Homo sapiens · seed P10275 · 920 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P10275 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 8037208 SCOP 8038722 SCOP 8094545 SCOP 8039734 SCOP 8040073 SCOP 8033332 SCOP 8068507 SCOP 8040407 RCSB 2AM9 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.
2AM9, 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.
202 distinct constructs across 368 entries. 359 polymer entities differ from the UniProt canonical sequence in some way, 0 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 |
|---|---|---|---|---|
| 14 | 90 | 1.61 | 3G9M | residues 436-525; P436G, P437S, K438H +1 more |
| 14 | 240 | 1.50 | 3OLL | residues 261-500 |
| 14 | 251 | 1.66 | 1T65 | residues 670-920 |
| 11 | 249 | 1.65 | 3B66 | residues 672-920 |
| 9 | 87 | 1.60 | 6FBQ | residues 126-212; N126G, M127S, A128H +1 more |
| 8 | 269 | 1.40 | 1T7R | residues 643-911; P643G, T644S, E645P +8 more |
| 7 | 250 | 1.42 | 4OHA | residues 671-920; R761A, T878A |
| 7 | 250 | 2.00 | 4OJB | residues 671-920; W742L, R761A |
| 7 | 256 | 1.65 | 2AX9 | residues 665-920 |
| 6 | 248 | 2.25 | 7YXC | A1F |
| 6 | 250 | 1.80 | 4OEZ | residues 671-920; R761A |
| 6 | 260 | 1.65 | 3ZR7 | residues 674-933; T674G, F675S, S676H +1 more |
| 6 | 280 | 1.80 | 4UDD | residues 498-777; K498G, G499S, N517D +3 more |
| 6 | 305 | 1.46 | 9GC7 | TEV site; residues 734-984; L734M, C808S, S810L +1 more |
| 5 | 114 | 1.85 | 5E69 | residues 390-506; 1 internal deletion; S390M, N391H, G392H +19 more |
| 5 | 247 | 1.54 | 7XVY | residues 256-502; R256G, E257P, L259G +6 more |
| 5 | 266 | 1.64 | 2AM9 | residues 655-920 |
| 4 | 256 | 1.80 | 1A28 | residues 678-933 |
| 4 | 257 | 2.28 | 2JJ3 | residues 249-505; G249M, G250H, A252H +3 more |
| 4 | 260 | 1.95 | 3G0W | residues 644-902; 1-residue insertion after 646; V644G |
| 3 | 94 | 2.30 | 1A6Y | residues 123-216; H147L |
| 3 | 94 | 2.30 | 5EMC | residues 407-500; S407G, S409H, S410M |
| 3 | 110 | 2.70 | 1KB2 | residues 16-125 |
| 3 | 249 | 1.45 | 6W9L | A1F |
| 3 | 257 | 1.87 | 2Q7I | residues 664-920 |
Showing the 25 most-used of 202.
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 |
|---|---|---|---|
| dimeric | 2 | 123 | 33.4% |
| tetrameric | 4 | 115 | 31.2% |
| monomeric | 1 | 112 | 30.4% |
| trimeric | 3 | 6 | 1.6% |
| hexameric | 6 | 4 | 1.1% |
| octameric | 8 | 4 | 1.1% |
| pentameric | 5 | 3 | 0.8% |
| 11-meric | 11 | 1 | 0.3% |
224 entries have the depositor's assembly corroborated by PISA, 115 carry the depositor's word alone and 28 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 20 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1L2J, 1NDE, 1NHZ, 1U9E, 2FSZ, 2OVH, 2OVM, 3D24, 3E7C, 3G6Q, 3G9I, 3K6P, 3OLL, 3OLS, 3OMO, 3OMP, 3OMQ, 4FN9, 4LSJ, 8IFO.
