Homo sapiens · seed P68431 · 136 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P68431 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 1.10.20.10 SCOP 8042439 SCOP 8041272 SCOP 8096712 SCOP 8036585 SCOP 8070527 SCOP 8039340 SCOP 8070531 SCOP 8070539 RCSB 8OOP 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.
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.
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.
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.
| Entities | Length | Best (Å) | Best entry | What 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.
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 |
|---|---|---|---|
| decameric | 10 | 332 | 28.0% |
| undecameric | 11 | 207 | 17.5% |
| dodecameric | 12 | 145 | 12.2% |
| tetradecameric | 14 | 71 | 6.0% |
| 20-meric | 20 | 42 | 3.5% |
| tridecameric | 13 | 41 | 3.5% |
| hexadecameric | 16 | 25 | 2.1% |
| dimeric | 2 | 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.
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 |
|---|---|---|---|
| Histone, subunit A | CATH 1.10.20.10 | 42–136 | 216 |
| Core histone-like | SCOP2B 8042439 | 24–102 | 14 |
| Core histone-like | SCOP2B 8041272 | 39–135 | 203 |
| Core histone-like | SCOP2B 8096712 | 39–135 | 41 |
| Core histone-like | SCOP2B 8036585 | 39–135 | 19 |
| Core histone-like | SCOP2B 8070527 | 40–136 | 20 |
| Core histone-like | SCOP2B 8039340 | 42–136 | 256 |
| Core histone-like | SCOP2B 8070531 | 42–135 | 114 |
| Core histone-like | SCOP2B 8070539 | 94–136 | 27 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| ZN | ion | Zinc Ion | 286 | 1.40 |
| MG | ion | Magnesium Ion | 170 | 2.17 |
| ADP | cofactor | Adenosine-5'-Diphosphate | 104 | 2.50 |
| MN | ion | Manganese (Ii) Ion | 97 | 1.94 |
| CL | ion | Chloride Ion | 78 | 1.80 |
| BEF | ion | Beryllium Trifluoride Ion | 43 | 2.80 |
| SO4 | ion | Sulfate Ion | 41 | 1.55 |
| SAH | cofactor | S-Adenosyl-L-Homocysteine | 38 | 2.39 |
| ATP | cofactor | Adenosine-5'-Triphosphate | 23 | 2.30 |
| SAM | cofactor | S-Adenosylmethionine | 23 | 2.57 |
| CA | ion | Calcium Ion | 17 | 2.11 |
| K | ion | Potassium Ion | 16 | 2.20 |
| PO4 | ion | Phosphate Ion | 14 | 1.90 |
| SF4 | ligand | Iron/sulfur Cluster | 12 | 3.10 |
| AGS | cofactor | Phosphothiophosphoric Acid-Adenylate Ester | 12 | 3.00 |
| GOL | cryoprotectant | Glycerol | 11 | 1.70 |
| NAG | cofactor | 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose | 9 | 2.89 |
| PTD | ligand | Pentanedial | 7 | 3.05 |
| OGA | ligand | N-Oxalylglycine | 6 | 1.80 |
| HEM | cofactor | Protoporphyrin Ix Containing Fe | 6 | 2.89 |
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).
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.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 618 | 1.40 | 66 | 100% |
| Xenopus laevis | 432 | 1.70 | 166 | 100% |
| Saccharomyces cerevisiae | 25 | 2.80 | 6 | 100% |
| Drosophila melanogaster | 24 | 2.10 | 1 | 100% |
| Arabidopsis thaliana | 20 | 2.71 | 5 | 100% |
| Saccharomyces cerevisiae S288C | 17 | 2.70 | 9 | 100% |
| Mus musculus | 11 | 2.34 | 1 | 100% |
| Gallus gallus | 10 | 1.90 | 0 | 100% |
| Unknown | 5 | 1.80 | 4 | 100% |
| Xenopus | 3 | 2.74 | 0 | 100% |
| Schizosaccharomyces pombe 972h- | 2 | 2.99 | 0 | 68% |
| Caenorhabditis elegans | 2 | 2.30 | 2 | 24% |
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
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 | 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 |