Homo sapiens · seed P03372 · 595 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P03372 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.30.50.10 CATH 1.10.565.10 SCOP 8039047 SCOP 8039031 SCOP 8068336 SCOP 8044103 SCOP 8038722 SCOP 8038695 SCOP 8094545 SCOP 8033858 SCOP 8033332 SCOP 8068507 RCSB 5T92 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.
5T92, 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.
300 distinct constructs across 760 entries. 771 polymer entities differ from the UniProt canonical sequence in some way, 2 carry a recognised expression tag and 1 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 |
|---|---|---|---|---|
| 121 | 257 | 1.60 | 5KCT | residues 298-554; Y537S |
| 19 | 255 | 1.80 | 4MGA | residues 298-552; I298G, K299S, R300H +2 more |
| 18 | 240 | 1.80 | 2P1T | residues 223-462 |
| 16 | 255 | 1.47 | 8DU8 | residues 300-554; R300M, C381S, C417S +2 more |
| 14 | 90 | 1.61 | 3G9M | residues 436-525; P436G, P437S, K438H +1 more |
| 14 | 240 | 1.50 | 3OLL | residues 261-500 |
| 14 | 258 | 1.72 | 2QZO | residues 297-554; M297S, Y537S |
| 13 | 257 | 1.58 | 7RS7 | residues 298-554; L372S, L536S |
| 12 | 231 | 2.00 | 4K4J | residues 228-458 |
| 10 | 238 | 2.00 | 1G5Y | residues 225-462 |
| 10 | 247 | 1.93 | 4IWF | residues 303-549; Y537S |
| 10 | 251 | 1.47 | 9N0C | residues 303-553; G303M, K304H, S305H +4 more |
| 10 | 251 | 1.50 | 9KNG | residues 213-458; 5-residue insertion after 227; R213M, I214G, D215S +11 more |
| 9 | 87 | 1.60 | 6FBQ | residues 126-212; N126G, M127S, A128H +1 more |
| 8 | 243 | 1.50 | 6LB4 | residues 220-462; V220G, E221S, T223H |
| 8 | 244 | 1.89 | 6STI | residues 219-462; E219G, V220S, E221H +1 more |
| 8 | 249 | 1.50 | 7R62 | residues 306-554; C381S, C417S, C530S +1 more |
| 8 | 251 | 1.60 | 3UUD | residues 302-552; Y537S |
| 8 | 252 | 1.68 | 7QVJ | residues 303-554; K303G, N304S, S305H +5 more |
| 8 | 259 | 1.77 | 4ZNV | residues 301-559; Y537S |
| 8 | 261 | 1.50 | 5DXE | residues 294-554; S294M, P295D, L296P +1 more |
| 7 | 248 | 1.60 | 1XPC | residues 307-554 |
| 7 | 248 | 1.84 | 2POG | residues 304-551; C381S, C417S, C530S |
| 6 | 230 | 1.70 | 2GPU | residues 229-458 |
| 6 | 242 | 1.68 | 8W03 | residues 305-546; L372S, L536S |
Showing the 25 most-used of 300.
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 |
|---|---|---|---|
| tetrameric | 4 | 408 | 53.7% |
| dimeric | 2 | 275 | 36.2% |
| monomeric | 1 | 45 | 5.9% |
| trimeric | 3 | 10 | 1.3% |
| hexameric | 6 | 10 | 1.3% |
| octameric | 8 | 6 | 0.8% |
| pentameric | 5 | 3 | 0.4% |
| dodecameric | 12 | 1 | 0.1% |
553 entries have the depositor's assembly corroborated by PISA, 158 carry the depositor's word alone and 47 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 38 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1A52, 1L2J, 1NDE, 1NHZ, 1S9P, 1S9Q, 1U9E, 1XDK, 1XLS, 1XVP, 2ACL, 2FSZ, 3A9E, 3D24, 3E7C, 3FAL, 3FUG, 3G6Q, 3G9I, 3K6P.
