CODSWALLOP

Ribonuclease pancreatic

Bos taurus · seed P61823 · 150 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.

500Entries 500Entities 149Constructs 15Organisms 171Ligand-bound
0.85 ÅBest res.
1.80 ÅMedian res.

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

The reference structure

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.

Rendered structure of 1RAS
1RAS 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.

175150493 constructs

Constructs, most-used first

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.

EntitiesLengthBest (Å)Best entryWhat 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.

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".

S58R 32% K63S 30% D64P 30% Y102K 30% S106Q 30% N139G 29% K57R 29% Q54S 28% A32T 27% Q81K 27% A30R 27% T43P 26% A46G 26% T104S 26% Q127A 26% E112L 26% S42K 26% K124R 25% K27D 25% S76N 25% A128G 25% S85E 24% N129F 24% N50R 24% M39Y 24% E28N 24% Q100I 24% A122Q 24% K117P 24% K130R 24%

What it assembles into

Oligomeric stateChainsEntriesShare
monomeric1 373 74.6%
dimeric2 114 22.8%
tetrameric4 6 1.2%
trimeric3 2 0.4%
hexameric6 1 0.2%
heptameric7 1 0.2%
82-meric82 1 0.2%
85-meric85 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.

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.

CATHRibonuclease A-like domainSCOP2BRNase A-likeRNase A-likeRNase A-likeRNase A-likeRNase A-like175150
DomainSourceSpan (seed)Chains
Ribonuclease A-like domainCATH 3.10.130.10 27–150 383
RNase A-likeSCOP2B 8038165 27–150 309
RNase A-likeSCOP2B 8034213 27–150 21
RNase A-likeSCOP2B 8038842 30–150 25
RNase A-likeSCOP2B 8035353 35–150 10
RNase A-likeSCOP2B 8040055 36–150 46

What binds it

AMP AMP8 entries F3I F3I6 entries NH3 NH35 entries VVU VVU5 entries U3P U3P4 entries CGP CGP4 entries C3P C3P4 entries D1O D1O4 entries U2G U2G3 entries ADP ADP3 entries CPA CPA3 entries C5P C5P3 entries
ComponentClassNameEntriesBest (Å)
SO4ion Sulfate Ion 131 0.85
CLion Chloride Ion 72 1.01
PO4ion Phosphate Ion 25 1.04
ACTcryoprotectant Acetate Ion 23 0.87
NAion Sodium Ion 21 0.94
GOLcryoprotectant Glycerol 20 1.49
PEGcryoprotectant Di(Hydroxyethyl)ether 18 1.01
CITbuffer Citric Acid 16 1.17
FMTbuffer Formic Acid 16 0.94
IPAcryoprotectant Isopropyl Alcohol 14 0.85
TARbuffer D(-)-Tartaric Acid 11 1.04
EDOcryoprotectant 1,2-Ethanediol 9 1.02
TLAbuffer L(+)-Tartaric Acid 9 1.04
PTion Platinum (Ii) Ion 9 1.76
AMPcofactor Adenosine Monophosphate 8 1.50
ACYcryoprotectant Acetic Acid 7 0.98
ZNion Zinc Ion 7 1.04
F3Iligand (Mi2-Acetato-O, O')-Hexaaquo-Dirhodium (Ii) 6 1.15
MPDcryoprotectant (4s)-2-Methyl-2,4-Pentanediol 5 1.40
DMScryoprotectant Dimethyl Sulfoxide 5 1.76

How it crystallises

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).

Precipitants

PEG × Sodium citrate × Ammonium sulfate × Sodium chloride × Isopropanol × Lithium sulfate × Sodium formate × Ethanol × MPD × Ammonium phosphate × Magnesium chloride × Dioxane × Sodium malonate × Calcium chloride ×

Buffers

Citrate × Sodium acetate × Tris × Phosphate × Sodium cacodylate × HEPES × Bis-Tris propane × Bis-Tris × MES × Imidazole ×

Which entries to trust

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.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Bos taurus362 0.85 143 100%
Homo sapiens96 0.98 19 93%
Escherichia coli 'BL21-Gold(DE3)pLysS AG11 0.94 6 79%
Mus musculus6 1.50 0 93%
synthetic construct5 1.14 0 81%
Sus scrofa4 1.25 2 77%
Rattus norvegicus3 1.78 0 82%
Gallus gallus2 1.76 1 83%
Lithobates pipiens2 1.80 0 76%
Salmo salar2 1.89 0 78%
Arabidopsis thaliana2 3.50 0 14%
Chelonia mydas1 1.60 0 82%

Seed sequence

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

1MALKSLVLLS LLVLVLLLVR VQPSLGKETA AAKFERQHMD SSTSAASSSN YCNQMMKSRN
61LTKDRCKPVN TFVHESLADV QAVCSQKNVA CKNGQTNCYQ SYSTMSITDC RETGSSKYPN
121CAYKTTQANK HIIVACEGNP YVPVHFDASV

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 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