Homo sapiens · seed O60885 · 1362 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt O60885 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 1.20.920.10 CATH 3.30.40.10 SCOP 8084245 SCOP 8097864 SCOP 8033300 SCOP 8084225 SCOP 8084255 SCOP 8084237 SCOP 8084235 SCOP 8084285 SCOP 8084279 SCOP 8040939 SCOP 8084259 SCOP 8084241 RCSB 9KEM 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.
9KEM, 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.
314 distinct constructs across 1,996 entries. 1,997 polymer entities differ from the UniProt canonical sequence in some way, 1 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 |
|---|---|---|---|---|
| 310 | 127 | 0.94 | 4QB3 | residues 42-168; T43M |
| 297 | 156 | 1.33 | 5PQI | residues 529-688; 2 internal deletions; R529M, D531H, L532H +18 more |
| 199 | 138 | 1.49 | 5PG1 | residues 2034-2168; 3-residue insertion after 2052; K2034M, K2035H, R2036H +16 more |
| 118 | 149 | 1.09 | 5S9G | residues 1297-1440; 5-residue insertion after 1305; T1297M, R1298H, K1299H +13 more |
| 58 | 119 | 1.05 | 5J0D | residues 1079-1197; Q1079S, P1080M |
| 39 | 115 | 1.28 | 7NPZ | residues 341-455; S341G, K342S, K343M |
| 31 | 141 | 1.28 | 8K14 | residues 28-168; T28M, T29K, Q30K +13 more |
| 29 | 129 | 0.99 | 7Z9W | residues 40-168; A40G, A41S, S42H +1 more |
| 27 | 125 | 1.20 | 6JJ5 | residues 43-167; T43M |
| 26 | 117 | 1.70 | 4IR5 | residues 2052-2168; F2052S, T2053M |
| 25 | 105 | 1.09 | 7BLA | residues 1794-1898; N1794S, H1795M, E1845H +1 more |
| 22 | 123 | 1.05 | 5R4O | residues 2915-3037; C2915S, Q2916M |
| 20 | 109 | 1.35 | 5UF0 | residues 349-457; K349S, V350H, S351M |
| 20 | 123 | 1.35 | 6V1B | residues 128-250; A128S, C129M, R130L +13 more |
| 19 | 105 | 1.30 | 7BL9 | residues 1794-1898; N1794S, H1795M |
| 19 | 128 | 1.18 | 5S8F | residues 1313-1440; A1313S, Q1314M |
| 18 | 116 | 1.65 | 5DYU | residues 2052-2167; F2052S, T2053M |
| 15 | 119 | 1.68 | 5MKX | residues 713-831; P713S, S714M |
| 14 | 122 | 1.50 | 6JKE | residues 73-194 |
| 14 | 126 | 1.13 | 9F1J | residues 43-168; T43M |
| 12 | 114 | 1.20 | 5O38 | residues 342-455; K342S, K343M, L383V |
| 12 | 116 | 1.40 | 4OUF | residues 1082-1197 |
| 12 | 124 | 1.43 | 4HXS | residues 43-166; T43M |
| 12 | 154 | 1.60 | 4ALG | residues 47-200; T47G, M48S, A49S +16 more |
| 11 | 113 | 1.39 | 7MRD | residues 25-137; N25G, G26A, R27A +1 more |
Showing the 25 most-used of 314.
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 |
|---|---|---|---|
| monomeric | 1 | 1,722 | 86.3% |
| dimeric | 2 | 191 | 9.6% |
| trimeric | 3 | 36 | 1.8% |
| tetrameric | 4 | 27 | 1.4% |
| undecameric | 11 | 11 | 0.6% |
| hexameric | 6 | 3 | 0.2% |
| octameric | 8 | 2 | 0.1% |
| 27-meric | 27 | 1 | 0.1% |
955 entries have the depositor's assembly corroborated by PISA, 982 carry the depositor's word alone and 59 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 22 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 2DVQ, 2DVR, 2DVS, 2FSA, 3AQA, 3HMF, 3ONI, 4QC3, 4QEV, 4QEW, 5TWX, 5VBR, 5XZC, 6V1B, 7L9J, 7RJM, 7TUQ, 7TV0, 8B5B, 8CV4.