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 |
|---|---|---|---|
| Erythroid Transcription Factor GATA-1, subunit A | CATH 3.30.50.10 | 186–264 | 62 |
| Retinoid X Receptor | CATH 1.10.565.10 | 310–548 | 583 |
| Glucocorticoid receptor-like (DNA-binding domain) | SCOP2B 8039047 | 189–259 | 14 |
| Glucocorticoid receptor-like (DNA-binding domain) | SCOP2B 8039031 | 191–269 | 17 |
| Glucocorticoid receptor-like (DNA-binding domain) | SCOP2B 8068336 | 199–271 | 18 |
| Nuclear receptor ligand-binding domain | SCOP2B 8044103 | 307–548 | 372 |
| Nuclear receptor ligand-binding domain | SCOP2B 8038722 | 311–547 | 38 |
| Nuclear receptor ligand-binding domain | SCOP2B 8038695 | 314–543 | 89 |
| Nuclear receptor ligand-binding domain | SCOP2B 8094545 | 316–562 | 9 |
| Nuclear receptor ligand-binding domain | SCOP2B 8033858 | 318–539 | 31 |
| Nuclear receptor ligand-binding domain | SCOP2B 8033332 | 326–572 | 32 |
| Nuclear receptor ligand-binding domain | SCOP2B 8068507 | 342–585 | 28 |
EST32 entries
DEX19 entries
9CR18 entries
OHT13 entries
CPS9 entries
RAL7 entries
REA6 entries
2OH6 entries
4865 entries
GEN5 entries
1CA5 entries
STR5 entries
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| ZN | ion | Zinc Ion | 113 | 1.60 |
| GOL | cryoprotectant | Glycerol | 63 | 1.33 |
| EDO | cryoprotectant | 1,2-Ethanediol | 49 | 1.10 |
| EST | ligand | Estradiol | 32 | 1.45 |
| CL | ion | Chloride Ion | 25 | 1.33 |
| SO4 | ion | Sulfate Ion | 22 | 1.75 |
| DEX | ligand | Dexamethasone | 19 | 1.50 |
| 9CR | ligand | (9cis)-Retinoic Acid | 18 | 1.98 |
| OHT | ligand | 4-Hydroxytamoxifen | 13 | 1.70 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 11 | 1.75 |
| CPS | ligand | 3-[(3-Cholamidopropyl)dimethylammonio]-1-Propanesulfonate | 9 | 1.80 |
| RAL | ligand | Raloxifene | 7 | 1.60 |
| ACT | cryoprotectant | Acetate Ion | 7 | 1.89 |
| NA | ion | Sodium Ion | 7 | 1.33 |
| MG | ion | Magnesium Ion | 7 | 1.45 |
| REA | ligand | Retinoic Acid | 6 | 2.00 |
| 2OH | ligand | 4,4'-Propane-2,2-Diyldiphenol | 6 | 1.60 |
| FMT | buffer | Formic Acid | 6 | 1.65 |
| 486 | ligand | 11-(4-Dimethylamino-Phenyl)-17-Hydroxy-13-Methyl-17-Prop-1-Ynyl- | 5 | 2.01 |
| GEN | ligand | Genistein | 5 | 1.33 |
Parsed from the free text 725 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 732
entries that recorded anything at all.
Median pH 7.5
(range 4.2 to 9.0).