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 | 561–638 | 57 |
| Retinoid X Receptor | CATH 1.10.565.10 | 673–920 | 247 |
| Glucocorticoid receptor-like (DNA-binding domain) | SCOP2B 8039047 | 564–634 | 14 |
| Glucocorticoid receptor-like (DNA-binding domain) | SCOP2B 8039031 | 565–643 | 12 |
| Glucocorticoid receptor-like (DNA-binding domain) | SCOP2B 8068336 | 581–653 | 18 |
| Nuclear receptor ligand-binding domain | SCOP2B 8037208 | 672–919 | 90 |
| Nuclear receptor ligand-binding domain | SCOP2B 8038722 | 673–908 | 37 |
| Nuclear receptor ligand-binding domain | SCOP2B 8094545 | 673–919 | 9 |
| Nuclear receptor ligand-binding domain | SCOP2B 8039734 | 677–920 | 18 |
| Nuclear receptor ligand-binding domain | SCOP2B 8040073 | 681–920 | 7 |
| Nuclear receptor ligand-binding domain | SCOP2B 8033332 | 683–920 | 32 |
| Nuclear receptor ligand-binding domain | SCOP2B 8068507 | 694–920 | 29 |
DHT48 entries
DEX19 entries
STR8 entries
1988 entries
HFT8 entries
CPS8 entries
4866 entries
1CA6 entries
R185 entries
EST5 entries
4HY4 entries
NDR3 entries
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| ZN | ion | Zinc Ion | 108 | 1.60 |
| SO4 | ion | Sulfate Ion | 69 | 1.40 |
| DHT | ligand | 5-Alpha-Dihydrotestosterone | 48 | 1.40 |
| GOL | cryoprotectant | Glycerol | 48 | 1.44 |
| EDO | cryoprotectant | 1,2-Ethanediol | 32 | 1.10 |
| DEX | ligand | Dexamethasone | 19 | 1.50 |
| TES | buffer | Testosterone | 11 | 1.64 |
| CL | ion | Chloride Ion | 9 | 1.71 |
| STR | ligand | Progesterone | 8 | 1.55 |
| 198 | ligand | R-Bicalutamide | 8 | 1.80 |
| HFT | ligand | Hydroxyflutamide | 8 | 1.42 |
| CPS | ligand | 3-[(3-Cholamidopropyl)dimethylammonio]-1-Propanesulfonate | 8 | 1.80 |
| 486 | ligand | 11-(4-Dimethylamino-Phenyl)-17-Hydroxy-13-Methyl-17-Prop-1-Ynyl- | 6 | 1.80 |
| 1CA | ligand | Desoxycorticosterone | 6 | 1.95 |
| IMD | buffer | Imidazole | 6 | 1.40 |
| R18 | ligand | (17beta)-17-Hydroxy-17-Methylestra-4,9,11-Trien-3-One | 5 | 1.80 |
| NA | ion | Sodium Ion | 5 | 1.70 |
| EST | ligand | Estradiol | 5 | 1.50 |
| MG | ion | Magnesium Ion | 5 | 2.07 |
| MPD | cryoprotectant | (4s)-2-Methyl-2,4-Pentanediol | 5 | 1.46 |
Parsed from the free text 333 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 338
entries that recorded anything at all.
Median pH 7.0
(range 4.2 to 8.5).
367 entries carry a wwPDB validation report: 94 clean, 136 worth a check and 137 with something to explain. Median clashscore 7.8, median RSRZ outliers 5.2%, median R-free minus R-work 0.038. 339 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 284 | 1.10 | 215 | 40% |
| Rattus norvegicus | 31 | 1.61 | 6 | 40% |
| unidentified | 13 | 1.90 | 10 | 36% |
| synthetic construct | 10 | 1.45 | 5 | 36% |
| Mus musculus | 9 | 1.50 | 4 | 36% |
| Pan troglodytes | 8 | 1.40 | 8 | 28% |
| Drosophila melanogaster | 3 | 1.95 | 0 | 8% |
| Unknown | 3 | 2.04 | 3 | 27% |
| Heliothis virescens | 1 | 11.60 | 2 | 8% |
| Escherichia phage EcSzw-2 | 1 | 1.55 | 1 | 27% |
| Escherichia coli BL21 | 1 | 2.10 | 1 | 27% |
| Escherichia coli BL21(DE3) | 1 | 2.29 | 1 | 28% |
920 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 |
| 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 | 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 | 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 | A hotspot for posttranslational modifications on the androgen receptor dimer interface drives pathology and anti-androgen resistance. Sci Adv doi:10.1126/sciadv.ade2175 |
| 2023 | A partially open conformation of an androgen receptor ligand-binding domain with drug-resistance mutations. Acta Crystallogr.,Sect.F doi:10.1107/S2053230X23002224 |
| 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 | 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 | 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 | Structure-Based Study to Overcome Cross-Reactivity of Novel Androgen Receptor Inhibitors. Cells doi:10.3390/cells11182785 |