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 |
|---|---|---|---|
| Bromodomain-like | CATH 1.20.920.10 | 358–468 | 1,411 |
| Zinc/RING finger domain, C3HC4 (zinc finger) | CATH 3.30.40.10 | 491–499 | 31 |
| Bromodomain | SCOP2B 8084245 | 60–165 | 519 |
| Bromodomain | SCOP2B 8097864 | 61–176 | 53 |
| Bromodomain | SCOP2B 8033300 | 69–176 | 22 |
| Bromodomain | SCOP2B 8084225 | 73–188 | 42 |
| Bromodomain | SCOP2B 8084255 | 355–462 | 93 |
| Bromodomain | SCOP2B 8084237 | 356–458 | 54 |
| Bromodomain | SCOP2B 8084235 | 374–486 | 258 |
| Bromodomain | SCOP2B 8084285 | 378–477 | 52 |
| Bromodomain | SCOP2B 8084279 | 379–494 | 141 |
| Bromodomain | SCOP2B 8040939 | 380–493 | 113 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| EDO | cryoprotectant | 1,2-Ethanediol | 1,030 | 0.94 |
| NA | ion | Sodium Ion | 348 | 1.16 |
| GOL | cryoprotectant | Glycerol | 132 | 0.91 |
| DMS | cryoprotectant | Dimethyl Sulfoxide | 84 | 1.05 |
| SO4 | ion | Sulfate Ion | 61 | 1.15 |
| ZN | ion | Zinc Ion | 57 | 1.14 |
| CL | ion | Chloride Ion | 51 | 0.91 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 28 | 1.04 |
| NO3 | ion | Nitrate Ion | 25 | 1.42 |
| MG | ion | Magnesium Ion | 19 | 1.62 |
| FMT | buffer | Formic Acid | 17 | 1.20 |
| ACT | cryoprotectant | Acetate Ion | 15 | 1.07 |
| BU3 | cryoprotectant | (R,r)-2,3-Butanediol | 14 | 1.25 |
| MES | buffer | 2-(N-Morpholino)-Ethanesulfonic Acid | 12 | 1.59 |
| NI | ion | Nickel (Ii) Ion | 11 | 1.10 |
| K | ion | Potassium Ion | 11 | 1.23 |
| SCN | ion | Thiocyanate Ion | 9 | 1.05 |
| PGE | cryoprotectant | Triethylene Glycol | 9 | 0.94 |
| CA | ion | Calcium Ion | 9 | 1.07 |
| NH2 | solvent | Amino Group | 9 | 1.47 |
Parsed from the free text 1,918 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 1,926
entries that recorded anything at all.
Median pH 7.0
(range 3.5 to 10.5).
