Bos taurus · seed P61823 · 150 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P61823 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.10.130.10 SCOP 8038165 SCOP 8034213 SCOP 8038842 SCOP 8035353 SCOP 8040055 RCSB 1RAS 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.
1RAS, 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.
149 distinct constructs across 500 entries. 488 polymer entities differ from the UniProt canonical sequence in some way, 10 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 |
|---|---|---|---|---|
| 245 | 124 | 0.85 | 6ETK | residues 27-150 |
| 24 | 135 | 0.94 | 9R6D | residues 27-161; V27M |
| 21 | 104 | 1.22 | 4O36 | residues 47-150 |
| 14 | 124 | 1.45 | 1N1X | residues 27-150 |
| 10 | 123 | 1.76 | 8OO3 | residues 25-147 |
| 7 | 101 | 1.76 | 9GF9 | residues 50-150 |
| 4 | 128 | 1.04 | 6ENP | residues 23-150; A23M |
| 4 | 128 | 1.50 | 3MZQ | residues 23-150 |
| 3 | 118 | 1.80 | 1SRN | residues 27-144 |
| 3 | 124 | 1.40 | 3DIB | residues 27-150; I132A |
| 3 | 124 | 2.25 | 3BCM | residues 27-150; P45A, L54Q, N93D |
| 3 | 125 | 1.45 | 4WYZ | residues 26-150; G26M, A135G |
| 3 | 147 | 2.80 | 9BDL | matches the canonical sequence |
| 2 | 113 | 2.00 | 3SRN | residues 27-139 |
| 2 | 120 | 2.10 | 1RNF | residues 28-147; G28M |
| 2 | 121 | 1.35 | 5EOP | residues 26-146 |
| 2 | 121 | 1.50 | 2BWK | residues 25-145 |
| 2 | 123 | 1.70 | 1RAS | residues 28-150 |
| 2 | 123 | 1.80 | 1K59 | residues 25-147; Q141G |
| 2 | 124 | 0.87 | 1DY5 | residues 27-150; N93D |
| 2 | 124 | 1.29 | 3QL1 | residues 27-150; A30C, D109E, V144C |
| 2 | 124 | 1.60 | 3FL3 | residues 27-150; A45P, Q54L, K57C +1 more |
| 2 | 124 | 2.00 | 3RSK | residues 27-150; K33A, R36A, K92A |
| 2 | 124 | 2.10 | 3RH1 | residues 27-150; P140A |
| 2 | 124 | residues 27-150; N93D |
Showing the 25 most-used of 149.
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 |
|---|---|---|---|
| monomeric | 1 | 373 | 74.6% |
| dimeric | 2 | 114 | 22.8% |
| tetrameric | 4 | 6 | 1.2% |
| trimeric | 3 | 2 | 0.4% |
| hexameric | 6 | 1 | 0.2% |
| heptameric | 7 | 1 | 0.2% |
| 82-meric | 82 | 1 | 0.2% |
| 85-meric | 85 | 1 | 0.2% |
255 entries have the depositor's assembly corroborated by PISA, 241 carry the depositor's word alone and 4 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 33 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 11BG, 1BSR, 1CJQ, 1FEV, 1J7Z, 1J80, 1J81, 1RBE, 1RBG, 1RBH, 1RNM, 1Z3L, 1Z3M, 1Z6D, 2E0L, 2E0M, 2E0O, 2ZPO, 3BCP, 3DH5.
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 |
|---|---|---|---|
| Ribonuclease A-like domain | CATH 3.10.130.10 | 27–150 | 383 |
| RNase A-like | SCOP2B 8038165 | 27–150 | 309 |
| RNase A-like | SCOP2B 8034213 | 27–150 | 21 |
| RNase A-like | SCOP2B 8038842 | 30–150 | 25 |
| RNase A-like | SCOP2B 8035353 | 35–150 | 10 |
| RNase A-like | SCOP2B 8040055 | 36–150 | 46 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| SO4 | ion | Sulfate Ion | 131 | 0.85 |
| CL | ion | Chloride Ion | 72 | 1.01 |
| PO4 | ion | Phosphate Ion | 25 | 1.04 |
| ACT | cryoprotectant | Acetate Ion | 23 | 0.87 |
| NA | ion | Sodium Ion | 21 | 0.94 |
| GOL | cryoprotectant | Glycerol | 20 | 1.49 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 18 | 1.01 |
| CIT | buffer | Citric Acid | 16 | 1.17 |
| FMT | buffer | Formic Acid | 16 | 0.94 |
| IPA | cryoprotectant | Isopropyl Alcohol | 14 | 0.85 |
| TAR | buffer | D(-)-Tartaric Acid | 11 | 1.04 |
| EDO | cryoprotectant | 1,2-Ethanediol | 9 | 1.02 |
| TLA | buffer | L(+)-Tartaric Acid | 9 | 1.04 |
| PT | ion | Platinum (Ii) Ion | 9 | 1.76 |
| AMP | cofactor | Adenosine Monophosphate | 8 | 1.50 |
| ACY | cryoprotectant | Acetic Acid | 7 | 0.98 |
| ZN | ion | Zinc Ion | 7 | 1.04 |
| F3I | ligand | (Mi2-Acetato-O, O')-Hexaaquo-Dirhodium (Ii) | 6 | 1.15 |
| MPD | cryoprotectant | (4s)-2-Methyl-2,4-Pentanediol | 5 | 1.40 |
| DMS | cryoprotectant | Dimethyl Sulfoxide | 5 | 1.76 |
Parsed from the free text 404 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 429
entries that recorded anything at all.
