CODSWALLOP

Rhodopsin

Homo sapiens · seed P08100 · 348 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026

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.

103Entries 104Entities 38Constructs 7Organisms 70Ligand-bound
1.80 ÅBest res.
3.00 ÅMedian res.

Every figure here is counted over the whole family rather than quoted from one entry.

The reference structure

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.

Rendered structure of 4ZWJ
4ZWJ at the RCSB · open it in the 3D viewer

Which residues anyone has ever seen

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.

1174348100 constructs

Constructs, most-used first

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.

EntitiesLengthBest (Å)Best entryWhat 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.

Positions people deliberately mutate

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".

N2C 48% F56A 26% A124G 25% N111V 25% F116T 25% A117D 25% G120C 25% E122I 25% I123S 25% E113Q 24% E5Q 24% G90A 23% S22G 23% T319K 23% T320L 23% M207L 22% V210T 22% H211C 22% I217Y 22% F220I 22% F228R 22% T229A 22% E232Q 22% I255V 22% I256V 22% M257Y 22% I259L 22% L262C 22% I263L 22% M317I 22%

What it assembles into

Oligomeric stateChainsEntriesShare
dimeric2 35 34.0%
monomeric1 31 30.1%
pentameric5 13 12.6%
tetrameric4 11 10.7%
hexameric6 3 2.9%
56-meric56 3 2.9%
trimeric3 3 2.9%
heptameric7 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.

Domain architecture

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.

CATH1.10.530.40Rhodopsin 7-helix transmemSCOP2BLysozyme-likeG protein-coupled receptorG protein-coupled receptorCytochromes1174348
DomainSourceSpan (seed)Chains
1.10.530.40CATH 1–348 2
Rhodopsin 7-helix transmembrane proteinsCATH 1.20.1070.10 2–327 46
Lysozyme-likeSCOP2B 8033861 1–160 4
G protein-coupled receptor-likeSCOP2B 8042778 2–327 56
G protein-coupled receptor-likeSCOP2B 8070800 161–348 3
CytochromesSCOP2B 8057879 251–348 5

What binds it

RET RET47 entries NAG NAG10 entries HTO HTO7 entries ACE ACE6 entries DAO DAO5 entries SGV SGV4 entries HSM HSM3 entries BGL BGL1 entries 4E6 4E61 entries ID3 ID31 entries 7AB 7AB1 entries DOK DOK1 entries
ComponentClassNameEntriesBest (Å)
RETligand Retinal 47 1.80
PLMlipid/detergent Palmitic Acid 42 1.80
BOGlipid/detergent Octyl Beta-D-Glucopyranoside 25 2.30
ZNion Zinc Ion 15 2.20
NAGcofactor 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose 10 1.80
SO4ion Sulfate Ion 10 2.30
ACTcryoprotectant Acetate Ion 9 2.30
HGion Mercury (Ii) Ion 8 2.20
HTOligand Heptane-1,2,3-Triol 7 2.20
CLRlipid/detergent Cholesterol 7 2.60
ACEligand Acetyl Group 6 1.80
HTGlipid/detergent Heptyl 1-Thio-Beta-D-Glucopyranoside 5 2.20
MGion Magnesium Ion 5 2.69
DAOligand Lauric Acid 5 1.80
OLClipid/detergent (2r)-2,3-Dihydroxypropyl (9z)-Octadec-9-Enoate 5 1.80
SGVligand Sangivamycin 4 4.00
PEFlipid/detergent Di-Palmitoyl-3-Sn-Phosphatidylethanolamine 3 2.65
BNGlipid/detergent Nonyl Beta-D-Glucopyranoside 3 2.29
HSMligand Histamine 3 2.70
C8Elipid/detergent (Hydroxyethyloxy)tri(Ethyloxy)octane 2 2.65

How it crystallises

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).

Precipitants

Ammonium sulfate × PEG × Lithium sulfate × Sodium citrate ×

Buffers

Sodium acetate × MES × Citrate × HEPES × Sodium cacodylate ×

Which entries to trust

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.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Bos taurus70 1.80 48 100%
Homo sapiens18 2.48 18 99%
Unknown6 1 100%
Macaca fascicularis3 3.21 3 98%
Enterobacteria phage RB551 3.01 0 100%
Oryctolagus cuniculus2 3.25 0 40%
Tequatrovirus T42 3.30 0 100%
Escherichia coli1 4.50 0 93%

Seed sequence

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

1MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
61VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG
121GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP
181EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES
241ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI
301YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA

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.

Primary citations

One record per paper, not per entry.

YearCitation
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