1,995 entries carry a wwPDB validation report: 1,249 clean, 659 worth a check and 87 with something to explain. Median clashscore 2.93, median RSRZ outliers 3.48%, median R-free minus R-work 0.033. 1,981 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 1,944 | 0.91 | 1296 | 53% |
| Mus musculus | 21 | 1.20 | 9 | 24% |
| Nakaseomyces glabratus | 6 | 1.08 | 4 | 15% |
| Plasmodium falciparum 3D7 | 6 | 1.56 | 2 | 13% |
| Candida albicans | 4 | 1.20 | 2 | 16% |
| Plasmodium vivax | 4 | 1.61 | 4 | 7% |
| Thermochaetoides thermophila | 3 | 3.50 | 0 | 7% |
| Schistosoma mansoni | 2 | 1.22 | 2 | 8% |
| Plasmodium falciparum | 2 | 1.25 | 2 | 13% |
| Cryptosporidium parvum | 1 | 1.38 | 1 | 5% |
| Candida albicans SC5314 | 1 | 1.45 | 1 | 8% |
| Fusarium graminearum | 1 | 1.58 | 0 | 8% |
1362 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 | Differential Water Networks Guide Selectivity Optimization of a Cell Active BPTF Inhibitor in Neuroblastoma. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.4580510 |
| 2026 | BET Bromodomain Targeting by NSAIDs: Structural, Biophysical, and Computational Insights. Proteins doi:10.1002/prot.70154 |
| 2026 | Structural Basis for BD1-Preferring 2,4-Disubstituted Pyrimidine BRDT Inhibitors. J.Med.Chem. doi:10.1021/acs.jmedchem.6c00180 |
| 2026 | Stabilizing Plasmodium falciparum proteins for small molecule drug discovery. Protein Sci. doi:10.1002/pro.70614 |
| 2026 | The effect of peptide size on target affinity in mRNA display-derived macrocyclic peptides. Chem.Commun.(Camb.) doi:10.1039/d5cc06167a |
| 2026 | Structural insights into histone mimicry by the small hepatitis delta antigen. J.Biol.Chem. doi:10.1016/j.jbc.2026.113252 |
| 2026 | Discovery and Structural Optimization of BRD4-Selective Monovalent Direct Degraders. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.6c00022 |
| 2026 | Cell type-selective targeting by heterobifunctional protein binders via in-cell enrichment. Nat Commun doi:10.1038/s41467-026-77460-w |
| 2026 | Structural mechanism of diacetylated histone H2A recognition by Bromodomain-containing protein 4 in Regulation of non-homologous end-joining DNA repair. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2026.152638 |
| 2026 | Fragment-Based Acs Omega doi:10.1021/acsomega.6c06516 |
| 2026 | Chemical tools for BAZ2A/B biology: discovery of dual and BAZ2B-selective PROTAC degraders. Rsc Med Chem doi:10.1039/d6md00244g |
| 2026 | BRD4 binds the nucleosome via both histone and DNA interactions. Mol.Cell doi:10.1016/j.molcel.2026.07.012 |
| 2026 | Charged molecular glue discovery enabled by targeted degron display. Nat.Chem.Biol. doi:10.1038/s41589-026-02182-5 |
| 2026 | BRD9 recognizes lactate-induced H3K18 lactylation to drive oncogenic chromatin remodeling in hepatocellular carcinoma. Cell Death Differ. doi:10.1038/s41418-026-01698-6 |
| 2026 | Recruitment of BRD4 to the ASXL1 genomic targets depends on the extra-terminal domain of BRD4. Nat Commun doi:10.1038/s41467-026-69565-z |
| 2025 | Humanized Candida and NanoBiT Assays Expedite Discovery of Bdf1 Bromodomain Inhibitors With Antifungal Potential. Adv Sci doi:10.1002/advs.202404260 |
| 2025 | Binding-Site Purification of Actives (B-SPA) Enables Efficient Large-Scale Progression of Fragment Hits by Combining Multi-Step Array Synthesis With HT Crystallography. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202424373 |
| 2025 | Structure-Based Rational Design and Evaluation of BET-Aurora Kinase Dual-Inhibitors for Treatment of Cancers. J.Med.Chem. doi:10.1021/acs.jmedchem.4c01933 |