758 entries carry a wwPDB validation report: 247 clean, 289 worth a check and 222 with something to explain. Median clashscore 6.25, median RSRZ outliers 4.55%, median R-free minus R-work 0.042. 719 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 665 | 1.10 | 604 | 100% |
| Rattus norvegicus | 29 | 1.61 | 4 | 56% |
| Mus musculus | 19 | 1.50 | 13 | 58% |
| unidentified | 13 | 1.90 | 10 | 47% |
| Melanotaenia fluviatilis | 11 | 1.47 | 10 | 40% |
| synthetic construct | 10 | 1.45 | 5 | 48% |
| Drosophila melanogaster | 3 | 1.95 | 0 | 13% |
| Unknown | 3 | 2.04 | 3 | 24% |
| Heliothis virescens | 1 | 11.60 | 2 | 13% |
| Saguinus oedipus | 1 | 2.35 | 0 | 11% |
| Heterocephalus glaber | 1 | 2.35 | 1 | 30% |
| Magallana gigas | 1 | 2.60 | 0 | 39% |
595 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 | Mineralocorticoid Receptor Antagonists With an Acylurea as a Key Polar Interaction Motif. Chemmedchem doi:10.1002/cmdc.202501047 |
| 2026 | A distinct zearalenone detoxification strategy mediated by cytochrome P450. Food Chem doi:10.1016/j.foodchem.2026.148697 |
| 2026 | Allosteric Induction of Estrogen Receptor Ligand Binding Domain Tetramerization by a Distinct Complete Estrogen Receptor Antagonist. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.5c00667 |
| 2026 | Induced ubiquitination of the partially disordered estrogen receptor alpha via a 14-3-3 directed molecular glue-PROTAC. Nat Commun doi:10.1038/s41467-026-75333-w |
| 2025 | Development of an RXR Agonist Scaffold with Pronounced Homodimer Preference. J.Med.Chem. doi:10.1021/acs.jmedchem.5c01090 |
| 2025 | Identification of indoles as potential endogenous ligands of ERR gamma and their modulation on drug binding. Acta Pharmacol.Sin. doi:10.1038/s41401-025-01550-6 |
| 2025 | Targeting unique ligand binding domain structural features downregulates DKK1 in Y537S ESR1 mutant breast cancer cells. Breast Cancer Res doi:10.1186/s13058-024-01945-z |
| 2025 | Structural Tuning of Partial RXR Agonism and Antagonism. J.Med.Chem. doi:10.1021/acs.jmedchem.5c02270 |
| 2025 | A ternary switch model governing ER alpha ligand binding domain conformation. Nat Commun doi:10.1038/s41467-025-65323-9 |
| 2025 | Discovery of Palazestrant (OP-1250), a Potent and Orally Bioavailable Complete Estrogen Receptor Antagonist (CERAN) and Selective Estrogen Receptor Degrader (SERD). Acs Omega doi:10.1021/acsomega.4c11023 |
| 2025 | The multimerization pathway of the glucocorticoid receptor. Nucleic Acids Res. doi:10.1093/nar/gkaf1003 |
| 2025 | New structural insights into the control of the retinoic acid receptors RAR/RXR by DNA, ligands, and transcriptional coregulators. Nucleic Acids Res. doi:10.1093/nar/gkaf967 |
| 2024 | Asymmetric allostery in estrogen receptor-alpha homodimers drives responses to the ensemble of estrogens in the hormonal milieu. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2321344121 |
| 2024 | Structure-Guided Design of a Highly Potent Partial RXR Agonist with Superior Physicochemical Properties. J.Med.Chem. doi:10.1021/acs.jmedchem.3c02095 |
| 2024 | Structural mechanism underlying variations in DNA binding by the androgen receptor. J.Steroid Biochem.Mol.Biol. doi:10.1016/j.jsbmb.2024.106499 |
| 2024 | Minimising the payload solvent exposed hydrophobic surface area optimises the antibody-drug conjugate properties. Rsc Med Chem doi:10.1039/d3md00540b |
| 2024 | Structural characterization of the DNA binding mechanism of retinoic acid-related orphan receptor gamma. Structure doi:10.1016/j.str.2024.01.004 |
| 2024 | Structural basis for the full and partial agonist activities of retinoid X receptor alpha ligands with an iso-butoxy and an isopropyl group Biochem.Biophys.Res.Commun. doi:10.1016/j.bbrc.2024.150617 |
| 2024 | Nucleosome-bound NR5A2 structure reveals pioneer factor mechanism by DNA minor groove anchor competition. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01239-0 |
