Homo sapiens · seed P08100 · 348 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P08100 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 1.10.530.40 CATH 1.20.1070.10 SCOP 8033861 SCOP 8042778 SCOP 8070800 SCOP 8057879 RCSB 4ZWJ 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.
4ZWJ, 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.
38 distinct constructs across 103 entries. 57 polymer entities differ from the UniProt canonical sequence in some way, 14 carry a recognised expression tag and 8 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 |
|---|---|---|---|---|
| 33 | 348 | 1.80 | 7ZBC | matches the canonical sequence |
| 13 | 349 | 1.80 | 8A6E | matches the canonical sequence |
| 7 | 349 | 2.46 | 6FKC | N2C, D282C |
| 4 | 229 | 2.69 | 8RJB | Strep-II; residues 1-129; 1 internal deletion; M1Q, G3L, T4K +37 more |
| 4 | 348 | 3.21 | 8P12 | N2C, M257Y, D282C |
| 4 | 659 | 2.70 | 8YN5 | His8; TEV site |
| 2 | 349 | 2.30 | 5DYS | N2C, T94I, D282C |
| 2 | 349 | 2.90 | 4BEY | N2C, G90D, D282C |
| 2 | 389 | 2.59 | 9W32 | 1 internal deletion; M1L, R2L, K3V +25 more |
| 2 | 461 | 2.70 | 8YUU | FLAG; 3C/PreScission site |
| 2 | 488 | 3.06 | 9QP4 | FLAG; fused to BRIL (internal); 3C/PreScission site; 8-residue insertion after 231; Q231A |
| 2 | 906 | 3.01 | 5W0P | fused to T4 lysozyme; residues 4-348; E113Q, M257Y, N282C |
| 2 | 906 | 3.30 | 4ZWJ | fused to T4 lysozyme; residues 4-348; E113Q, M257Y, N282C |
| 1 | 25 | residues 291-315 | ||
| 1 | 26 | residues 268-293 | ||
| 1 | 31 | residues 93-123 | ||
| 1 | 34 | residues 172-205 | ||
| 1 | 40 | residues 1-40; Q36E | ||
| 1 | 273 | 3.88 | 7TUT | no UniProt reference for this entity, so it cannot be diffed against a canonical sequence |
| 1 | 316 | 3.12 | 6FUF | residues 2-317; N2C, M257Y, D282C |
| 1 | 323 | 3.10 | 9NYX | residues 1-322 |
| 1 | 327 | 2.36 | 6FK6 | residues 1-326; N2C, D282C |
| 1 | 329 | 3.03 | 6FKB | residues 1-328; N2C, D282C |
| 1 | 348 | 2.61 | 8Y02 | E107Q |
| 1 | 348 | 3.40 | 3C9M | N2C, D282C |
Showing the 25 most-used of 38.
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 | 35 | 34.0% |
| monomeric | 1 | 31 | 30.1% |
| pentameric | 5 | 13 | 12.6% |
| tetrameric | 4 | 11 | 10.7% |
| hexameric | 6 | 3 | 2.9% |
| 56-meric | 56 | 3 | 2.9% |
| trimeric | 3 | 3 | 2.9% |
| heptameric | 7 | 2 | 1.9% |
44 entries have the depositor's assembly corroborated by PISA, 52 carry the depositor's word alone and 7 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 7 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1F88, 1HZX, 1L9H, 3OAX, 3PQR, 5TE3, 6PH7.