| 2025 | Structure-Guided Design of ISOX-DUAL-Based Degraders Targeting BRD4 and CBP/EP300: A Case of Degrader Collapse. J.Med.Chem. doi:10.1021/acs.jmedchem.5c00395 |
| 2025 | Structure-activity relationships can be directly extracted from high-throughput crystallographic evaluation of fragment elaborations in crude reaction mixtures. Chem Sci doi:10.1039/d5sc04919a |
| 2025 | Macrocyclic dihydropyridine analogs as pan-BET BD2-preferred inhibitors. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2025.117504 |
| 2025 | A bottom-up approach to find lead compounds in expansive chemical spaces. Commun Chem doi:10.1038/s42004-025-01610-2 |
| 2025 | Discovery of 5-imidazole-3-methylbenz[d]isoxazole derivatives as potent and selective CBP/p300 bromodomain inhibitors for the treatment of acute myeloid leukemia. Acta Pharmacol.Sin. doi:10.1038/s41401-025-01478-x |
| 2025 | A Novel Inhibitor against the Bromodomain Protein 1 of the Malaria Pathogen Plasmodium Falciparum. Chemmedchem doi:10.1002/cmdc.202500024 |
| 2025 | Multi-Water Bridges Enable Design of BET BD1-Selective Inhibitors for Pancreatic Cancer Therapy. J.Med.Chem. doi:10.1021/acs.jmedchem.4c03069 |
| 2025 | Polybromo-1 Bromodomain Inhibitor Selectivity Is Mediated by a Unique Ligand-Binding Pocket Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.5c00352 |
| 2025 | Key imidazolyl groups that induce phenylalanine flipping enhance the efficacy of oral BRD9 inhibitors for AML treatment. Acta Pharm Sin B doi:10.1016/j.apsb.2025.08.006 |
| 2025 | Positional isomers of Indolyl-benzodiazepines display dissimilar binding and recruitment of BET transcriptional regulators to targeted genomic loci. Bioorg.Chem. doi:10.1016/j.bioorg.2025.108813 |
| 2025 | A Bivalent Molecular Glue Linking Lysine Acetyltransferases to Oncogene-induced Cell Death. Biorxiv doi:10.1101/2025.03.14.643404 |
| 2025 | Enzyme-Activated Sugar-Coated Bifunctional Degraders. J.Am.Chem.Soc. doi:10.1021/jacs.5c09843 |
| 2025 | Design of PROTACs utilizing the E3 ligase GID4 for targeted protein degradation. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01537-1 |
| 2025 | Structural basis for DCAF2 as a novel E3 ligase for PROTAC-mediated targeted protein degradation. Structure doi:10.1016/j.str.2025.09.006 |
| 2025 | Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase module. Mol.Cell doi:10.1016/j.molcel.2025.10.025 |
| 2024 | Discovery of a potent, orally available furopyridine derivative as a novel selective bromodomain and extra-terminal domain (BET)-first bromodomain (BD1) inhibitor. Bioorg.Med.Chem.Lett. doi:10.1016/j.bmcl.2024.129848 |
| 2024 | Development of Potent Dual BET/HDAC Inhibitors via Pharmacophore Merging and Structure-Guided Optimization. Acs Chem.Biol. doi:10.1021/acschembio.3c00427 |
| 2024 | High resolution crystal structure of BRD4-BD1 in complex with a novel inhibitor precursor. Biochem.Biophys.Res.Commun. doi:10.1016/j.bbrc.2023.149284 |
| 2024 | Probing Protein-Ligand Methyl-pi Interaction Geometries through Chemical Shift Measurements of Selectively Labeled Methyl Groups. J Med Chem doi:10.1039/b508541a |
| 2024 | Enhanced cellular death in liver and breast cancer cells by dual BET/BRPF1 inhibitors. Protein Sci. doi:10.1002/pro.5191 |
| 2024 | Probing Protein-Ligand Methyl-pi Interaction Geometries through Chemical Shift Measurements of Selectively Labeled Methyl Groups. J.Med.Chem. doi:10.1021/acs.jmedchem.4c01128 |
| 2024 | Discovery of (R)-4-(8-methoxy-2-methyl-1-(1-phenylethy)-1H-imidazo[4,5-c]quinnolin-7-yl)-3,5-dimethylisoxazole as a potent and selective BET inhibitor for treatment of acute myeloid leukemia (AML) guided by FEP calculation. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2023.115924 |