CODSWALLOP

Histone H3.1

Homo sapiens · seed P68431 · 136 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.

1,185Entries 1,207Entities 203Constructs 25Organisms 266Ligand-bound
1.40 ÅBest res.
3.30 ÅMedian res.

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

The reference structure

8OOP, 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 8OOP
8OOP 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.

1681361170 constructs

Constructs, most-used first

203 distinct constructs across 1,185 entries. 753 polymer entities differ from the UniProt canonical sequence in some way, 15 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
174 135 1.94 1KX5 residues 2-136; G103A
108 139 1.89 7VZ4 matches the canonical sequence
106 136 2.48 8VG1 matches the canonical sequence
79 136 2.42 8RUP G103A
65 136 1.90 1TZY matches the canonical sequence
52 135 2.70 8OOP residues 2-136
34 135 2.30 7TN2 residues 2-136; G103A, C111A
34 135 2.36 8JLB residues 2-136; C111A
30 139 2.18 5X7X matches the canonical sequence
28 136 3.20 6T79 C111A
24 140 2.91 7LYA matches the canonical sequence
20 136 2.80 7Z0O matches the canonical sequence
18 135 2.30 2NQB residues 2-136
17 136 2.50 6ZHX G103A, C111A
17 136 2.50 8PKJ matches the canonical sequence
17 140 2.44 7R5R matches the canonical sequence
14 136 2.75 9K3Z matches the canonical sequence
12 98 1.99 6IPU residues 39-136
12 99 2.79 9GEO residues 38-136; G103A
9 136 2.90 9EGX K37M
9 157 3.10 9MLR His6; TEV site
6 79 1.80 7CIZ residues 58-136
6 98 2.98 9LJ2 residues 38-135
6 99 2.50 9D3P residues 38-136
6 135 2.30 1P3I residues 2-136; G35E, V36S, G103A

Showing the 25 most-used of 203.

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".

C97S 69% G103A 42% C111A 20% M91G 16% V90I 14% A32S 14% S88A 12% M121F 7% A136S 7% R54K 6% Y55F 6% K37S 6% K80T 5% V36S 5% G35A 5% D78K 5% A112T 5% A76C 5% Q77V 5% E60H 5% Y42R 5% F85W 5% I125V 5% T23S 4% Q69S 4% I113L 4% K5M 4% S29R 4% T33L 4% K38H 4%

What it assembles into

Oligomeric stateChainsEntriesShare
decameric10 332 28.0%
undecameric11 207 17.5%
dodecameric12 145 12.2%
tetradecameric14 71 6.0%
20-meric20 42 3.5%
tridecameric13 41 3.5%
hexadecameric16 25 2.1%
dimeric2 23 1.9%

564 entries have the depositor's assembly corroborated by PISA, 610 carry the depositor's word alone and 4 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 11 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 2HUE, 3TU4, 4H9P, 4H9Q, 4H9R, 4H9S, 4J8V, 4J8X, 5NL0, 7VCQ, 7XVL.

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.

CATHHistone, subunit ASCOP2BCore histone-likeCore histone-likeCore histone-likeCore histone-likeCore histone-likeCore histone-likeCore histone-likeCore histone-like168136
DomainSourceSpan (seed)Chains
Histone, subunit ACATH 1.10.20.10 42–136 216
Core histone-likeSCOP2B 8042439 24–102 14
Core histone-likeSCOP2B 8041272 39–135 203
Core histone-likeSCOP2B 8096712 39–135 41
Core histone-likeSCOP2B 8036585 39–135 19
Core histone-likeSCOP2B 8070527 40–136 20
Core histone-likeSCOP2B 8039340 42–136 256
Core histone-likeSCOP2B 8070531 42–135 114
Core histone-likeSCOP2B 8070539 94–136 27