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 |
|---|---|---|---|
| 1.10.530.40 | CATH | 1–348 | 2 |
| Rhodopsin 7-helix transmembrane proteins | CATH 1.20.1070.10 | 2–327 | 46 |
| Lysozyme-like | SCOP2B 8033861 | 1–160 | 4 |
| G protein-coupled receptor-like | SCOP2B 8042778 | 2–327 | 56 |
| G protein-coupled receptor-like | SCOP2B 8070800 | 161–348 | 3 |
| Cytochromes | SCOP2B 8057879 | 251–348 | 5 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| RET | ligand | Retinal | 47 | 1.80 |
| PLM | lipid/detergent | Palmitic Acid | 42 | 1.80 |
| BOG | lipid/detergent | Octyl Beta-D-Glucopyranoside | 25 | 2.30 |
| ZN | ion | Zinc Ion | 15 | 2.20 |
| NAG | cofactor | 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose | 10 | 1.80 |
| SO4 | ion | Sulfate Ion | 10 | 2.30 |
| ACT | cryoprotectant | Acetate Ion | 9 | 2.30 |
| HG | ion | Mercury (Ii) Ion | 8 | 2.20 |
| HTO | ligand | Heptane-1,2,3-Triol | 7 | 2.20 |
| CLR | lipid/detergent | Cholesterol | 7 | 2.60 |
| ACE | ligand | Acetyl Group | 6 | 1.80 |
| HTG | lipid/detergent | Heptyl 1-Thio-Beta-D-Glucopyranoside | 5 | 2.20 |
| MG | ion | Magnesium Ion | 5 | 2.69 |
| DAO | ligand | Lauric Acid | 5 | 1.80 |
| OLC | lipid/detergent | (2r)-2,3-Dihydroxypropyl (9z)-Octadec-9-Enoate | 5 | 1.80 |
| SGV | ligand | Sangivamycin | 4 | 4.00 |
| PEF | lipid/detergent | Di-Palmitoyl-3-Sn-Phosphatidylethanolamine | 3 | 2.65 |
| BNG | lipid/detergent | Nonyl Beta-D-Glucopyranoside | 3 | 2.29 |
| HSM | ligand | Histamine | 3 | 2.70 |
| C8E | lipid/detergent | (Hydroxyethyloxy)tri(Ethyloxy)octane | 2 | 2.65 |
Parsed from the free text 52 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 52
entries that recorded anything at all.
Median pH 6.0
(range 4.5 to 9.0).
103 entries carry a wwPDB validation report: 39 clean, 31 worth a check and 33 with something to explain. Median clashscore 6.43, median RSRZ outliers 8.59%, median R-free minus R-work 0.029. 95 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Bos taurus | 70 | 1.80 | 48 | 100% |
| Homo sapiens | 18 | 2.48 | 18 | 99% |
| Unknown | 6 | 1 | 100% | |
| Macaca fascicularis | 3 | 3.21 | 3 | 98% |
| Enterobacteria phage RB55 | 1 | 3.01 | 0 | 100% |
| Oryctolagus cuniculus | 2 | 3.25 | 0 | 40% |
| Tequatrovirus T4 | 2 | 3.30 | 0 | 100% |
| Escherichia coli | 1 | 4.50 | 0 | 93% |
348 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 | Cryo-electron microscopy structures of human cone visual pigments Science doi:10.1126/science.adz8141 |
| 2026 | Biophysical and structural analysis of human green cone opsin. Biophys.J. doi:10.1016/j.bpj.2026.03.029 |
| 2026 | Decoding ligand recognition and constitutive activation of histamine H3 and H4 receptors. Acta Pharmacol.Sin. doi:10.1038/s41401-025-01633-4 |
| 2026 | Illuminating the molecular basis of human daylight vision. Science doi:10.1126/science.adz3624 |
| 2026 | Structural analysis of rhodopsin states in megabody complexes. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2532336123 |
| 2026 | Structural insights into spectral tuning and retinal exchange in cone visual pigments. Science doi:10.1126/science.adz3996 |
| 2025 | Structural insights into nonpeptide antagonist inhibition of somatostatin receptor subtype 5. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2522515122 |
| 2025 | Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2516318122 |
| 2025 | Tool antibody fragments reveal multiple conformations of the rhodopsin-Gi signaling complex. Biophys.J. doi:10.1016/j.bpj.2025.09.044 |
| 2024 | Structural analysis of the dynamic ribosome-translocon complex. Elife doi:10.7554/eLife.95814 |
| 2024 | Structural basis of ligand recognition and activation of the histamine receptor family. Nat Commun doi:10.1038/s41467-024-52585-y |
