CODSWALLOP

Bacteriorhodopsin

Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) · seed P02945 · 262 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.

284Entries 284Entities 114Constructs 42Organisms 277Ligand-bound
1.05 ÅBest res.
2.10 ÅMedian res.

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

The reference structure

6GA7, 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 6GA7
6GA7 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.

1131262283 constructs

Constructs, most-used first

114 distinct constructs across 284 entries. 219 polymer entities differ from the UniProt canonical sequence in some way, 26 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.

EntitiesLengthBest (Å)Best entryWhat was made
54 248 1.05 7Z09 residues 14-261
31 249 1.52 1P8H residues 14-262
13 262 1.43 1M0K matches the canonical sequence
12 229 1.60 7ZN3 matches the canonical sequence
10 291 1.70 5B0W L188I, M210I, N212S +6 more
6 231 1.66 9F9H residues 17-247; I17A
6 248 1.90 5JJE His7; residues 2-239
5 241 1.07 6S6C residues 7-247
4 228 1.25 5ZIM residues 18-245
4 229 1.29 5ZIL residues 18-246
4 230 1.33 7XJC residues 18-247
4 231 1.65 1KGB residues 14-244
4 234 1.58 7ZOU matches the canonical sequence
4 249 2.00 1MGY residues 14-262; D98S
4 283 1.70 8QLE no UniProt reference for this entity, so it cannot be diffed against a canonical sequence
4 327 2.44 8R0P matches the canonical sequence
3 253 2.10 2EI4 residues 7-259
3 261 2.15 5AHY His6; residues 20-274
2 71 residues 14-84
2 227 1.70 1F50 residues 18-244; E217Q
2 231 1.44 9F9G residues 17-247
2 232 1.90 6K6I matches the canonical sequence
2 249 1.62 1P8U residues 14-262; V62A
2 249 2.00 2I1X residues 14-262; D109A
2 250 2.10 4L35 matches the canonical sequence

Showing the 25 most-used of 114.

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".

M69A 36% Y144G 36% F167G 36% V186T 35% M45R 35% T60I 35% T68A 35% K172A 34% G129V 34% S206P 34% G168P 34% I130L 34% G133V 34% I211L 34% F67A 33% D115K 33% Q88E 33% Q118L 33% T170R 33% N215G 33% F243L 33% S196T 33% Y160V 33% F169L 33% F148Y 32% E174S 32% S227V 32% S145T 32% Y77Q 32% M81E 32%

What it assembles into

Oligomeric stateChainsEntriesShare
trimeric3 178 62.7%
monomeric1 77 27.1%
pentameric5 13 4.6%
dimeric2 7 2.5%
tetrameric4 6 2.1%
hexameric6 3 1.1%

192 entries have the depositor's assembly corroborated by PISA, 81 carry the depositor's word alone and 3 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 9 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1VJM, 2Z55, 3AM6, 3UTV, 3UTW, 3UTX, 3UTY, 4HWL, 5AZD.

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.

CATH1.10.287.170Rhodopsin 7-helix transmemSCOP2BG protein-coupled receptorG protein-coupled receptorG protein-coupled receptorG protein-coupled receptorG protein-coupled receptorG protein-coupled receptorG protein-coupled receptor1131262
DomainSourceSpan (seed)Chains
1.10.287.170CATH 15–83 2
Rhodopsin 7-helix transmembrane proteinsCATH 1.20.1070.10 18–245 208
G protein-coupled receptor-likeSCOP2B 8039329 19–244 166
G protein-coupled receptor-likeSCOP2B 8071318 19–262 6
G protein-coupled receptor-likeSCOP2B 8094347 19–259 5
G protein-coupled receptor-likeSCOP2B 8071304 23–255 3
G protein-coupled receptor-likeSCOP2B 8097220 28–262 4
G protein-coupled receptor-likeSCOP2B 8042369 29–248 6
G protein-coupled receptor-likeSCOP2B 8071306 32–259 5