What binds it

ADP ADP104 entries SAH SAH38 entries ATP ATP23 entries SAM SAM23 entries SF4 SF412 entries AGS AGS12 entries NAG NAG9 entries PTD PTD7 entries OGA OGA6 entries HEM HEM6 entries AMP AMP5 entries FAD FAD5 entries
ComponentClassNameEntriesBest (Å)
ZNion Zinc Ion 286 1.40
MGion Magnesium Ion 170 2.17
ADPcofactor Adenosine-5'-Diphosphate 104 2.50
MNion Manganese (Ii) Ion 97 1.94
CLion Chloride Ion 78 1.80
BEFion Beryllium Trifluoride Ion 43 2.80
SO4ion Sulfate Ion 41 1.55
SAHcofactor S-Adenosyl-L-Homocysteine 38 2.39
ATPcofactor Adenosine-5'-Triphosphate 23 2.30
SAMcofactor S-Adenosylmethionine 23 2.57
CAion Calcium Ion 17 2.11
Kion Potassium Ion 16 2.20
PO4ion Phosphate Ion 14 1.90
SF4ligand Iron/sulfur Cluster 12 3.10
AGScofactor Phosphothiophosphoric Acid-Adenylate Ester 12 3.00
GOLcryoprotectant Glycerol 11 1.70
NAGcofactor 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose 9 2.89
PTDligand Pentanedial 7 3.05
OGAligand N-Oxalylglycine 6 1.80
HEMcofactor Protoporphyrin Ix Containing Fe 6 2.89

How it crystallises

Parsed from the free text 269 depositors typed into _exptl_crystal_grow.pdbx_details, out of 273 entries that recorded anything at all. Median pH 6.0 (range 3.8 to 8.8).

Precipitants

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

Buffers

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

Which entries to trust

1,173 entries carry a wwPDB validation report: 875 clean, 155 worth a check and 143 with something to explain. Median clashscore 7.51, median RSRZ outliers 2.31%, median R-free minus R-work 0.045. 1,151 have released structure factors.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Homo sapiens618 1.40 66 100%
Xenopus laevis432 1.70 166 100%
Saccharomyces cerevisiae25 2.80 6 100%
Drosophila melanogaster24 2.10 1 100%
Arabidopsis thaliana20 2.71 5 100%
Saccharomyces cerevisiae S288C17 2.70 9 100%
Mus musculus11 2.34 1 100%
Gallus gallus10 1.90 0 100%
Unknown5 1.80 4 100%
Xenopus3 2.74 0 100%
Schizosaccharomyces pombe 972h-2 2.99 0 68%
Caenorhabditis elegans2 2.30 2 24%

Seed sequence

136 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

1MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
61LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI
121MPKDIQLARR IRGERA