| 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 | The multivalency of the glucocorticoid receptor ligand-binding domain explains its manifold physiological activities. Nucleic Acids Res. doi:10.1093/nar/gkac1119 |
| 2022 | Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism. Nature doi:10.1038/s41586-021-04252-1 |
| 2021 | Structural basis for glucocorticoid receptor recognition of both unmodified and methylated binding sites, precursors of a modern recognition element. Nucleic Acids Res. doi:10.1093/nar/gkab605 |
| 2021 | Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism. Nature doi:10.1038/s41586-021-04236-1 |
| 2021 | Discovery of a Novel Class of ERR alpha Agonists. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.1c00100 |
| 2020 | Disruption of a key ligand-H-bond network drives dissociative properties in vamorolone for Duchenne muscular dystrophy treatment. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2006890117 |
| 2020 | Structural basis for DNA recognition and allosteric control of the retinoic acid receptors RAR-RXR. Nucleic Acids Res. doi:10.1093/nar/gkaa697 |
| 2020 | Crystal structure of the mineralocorticoid receptor ligand-binding domain in complex with a potent and selective nonsteroidal blocker, esaxerenone (CS-3150). Febs Lett. doi:10.1002/1873-3468.13746 |
| 2020 | Structural basis of NR4A1 bound to the human pituitary proopiomelanocortin gene promoter. Biochem.Biophys.Res.Commun. doi:10.1016/j.bbrc.2019.11.192 |
| 2020 | Integrated Structural Modeling of Full-Length LRH-1 Reveals Inter-domain Interactions Contribute to Receptor Structure and Function Structure doi:10.1016/j.str.2020.04.020 |
| 2019 | Identification of Mineralocorticoid Receptor Modulators with Low Impact on Electrolyte Homeostasis but Maintained Organ Protection. J.Med.Chem. doi:10.1021/acs.jmedchem.8b01523 |
| 2019 | First High-Resolution Crystal Structures of the Glucocorticoid Receptor Ligand-Binding Domain-Peroxisome Proliferator-ActivatedgammaCoactivator 1-alphaComplex with Endogenous and Synthetic Glucocorticoids. Mol.Pharmacol. doi:10.1124/mol.119.116806 |
| 2019 | Modulation of RXR-DNA complex assembly by DNA context. Mol. Cell. Endocrinol. doi:10.1016/j.mce.2018.11.008 |
| 2019 | Structural basis of binding of homodimers of the nuclear receptor NR4A2 to selective Nur-responsive DNA elements. J.Biol.Chem. doi:10.1074/jbc.RA119.010730 |
| 2018 | Preclinical pharmacology of AZD9977: A novel mineralocorticoid receptor modulator separating organ protection from effects on electrolyte excretion. PLoS ONE doi:10.1371/journal.pone.0193380 |
| 2018 | Cryptic glucocorticoid receptor-binding sites pervade genomic NF-kappa B response elements. Nat Commun doi:10.1038/s41467-018-03780-1 |
| 2018 | Discovery of a Novel Oral Glucocorticoid Receptor Modulator (AZD9567) with Improved Side Effect Profile. J. Med. Chem. doi:10.1021/acs.jmedchem.7b01690 |
| 2018 | Probing Dominant Negative Behavior of Glucocorticoid Receptor beta through a Hybrid Structural and Biochemical Approach. Mol. Cell. Biol. doi:10.1128/MCB.00453-17 |
| 2018 | The first crystal structure of a DNA-free nuclear receptor DNA binding domain sheds light on DNA-driven allostery in the glucocorticoid receptor. Sci Rep doi:10.1038/s41598-018-31812-9 |
| 2018 | Discovery of a Potent and Selective Steroidal Glucocorticoid Receptor Antagonist (ORIC-101). J. Med. Chem. doi:10.1021/acs.jmedchem.8b00743 |
| 2017 | Synthesis and biological evaluation of novel selective androgen receptor modulators (SARMs) Part III: Discovery of 4-(5-oxopyrrolidine-1-yl)benzonitrile derivative 2f as a clinical candidate. Bioorg. Med. Chem. doi:10.1016/j.bmc.2017.04.018 |
| 2017 | Structure-Based Drug Design of Mineralocorticoid Receptor Antagonists to Explore Oxosteroid Receptor Selectivity. ChemMedChem doi:10.1002/cmdc.201600529 |
| 2017 | Selective Nonsteroidal Glucocorticoid Receptor Modulators for the Inhaled Treatment of Pulmonary Diseases. J. Med. Chem. doi:10.1021/acs.jmedchem.7b01215 |