What binds it

RET RET247 entries LFA LFA45 entries DD9 DD944 entries HP6 HP641 entries C14 C1438 entries MYS MYS32 entries SQU SQU18 entries 22B 22B15 entries R16 R1615 entries HEX HEX8 entries CPS CPS6 entries SQL SQL5 entries
ComponentClassNameEntriesBest (Å)
RETligand Retinal 247 1.07
L2Pcryoprotectant 2,3-Di-Phytanyl-Glycerol 60 1.22
LI1cryoprotectant 1-[2,6,10.14-Tetramethyl-Hexadecan-16-Yl]-2-[2,10,14-Trimethylhe 48 1.43
D10lipid/detergent Decane 46 1.43
LFAligand Eicosane 45 1.05
DD9ligand Nonane 44 1.07
OCTlipid/detergent N-Octane 43 1.70
HP6ligand Heptane 41 1.43
C14ligand Tetradecane 38 1.70
OLClipid/detergent (2r)-2,3-Dihydroxypropyl (9z)-Octadec-9-Enoate 36 1.05
TRDlipid/detergent Tridecane 33 1.70
UNDlipid/detergent Undecane 33 1.70
OLAlipid/detergent Oleic Acid 33 1.05
MYSligand Pentadecane 32 1.70
CLion Chloride Ion 21 1.07
SQUligand 2,10,23-Trimethyl-Tetracosane 18 1.33
L3Plipid/detergent 2,3-Di-O-Phytanly-3-Sn-Glycero-1-Phosphoryl-3'-Sn-Glycerol-1'-Ph 17 1.70
PO4ion Phosphate Ion 17 1.43
22Bligand Bacterioruberin 15 1.70
R16ligand Hexadecane 15 1.07

How it crystallises

Parsed from the free text 224 depositors typed into _exptl_crystal_grow.pdbx_details, out of 251 entries that recorded anything at all. Median pH 5.6 (range 2.0 to 10.0).

Precipitants

PEG × Ammonium sulfate × Sodium chloride × Sodium citrate × MPD × Ammonium phosphate × Lithium sulfate × Calcium chloride × Magnesium chloride × Tacsimate × Sodium malonate ×

Buffers

Phosphate × Citrate × HEPES × Sodium acetate × MES × Tris × Glycine × Bis-Tris × Imidazole ×

Which entries to trust

276 entries carry a wwPDB validation report: 122 clean, 83 worth a check and 71 with something to explain. Median clashscore 8.11, median RSRZ outliers 2.83%, median R-free minus R-work 0.032. 228 have released structure factors.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Halobacterium salinarum106 1.05 103 100%
Halobacterium salinarum NRC-166 1.25 64 100%
Bacillus coahuilensis13 1.60 13 78%
Natronomonas pharaonis12 1.80 12 97%
Haloquadratum walsbyi DSM 167908 1.85 8 90%
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)8 8 95%
Erythrobacter7 1.70 7 60%
Halorubrum sodomense6 1.07 6 90%
Mastigocladopsis repens5 1.90 5 82%
Synechocystis sp. PCC 75094 1.58 4 82%
Natronomonas pharaonis DSM 21604 1.70 4 90%
Halobacterium sp. AUS-24 1.80 4 97%

Seed sequence

262 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

1MLELLPTAVE GVSQAQITGR PEWIWLALGT ALMGLGTLYF LVKGMGVSDP DAKKFYAITT
61LVPAIAFTMY LSMLLGYGLT MVPFGGEQNP IYWARYADWL FTTPLLLLDL ALLVDADQGT
121ILALVGADGI MIGTGLVGAL TKVYSYRFVW WAISTAAMLY ILYVLFFGFT SKAESMRPEV
181ASTFKVLRNV TVVLWSAYPV VWLIGSEGAG IVPLNIETLL FMVLDVSAKV GFGLILLRSR
241AIFGEAEAPE PSAGDGAAAT SD