| 2023 | Structures of human TR4LBD-JAZF1 and TR4DBD-DNA complexes reveal the molecular basis of transcriptional regulation. Nucleic Acids Res. doi:10.1093/nar/gkac1259 |
| 2023 | Discovery of a Potent and Orally Bioavailable Zwitterionic Series of Selective Estrogen Receptor Degrader-Antagonists. J.Med.Chem. doi:10.1021/acs.jmedchem.2c01964 |
| 2023 | Structural Determinants of the Binding and Activation of Estrogen Receptor alpha by Phenolic Thieno[2,3-d]pyrimidines Helv.Chim.Acta doi:10.1002/hlca.202300097 |
| 2023 | Structure-guided identification of novel dual-targeting estrogen receptor alpha degraders with aromatase inhibitory activity for the treatment of endocrine-resistant breast cancer. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2023.115328 |
| 2023 | Quaternary glucocorticoid receptor structure highlights allosteric interdomain communication. Nat.Struct.Mol.Biol. doi:10.1038/s41594-022-00914-4 |
| 2023 | ERR gamma-DBD undergoes dimerization and conformational rearrangement upon binding to the downstream site of the DR1 element. Biochem.Biophys.Res.Commun. doi:10.1016/j.bbrc.2023.03.038 |
| 2023 | Discovery of novel covalent selective estrogen receptor degraders against endocrine-resistant breast cancer. Acta Pharm Sin B doi:10.1016/j.apsb.2023.05.005 |
| 2023 | X-ray crystallography study and optimization of novel benzothiophene analogs as potent selective estrogen receptor covalent antagonists (SERCAs) with improved potency and safety profiles. Bioorg.Chem. doi:10.1016/j.bioorg.2023.106919 |
| 2023 | 2,4-Di-tert-butylphenol Induces Adipogenesis in Human Mesenchymal Stem Cells by Activating Retinoid X Receptors. Endocrinology doi:10.1210/endocr/bqad021 |
| 2023 | Asymmetric dimerization in a transcription factor superfamily is promoted by allosteric interactions with DNA. Nucleic Acids Res. doi:10.1093/nar/gkad632 |
| 2023 | Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor. Nat.Struct.Mol.Biol. doi:10.1038/s41594-023-01128-y |
| 2023 | Structural basis of the farnesoid X receptor/retinoid X receptor heterodimer on inverted repeat DNA. Comput Struct Biotechnol J doi:10.1016/j.csbj.2023.05.026 |
| 2022 | Stereospecific lasofoxifene derivatives reveal the interplay between estrogen receptor alpha stability and antagonistic activity in ESR1 mutant breast cancer cells. Elife doi:10.7554/eLife.72512 |
| 2022 | Unconventional isoquinoline-based SERMs elicit fulvestrant-like transcriptional programs in ER+ breast cancer cells. NPJ Breast Cancer doi:10.1038/s41523-022-00497-9 |
| 2022 | Evaluating the correlation of binding affinities between isothermal titration calorimetry and fragment molecular orbital method of estrogen receptor beta with diarylpropionitrile (DPN) or DPN derivatives. J.Steroid Biochem.Mol.Biol. doi:10.1016/j.jsbmb.2022.106152 |
| 2022 | A New Chemotype of Chemically Tractable Nonsteroidal Estrogens Based on a Thieno[2,3- d ]pyrimidine Core. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.2c00180 |
| 2022 | Design and in vitro characterization of RXR variants as tools to investigate the biological role of endogenous rexinoids. J.Mol.Endocrinol. doi:10.1530/JME-22-0021 |
| 2022 | Design, synthesis, biological evaluation and crystal structure determination of dual modulators of carbonic anhydrases and estrogen receptors. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2022.115011 |
| 2022 | Conformationally Defined Rexinoids for the Prevention of Inflammation and Nonmelanoma Skin Cancers. J.Med.Chem. doi:10.1021/acs.jmedchem.2c00735 |
| 2022 | The multivalency of the glucocorticoid receptor ligand-binding domain explains its manifold physiological activities. Nucleic Acids Res. doi:10.1093/nar/gkac1119 |
| 2022 | Integrative analysis reveals structural basis for transcription activation of Nurr1 and Nurr1-RXR alpha heterodimer. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2206737119 |