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
Open in CODSWALLOP UniProt P02945 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 1.10.287.170 CATH 1.20.1070.10 SCOP 8039329 SCOP 8071318 SCOP 8094347 SCOP 8071304 SCOP 8097220 SCOP 8042369 SCOP 8071306 RCSB 6GA7 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.
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.
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.
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.
| Entities | Length | Best (Å) | Best entry | What 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.
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 |
|---|---|---|---|
| trimeric | 3 | 178 | 62.7% |
| monomeric | 1 | 77 | 27.1% |
| pentameric | 5 | 13 | 4.6% |
| dimeric | 2 | 7 | 2.5% |
| tetrameric | 4 | 6 | 2.1% |
| hexameric | 6 | 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.
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 |
|---|---|---|---|
| 1.10.287.170 | CATH | 15–83 | 2 |
| Rhodopsin 7-helix transmembrane proteins | CATH 1.20.1070.10 | 18–245 | 208 |
| G protein-coupled receptor-like | SCOP2B 8039329 | 19–244 | 166 |
| G protein-coupled receptor-like | SCOP2B 8071318 | 19–262 | 6 |
| G protein-coupled receptor-like | SCOP2B 8094347 | 19–259 | 5 |
| G protein-coupled receptor-like | SCOP2B 8071304 | 23–255 | 3 |
| G protein-coupled receptor-like | SCOP2B 8097220 | 28–262 | 4 |
| G protein-coupled receptor-like | SCOP2B 8042369 | 29–248 | 6 |
| G protein-coupled receptor-like | SCOP2B 8071306 | 32–259 | 5 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| RET | ligand | Retinal | 247 | 1.07 |
| L2P | cryoprotectant | 2,3-Di-Phytanyl-Glycerol | 60 | 1.22 |
| LI1 | cryoprotectant | 1-[2,6,10.14-Tetramethyl-Hexadecan-16-Yl]-2-[2,10,14-Trimethylhe | 48 | 1.43 |
| D10 | lipid/detergent | Decane | 46 | 1.43 |
| LFA | ligand | Eicosane | 45 | 1.05 |
| DD9 | ligand | Nonane | 44 | 1.07 |
| OCT | lipid/detergent | N-Octane | 43 | 1.70 |
| HP6 | ligand | Heptane | 41 | 1.43 |
| C14 | ligand | Tetradecane | 38 | 1.70 |
| OLC | lipid/detergent | (2r)-2,3-Dihydroxypropyl (9z)-Octadec-9-Enoate | 36 | 1.05 |
| TRD | lipid/detergent | Tridecane | 33 | 1.70 |
| UND | lipid/detergent | Undecane | 33 | 1.70 |
| OLA | lipid/detergent | Oleic Acid | 33 | 1.05 |
| MYS | ligand | Pentadecane | 32 | 1.70 |
| CL | ion | Chloride Ion | 21 | 1.07 |
| SQU | ligand | 2,10,23-Trimethyl-Tetracosane | 18 | 1.33 |
| L3P | lipid/detergent | 2,3-Di-O-Phytanly-3-Sn-Glycero-1-Phosphoryl-3'-Sn-Glycerol-1'-Ph | 17 | 1.70 |
| PO4 | ion | Phosphate Ion | 17 | 1.43 |
| 22B | ligand | Bacterioruberin | 15 | 1.70 |
| R16 | ligand | Hexadecane | 15 | 1.07 |
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).
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.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Halobacterium salinarum | 106 | 1.05 | 103 | 100% |
| Halobacterium salinarum NRC-1 | 66 | 1.25 | 64 | 100% |
| Bacillus coahuilensis | 13 | 1.60 | 13 | 78% |
| Natronomonas pharaonis | 12 | 1.80 | 12 | 97% |
| Haloquadratum walsbyi DSM 16790 | 8 | 1.85 | 8 | 90% |
| Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) | 8 | 8 | 95% | |
| Erythrobacter | 7 | 1.70 | 7 | 60% |
| Halorubrum sodomense | 6 | 1.07 | 6 | 90% |
| Mastigocladopsis repens | 5 | 1.90 | 5 | 82% |
| Synechocystis sp. PCC 7509 | 4 | 1.58 | 4 | 82% |
| Natronomonas pharaonis DSM 2160 | 4 | 1.70 | 4 | 90% |
| Halobacterium sp. AUS-2 | 4 | 1.80 | 4 | 97% |
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
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 | 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 |