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 Structural, Mechanistic and Phylogenetic Insights Into a Freshwater Actinorhodopsin. J.Mol.Biol. doi:10.1016/j.jmb.2026.169725
2025 Engineering of soluble bacteriorhodopsin. Chem Sci doi:10.1039/d5sc02453f
2025 Microsecond Time-Resolved Cryo-EM Based on Jet Vitrification. Biorxiv doi:10.1101/2025.11.21.689681
2025 CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments. Sci Adv doi:10.1126/sciadv.adv1015
2025 Structural basis for no retinal binding in flotillin-associated rhodopsins. Structure doi:10.1016/j.str.2025.06.006
2025 Rhodopsin from Haloquadratum walsbyi is a light-driven magnesium transporter. Nat Commun doi:10.1038/s41467-025-59795-y
2025 Light-harvesting by antenna-containing xanthorhodopsin from an Antarctic Pseudanabaenaceae cyanobacterium. Commun Biol doi:10.1038/s42003-025-09294-z
2025 SecY translocon chaperones protein folding during membrane protein insertion. Cell doi:10.1016/j.cell.2025.01.037
2024 Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate. Nat Commun doi:10.1038/s41467-024-54422-8
2024 A subgroup of light-driven sodium pumps with an additional Schiff base counterion. Nat Commun doi:10.1038/s41467-024-47469-0
2024 Cyanorhodopsin-II represents a yellow-absorbing proton-pumping rhodopsin clade within cyanobacteria. Isme J doi:10.1093/ismejo/wrae175
2024 Light-driven anion-pumping rhodopsin with unique cytoplasmic anion-release mechanism. J.Biol.Chem. doi:10.1016/j.jbc.2024.107797
2023 Detailed analysis of distorted retinal and its interaction with surrounding residues in the K intermediate of bacteriorhodopsin Commun Biol doi:10.1038/s42003-023-04554-2
2023 Mechanisms of inward transmembrane proton translocation. Nat.Struct.Mol.Biol. doi:10.1038/s41594-023-01020-9
2023 A versatile approach to high-density microcrystals in lipidic cubic phase for room-temperature serial crystallography. J.Appl.Crystallogr. doi:10.1107/S1600576723006428
2023 Phototrophy by antenna-containing rhodopsin pumps in aquatic environments. Nature doi:10.1038/s41586-023-05774-6
2023 Mirror proteorhodopsins. Commun Chem doi:10.1038/s42004-023-00884-8
2022 True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins. Nat.Struct.Mol.Biol. doi:10.1038/s41594-022-00762-2
2022 Structural insights into light-driven anion pumping in cyanobacteria. Nat Commun doi:10.1038/s41467-022-34019-9
2022 High-pressure crystallography shows noble gas intervention into protein-lipid interaction and suggests a model for anaesthetic action. Commun Biol doi:10.1038/s42003-022-03233-y
2022 Two states of a light-sensitive membrane protein captured at room temperature using thin-film sample mounts. Acta Crystallogr D Struct Biol doi:10.1107/S2059798321011220
2022 Structural characterization of proton-pumping rhodopsin lacking a cytoplasmic proton donor residue by X-ray crystallography. J.Biol.Chem. doi:10.1016/j.jbc.2022.101722
2022 Photoinduced isomerization sampling of retinal in bacteriorhodopsin PNAS Nexus doi:10.1093/pnasnexus/pgac103
2022 Directional Proton Conductance in Bacteriorhodopsin Is Driven by Concentration Gradient, Not Affinity Gradient
2021 Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization. Nat Commun doi:10.1038/s41467-020-20596-0
2021 Structure-based insights into evolution of rhodopsins. Commun Biol doi:10.1038/s42003-021-02326-4
2021 Heavy Atom Detergent/Lipid Combined X-ray Crystallography for Elucidating the Structure-Function Relationships of Membrane Proteins. Membranes (Basel) doi:10.3390/membranes11110823
2020 How Does a Microbial Rhodopsin RxR Realize Its Exceptionally High Thermostability with the Proton-Pumping Function Being Retained? J.Phys.Chem.B doi:10.1021/acs.jpcb.9b10700
2020 A unique clade of light-driven proton-pumping rhodopsins evolved in the cyanobacterial lineage. Sci Rep doi:10.1038/s41598-020-73606-y
2020 The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants. J.Biol.Chem. doi:10.1074/jbc.RA120.014118
2019 Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin. Nat Commun doi:10.1038/s41467-019-10758-0
2019 Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science doi:10.1126/science.aaw8634
2019 Design of a light-gated proton channel based on the crystal structure ofCoccomyxarhodopsin. Sci.Signal. doi:10.1126/scisignal.aav4203
2019 X-ray Crystallographic Structure and Oligomerization of Gloeobacter Rhodopsin. Sci Rep doi:10.1038/s41598-019-47445-5
2018 X-ray structure analysis of bacteriorhodopsin at 1.3 angstrom resolution. Sci Rep doi:10.1038/s41598-018-31370-0
2018 Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science doi:10.1126/science.aat0094
2017 Integral Membrane Proteins Can Be Crystallized Directly from Nanodiscs Cryst.Growth Des. doi:10.1021/acs.cgd.6b01631
2017 New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex. Sci Rep doi:10.1038/srep41811
2017 Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs. Structure doi:10.1016/j.str.2016.12.004
2017 Chemically Stable Lipids for Membrane Protein Crystallization. Cryst Growth Des doi:10.1021/acs.cgd.7b00458