Median pH 5.5
(range 2.0 to 9.0).
500 entries carry a wwPDB validation report: 171 clean, 184 worth a check and 145 with something to explain. Median clashscore 6.57, median RSRZ outliers 4.62%, median R-free minus R-work 0.041. 403 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Bos taurus | 362 | 0.85 | 143 | 100% |
| Homo sapiens | 96 | 0.98 | 19 | 93% |
| Escherichia coli 'BL21-Gold(DE3)pLysS AG | 11 | 0.94 | 6 | 79% |
| Mus musculus | 6 | 1.50 | 0 | 93% |
| synthetic construct | 5 | 1.14 | 0 | 81% |
| Sus scrofa | 4 | 1.25 | 2 | 77% |
| Rattus norvegicus | 3 | 1.78 | 0 | 82% |
| Gallus gallus | 2 | 1.76 | 1 | 83% |
| Lithobates pipiens | 2 | 1.80 | 0 | 76% |
| Salmo salar | 2 | 1.89 | 0 | 78% |
| Arabidopsis thaliana | 2 | 3.50 | 0 | 14% |
| Chelonia mydas | 1 | 1.60 | 0 | 82% |
150 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 basis for saccharide binding by human RNase 2/EDN, a protein combining enzymatic and lectin properties Biorxiv doi:10.64898/2026.03.20.713198 |
| 2026 | Engineering human RNase 7 with an eosinophil RNase segment reveals determinants of cytotoxic and antimicrobial activity. J.Biol.Chem. doi:10.1016/j.jbc.2026.113189 |
| 2025 | Pseudouridine residues as substrates for serum ribonucleases. Rna doi:10.1261/rna.080404.125 |
| 2025 | Guanidinium-Stapled Helical Peptides for Targeting Protein-Protein Interactions. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202416348 |
| 2025 | Cytotoxicity and Binding to DNA, Lysozyme, Ribonuclease A, and Human Serum Albumin of the Diiodido Analog of Picoplatin. Inorg.Chem. doi:10.1021/acs.inorgchem.4c05424 |
| 2024 | Exchange of equatorial ligands in protein-bound paddlewheel Ru25+ complexes: new insights from X-ray crystallography and quantum chemistry Inorg Chem Front doi:10.1039/D4QI01846J |
| 2024 | Prolinyl Phosphoramidates of Nucleotides with Increased Reactivity. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202319958 |
| 2024 | Pentaphosphorylation via the Anhydride of Dihydrogen Pentametaphosphate: Access to Nucleoside Hexa- and Heptaphosphates and Study of Their Interaction with Ribonuclease A. Acs Cent.Sci. doi:10.1021/acscentsci.4c00835 |
| 2024 | Ancestral sequence reconstruction dissects structural and functional differences among eosinophil ribonucleases. J.Biol.Chem. doi:10.1016/j.jbc.2024.107280 |
| 2024 | Deciphering the role of neutral diruthenium complexes in protein binding. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2024.137691 |
| 2024 | Picoplatin binding to proteins: X-ray structures and mass spectrometry data on the adducts with lysozyme and ribonuclease A. Dalton Trans doi:10.1039/d4dt00773e |
| 2024 | P-Stereodefined morpholino dinucleoside 3',5'-phosphorothioates. Org.Biomol.Chem. doi:10.1039/d4ob01437e |
| 2024 | Cyanide mediated conformational changes resulted in the displacement of sulfate ion from the active site of bovine pancreatic ribonuclease A. Biochem.Biophys.Res.Commun. doi:10.1016/j.bbrc.2024.150868 |
| 2024 | Structural mechanism of angiogenin activation by the ribosome. Nature doi:10.1038/s41586-024-07508-8 |
| 2024 | The cryo-EM structure of the BoNT/Wo-NTNH complex reveals two immunoglobulin-like domains. Febs J. doi:10.1111/febs.16964 |
| 2023 | Ultra-high resolution X-ray structure of orthorhombic bovine pancreatic Ribonuclease A at 100K. BMC Chem doi:10.1186/s13065-023-00959-6 |
| 2023 | Ruthenium(II)–Arene Complexes with Glycosylated NHC-Carbene Co-Ligands: Synthesis, Hydrolytic Behavior, and Binding to Biological Molecules Organometallics doi:10.1021/acs.organomet.3c00128 |
