.10
AUion Gold Ion 25 1.17
NIion Nickel (Ii) Ion 14 1.70
PDion Palladium Ion 12 1.53
PLLligand Palladium(Ii) Allyl Complex 11 1.48
OXYsolvent Oxygen Molecule 11 1.34
CUion Copper (Ii) Ion 10 1.73
LFAligand Eicosane 8 1.76
Oion Oxygen Atom 8 2.02
COion Cobalt (Ii) Ion 7 1.35

How it crystallises

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).

Precipitants

Ammonium sulfate × Magnesium chloride × Sodium chloride × PEG × Calcium chloride × MPD × Isopropanol × Sodium formate × Sodium citrate × Lithium sulfate × Jeffamine × Dioxane × PEG (unspecified) × Ethanol ×

Buffers

Tris × HEPES × Sodium acetate × MES × Imidazole × CHES × Citrate × Sodium cacodylate × Phosphate × Bis-Tris × CAPS ×

Which entries to trust

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.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Homo sapiens209 1.06 31 100%
Equus caballus173 1.15 40 93%
Aquarana catesbeiana54 1.10 5 94%
Mus musculus31 1.09 0 100%
Penaeus japonicus23 1.16 0 91%
Pseudo-nitzschia multiseries16 1.65 0 70%
Thermotoga maritima MSB816 1.76 8 76%
Thermotoga maritima8 1.84 0 76%
Asterias forbesi6 1.91 0 93%
Azumapecten farreri5 2.03 1 93%
Tegillarca granosa4 1.78 0 92%
Glycine max4 1.80 0 94%

Seed sequence

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

1MTTASTSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS
61HEEREHAEKL MKLQNQRGGR IFLQDIKKPD CDDWESGLNA MECALHLEKN VNQSLLELHK
121LATDKNDPHL CDFIETHYLN EQVKAIKELG DHVTNLRKMG APESGLAEYL FDKHTLGDSD
181NES

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.

Primary citations

One record per paper, not per entry.

YearCitation
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