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 High-Yield Production of Modified DNA Enables Structural Analysis of PARP2 Recognition of Nucleosomal Single-Strand Breaks. J.Mol.Biol. doi:10.1016/j.jmb.2026.169753
2026 8oxoG:A Is Structurally Accommodated in the Nucleosome Core Particle, Yet Inaccessible to MUTYH-Initiated DNA Repair. Biomolecules doi:10.3390/biom16070999
2026 Molecular basis of nick ligation in the nucleosome by DNA Ligase III alpha Nat Commun doi:10.1038/s41467-026-77207-7
2026 Distinct associations of pioneer factor Ascl1-E12a with nucleosomes drive changes in cell fate. Mol.Cell doi:10.1016/j.molcel.2026.05.020
2026 Cryo-EM structure, enzymatic activity and genome targeting of canonical PRC1. Nat.Struct.Mol.Biol. doi:10.1038/s41594-026-01885-6
2026 Impacts of DNA methylation on H2A.Z deposition and nucleosome stability. Elife doi:10.7554/eLife.109762
2026 BRD4 binds the nucleosome via both histone and DNA interactions. Mol.Cell doi:10.1016/j.molcel.2026.07.012
2026 Cnp1 N-terminal dynamics regulate L1 loop recognition by Mis15 to orchestrate kinetochore assembly in Schizosaccharomyces pombe. J Mol Cell Biol doi:10.1093/jmcb/mjaf056
2026 Chromatin context-dependent deacetylation by the asymmetric Rpd3L. Nucleic Acids Res. doi:10.1093/nar/gkag443
2026 Structural basis for BCL7B-mediated ncBAF-nucleosome engagement. Nucleic Acids Res. doi:10.1093/nar/gkag092
2026 Mechanisms of DNMT3A-3L-mediated de novo DNA methylation on chromatin. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01704-4
2026 Different modes of engagement with the nucleosome acidic patch yield distinct functional outcomes. Nucleic Acids Res. doi:10.1093/nar/gkag693
2026 Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme. Sci Adv doi:10.1126/sciadv.aei7728
2026 Nucleosome spacing regulates linker methylation by DNMT3A2/3B3. Mol.Cell doi:10.1016/j.molcel.2026.01.030
2026 The DNMT1 CXXC domain senses CpG islands for DNA methylation inhibition To Be Published
2026 Trypanosome histone variants H3.V and H4.V promote nucleosome plasticity in repressed chromatin. Structure doi:10.1016/j.str.2026.01.008
2026 DNA-histone cross-link locks the nucleosome structure and disrupts its recognition and processing. Protein Cell doi:10.1093/procel/pwaf094
2026 Structural Characterization of Native RNA Polymerase II Transcription Complexes and Nucleosomes in Drosophila melanogaster. Nat Commun doi:10.1038/s41467-026-75963-0
2026 Recognition and remodelling of nucleosomes and hexasomes by the human INO80 complex. Nucleic Acids Res. doi:10.1093/nar/gkag138
2026 Structural basis of transcription-coupled H3K36 trimethylation by Set2 in coordination with FACT. Sci Adv doi:10.1126/sciadv.aed1952
2026 Structural principles underlying the evolution of SWI/SNF chromatin remodelers Sci Adv
2026 Allosteric activation of RNF20/RNF40-RAD6A-mediated H2BK120 monoubiquitylation by H2BS112 GlcNAcylation. Nat.Chem.Biol. doi:10.1038/s41589-025-02109-6
2026 Structural basis of nucleosome remodeling by Cockayne syndrome B homologue Komagataella phaffii Rad26. Nat Commun doi:10.1038/s41467-026-73500-7
2026 The human BAF chromatin remodeler processes nucleosomes bound by pioneer transcription factors OCT4-SOX2. Mol.Cell doi:10.1016/j.molcel.2026.01.021
2026 Structure and function of IWS1 in transcription elongation. Nucleic Acids Res. doi:10.1093/nar/gkag357
2026 Structural basis of RNA polymerase II transcription on the histone H3-H4 octasome. J.Biol.Chem. doi:10.1016/j.jbc.2026.111340
2026 Structural basis of complex assembly and nucleosome recognition by the chromatin remodeling ncBAF complex. J Mol Cell Biol doi:10.1093/jmcb/mjag020
2026 Structural basis of asymmetric transcription through a composite nucleosome formed by a hexasome and an octasome. Nat.Struct.Mol.Biol. doi:10.1038/s41594-026-01837-0
2026 DNA-PK driven nucleosome unwrapping enables NHEJ in chromatin Nat Commun doi:10.1038/s41467-026-77534-9
2026 The +1 nucleosome functions in RNA Pol II transcription initiation and the transition to elongation. Mol.Cell doi:10.1016/j.molcel.2026.06.042
2026 Models for the architecture of the human inner kinetochore on centromeric alpha-satellite CENP-A nucleosome arrays. Nat Commun doi:10.1038/s41467-026-72856-0
2026 A method for cryo-EM analysis of eukaryotic nucleosomes reconstituted in bacterial cells. Iscience doi:10.1016/j.isci.2025.114453
2026 Structural basis of nucleosome deubiquitination by the bidentate Calypso/Asx complex. Iscience doi:10.1016/j.isci.2026.114958
2026 Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome. Acta Crystallogr D Struct Biol doi:10.1107/S2059798326004158
2025 High-Resolution Cryo-EM Analyses of Nucleosomes. Methods Mol.Biol. doi:10.1007/978-1-0716-4486-7_6
2025 The structure and composition of native human nucleosomes Biorxiv doi:10.1101/2025.10.10.681767
2025 A pivot-tether model for nucleosome recognition by the chromosomal passenger complex. Embo Rep. doi:10.1038/s44319-025-00523-4
2025 The molecular basis of lamin-specific chromatin interactions. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01622-5
2025 Structural insights into chromatin remodeling by ISWI during active ATP hydrolysis. Science doi:10.1126/science.adu5654
2025 ncBAF recognizes the nucleosome through BCL7A in chromatin remodeling. Cell Discov doi:10.1038/s41421-025-00858-1