| 2023 | Cross-Linked Crystals of Dirhodium Tetraacetate/RNase A Adduct Can Be Used as Heterogeneous Catalysts. Inorg.Chem. doi:10.1021/acs.inorgchem.3c00852 |
| 2023 | Interaction of VIVO-8-hydroxyquinoline species with RNase A: the effect of metal ligands in the protein adduct stabilization Inorg Chem Front doi:10.1039/D3QI01023F |
| 2023 | Structural and Biochemical Characterization of the Human Angiogenin-Proliferating Cell Nuclear Antigen Interaction. Biochemistry doi:10.1021/acs.biochem.3c00158 |
| 2023 | Cisplatin binding to angiogenin protein: new molecular pathways and targets for the drug's anticancer activity. Dalton Trans doi:10.1039/d3dt01517c |
| 2023 | Experimental phasing opportunities for macromolecular crystallography at very long wavelengths. Commun Chem doi:10.1038/s42004-023-01014-0 |
| 2022 | Exploring the RNase A scaffold to combine catalytic and antimicrobial activities. Structural characterization of RNase 3/1 chimeras. Front Mol Biosci doi:10.3389/fmolb.2022.964717 |
| 2022 | Reactivity of a fluorine-containing dirhodium tetracarboxylate compound with proteins. Dalton Trans doi:10.1039/d2dt00082b |
| 2022 | Unexpected Imidazole Coordination to the Dirhodium Center in a Protein Environment: Insights from X-ray Crystallography and Quantum Chemistry. Inorg.Chem. doi:10.1021/acs.inorgchem.2c01370 |
| 2022 | Halo complexes of gold(I) containing glycoconjugate carbene ligands: synthesis, characterization, cytotoxicity and interaction with proteins and DNA model systems. Dalton Trans doi:10.1039/d2dt00423b |
| 2022 | Oxaliplatin inhibits angiogenin proliferative and cell migration effects in prostate cancer cells. J.Inorg.Biochem. doi:10.1016/j.jinorgbio.2021.111657 |
| 2022 | Structure of angiogenin dimer bound to double-stranded RNA. Acta Crystallogr.,Sect.F doi:10.1107/S2053230X22008317 |
| 2021 | Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the V IV O-Picolinato Complex with RNase A. Inorg.Chem. doi:10.1021/acs.inorgchem.1c02912 |
| 2021 | The structural features of an ancient ribonuclease from Salmo salar reveal an intriguing case of auto-inhibition. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2021.04.041 |
| 2021 | Reactions with Proteins of Three Novel Anticancer Platinum(II) Complexes Bearing N-Heterocyclic Ligands. Int J Mol Sci doi:10.3390/ijms221910551 |
| 2020 | Protein interactions of dirhodium tetraacetate: a structural study. Dalton Trans doi:10.1039/c9dt04819g |
| 2020 | The Enzyme-Free Release of Nucleotides from Phosphoramidates Depends Strongly on the Amino Acid. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202008665 |
| 2020 | Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding. Biochemistry doi:10.1021/acs.biochem.9b00888 |
| 2020 | Experimental phasing with vanadium and application to nucleotide-binding membrane proteins. Iucrj doi:10.1107/S2052252520012312 |
| 2019 | Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates. Biochim Biophys Acta Gen Subj doi:10.1016/j.bbagen.2018.09.021 |
| 2019 | Nucleoside Tetra- and Pentaphosphates Prepared Using a Tetraphosphorylation Reagent Are Potent Inhibitors of Ribonuclease A. J.Am.Chem.Soc. doi:10.1021/jacs.9b09760 |
| 2019 | Reaction with Proteins of a Five-Coordinate Platinum(II) Compound. Int J Mol Sci doi:10.3390/ijms20030520 |
| 2019 | Arsenoplatin-1 Is a Dual Pharmacophore Anticancer Agent. J.Am.Chem.Soc. doi:10.1021/jacs.8b13681 |
| 2019 | Structure, stability and aggregation propensity of a Ribonuclease A-Onconase chimera. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2019.04.164 |