| 2024 | Molecular Determinant Underlying Selective Coupling of Primary G-Protein by Class A GPCRs. Adv Sci doi:10.1002/advs.202310120 |
| 2023 | Ultrafast structural changes direct the first molecular events of vision. Nature doi:10.1038/s41586-023-05863-6 |
| 2023 | Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain. Nat Commun doi:10.1038/s41467-023-40911-9 |
| 2022 | Structural basis for recognition of antihistamine drug by human histamine receptor. Nat Commun doi:10.1038/s41467-022-33880-y |
| 2022 | Mechanism of an intramembrane chaperone for multipass membrane proteins. Nature doi:10.1038/s41586-022-05336-2 |
| 2021 | Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1. Nature doi:10.1038/s41586-021-03721-x |
| 2019 | Structures of the Rhodopsin-Transducin Complex: Insights into G-Protein Activation. Mol.Cell doi:10.1016/j.molcel.2019.06.007 |
| 2019 | Cryo-EM structure of the rhodopsin-G alpha i-beta gamma complex reveals binding of the rhodopsin C-terminal tail to the G beta subunit. Elife doi:10.7554/eLife.46041 |
| 2019 | Cryo-EM structure of the native rhodopsin dimer in nanodiscs. J.Biol.Chem. doi:10.1074/jbc.RA119.010089 |
| 2018 | Ligand channel in pharmacologically stabilized rhodopsin. Proc. Natl. Acad. Sci. U.S.A. doi:10.1073/pnas.1718084115 |
| 2018 | Crystal structure of rhodopsin in complex with a mini-Gosheds light on the principles of G protein selectivity. Sci Adv doi:10.1126/sciadv.aat7052 |
| 2018 | High-throughput in situ X-ray screening of and data collection from protein crystals at room temperature and under cryogenic conditions. Nat Protoc doi:10.1038/nprot.2017.135 |
| 2018 | Cryo-EM structure of human rhodopsin bound to an inhibitory G protein. Nature doi:10.1038/s41586-018-0215-y |
| 2017 | Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism. Proc. Natl. Acad. Sci. U.S.A. doi:10.1073/pnas.1617446114 |
| 2017 | Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors. Cell doi:10.1016/j.cell.2017.07.002 |
| 2016 | Structural role of the T94I rhodopsin mutation in congenital stationary night blindness. Embo Rep. doi:10.15252/embr.201642671 |
| 2016 | X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex. Sci Data doi:10.1038/sdata.2016.21 |
| 2015 | The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation. Structure doi:10.1016/j.str.2015.09.015 |
| 2015 | Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature doi:10.1038/nature14656 |
| 2014 | Crystal structure of a common GPCR-binding interface for G protein and arrestin. Nat Commun doi:10.1038/ncomms5801 |
| 2013 | Opsin, a structural model for olfactory receptors? Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.201302374 |
| 2013 | Insights Into Congenital Stationary Night Blindness Based on the Structure of G90D Rhodopsin. Embo Rep. doi:10.1038/EMBOR.2013.44 |
| 2012 | Stabilized G Protein Binding Site in the Structure of Constitutively Active Metarhodopsin-II. Proc.Natl.Acad.Sci.USA doi:10.1073/PNAS.1114089108 |
| 2011 | Crystal structure of metarhodopsin II. Nature doi:10.1038/nature09789 |
| 2011 | The Structural Basis of Agonist Induced Activation in Constitutively Active Rhodopsin Nature doi:10.1038/NATURE09795 |
| 2010 | Binding of more than one retinoid to visual opsins Biophys.J. doi:10.1016/j.bpj.2010.08.003 |
| 2008 | Alternative models for two crystal structures of bovine rhodopsin. Acta Crystallogr.,Sect.D doi:10.1107/S0907444908017162 |
| 2008 | Crystal structure of the ligand-free G-protein-coupled receptor opsin Nature doi:10.1038/nature07063 |
| 2008 | Crystal structure of opsin in its G-protein-interacting conformation Nature doi:10.1038/nature07330 |