Meleagris gallopavo · seed 135L_1 · 129 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P00703 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 1.10.530.10 SCOP 8037428 SCOP 8043304 RCSB 1IOT PDBe PF00062
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.
1IOT, 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.
280 distinct constructs across 1,699 entries. 1,621 polymer entities differ from the UniProt canonical sequence in some way, 1 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 |
|---|---|---|---|---|
| 1252 | 129 | 0.65 | 2VB1 | residues 19-147 |
| 64 | 147 | 0.83 | 9QUM | matches the canonical sequence |
| 36 | 130 | 1.04 | 2NWD | residues 19-148 |
| 12 | 123 | 1.90 | 1YRO | residues 21-143 |
| 12 | 129 | 1.12 | 1JSE | residues 19-147 |
| 7 | 129 | 1.60 | 1LMQ | residues 16-144; A101D |
| 6 | 128 | 0.98 | 5HMV | residues 19-146 |
| 5 | 123 | 1.85 | 6IP9 | residues 20-142 |
| 5 | 127 | 1.20 | 6F9Y | residues 19-145 |
| 4 | 130 | 0.89 | 7P6M | residues 18-147 |
| 4 | 130 | 1.80 | 1HNL | residues 19-148; C95A |
| 3 | 129 | 1.11 | 5V92 | residues 19-147; N84D, P97R, S118R +1 more |
| 3 | 129 | 1.90 | 1DKK | matches the canonical sequence |
| 2 | 121 | 1.20 | 7EKA | residues 20-140 |
| 2 | 122 | 1.90 | 2FBD | residues 20-141 |
| 2 | 125 | 2.29 | 9J0L | residues 23-147 |
| 2 | 127 | 1.76 | 1UIA | residues 19-147; 1 internal deletion |
| 2 | 129 | 1.39 | 7YNV | residues 19-147; A49V |
| 2 | 129 | 1.56 | 3WVY | residues 19-147; D66A |
| 2 | 129 | 1.64 | 1H6M | residues 19-147; E53Q |
| 2 | 129 | 1.80 | 1LZD | residues 19-147; W80Y |
| 2 | 129 | 1.90 | 3A3R | residues 19-147; N77D |
| 2 | 129 | 1.90 | 5VJQ | residues 19-147; G55S, N84D, R89G +1 more |
| 2 | 130 | 1.70 | 1TCY | residues 19-148; Y81F |
| 2 | 130 | 1.77 | 1TBY | residues 19-148; Y81L |
Showing the 25 most-used of 280.
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 | 1,545 | 90.9% |
| dimeric | 2 | 72 | 4.2% |
| trimeric | 3 | 67 | 3.9% |
| tetrameric | 4 | 3 | 0.2% |
| heptameric | 7 | 3 | 0.2% |
| hexameric | 6 | 1 | 0.1% |
| 24-meric | 24 | 1 | 0.1% |
| tridecameric | 13 | 1 | 0.1% |
894 entries have the depositor's assembly corroborated by PISA, 760 carry the depositor's word alone and 45 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 19 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1ZMY, 2FBD, 2HU1, 2HU3, 3F6Z, 3LN2, 3P66, 3TMU, 3TMV, 3TMW, 3TMX, 3WU7, 3WU8, 3WU9, 3WUA, 4LYB, 4LYC, 4PHI, 5KKI.
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 |
|---|---|---|---|
| 1.10.530.10 | CATH | 1–129 | 1,288 |
| Lysozyme-like | SCOP2B 8037428 | 1–129 | 1,277 |
| Lysozyme-like | SCOP2B 8043304 | 1–129 | 211 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| NA | ion | Sodium Ion | 874 | 0.80 |
| CL | ion | Chloride Ion | 780 | 0.80 |
| ACT | cryoprotectant | Acetate Ion | 149 | 0.65 |
| EDO | cryoprotectant | 1,2-Ethanediol | 145 | 0.65 |
| GOL | cryoprotectant | Glycerol | 121 | 1.05 |
| NO3 | ion | Nitrate Ion | 115 | 0.65 |
| DMS | cryoprotectant | Dimethyl Sulfoxide | 64 | 0.98 |
| PT | ion | Platinum (Ii) Ion | 38 | 0.98 |
| CA | ion | Calcium Ion | 35 | 1.15 |
| NDG | cofactor | 2-Acetamido-2-Deoxy-Alpha-D-Glucopyranose | 31 | 1.45 |
| SO4 | ion | Sulfate Ion | 30 | 1.13 |
| RU | ion | Ruthenium Ion | 28 | 0.98 |
| EPE | buffer | 4-(2-Hydroxyethyl)-1-Piperazine Ethanesulfonic Acid | 21 | 0.94 |
| BR | ion | Bromide Ion | 18 | 1.03 |
| CPT | ligand | Cisplatin | 18 | 0.98 |
| AU | ion | Gold Ion | 17 | 1.10 |
| DO3 | ligand | 10-((2r)-2-Hydroxypropyl)-1,4,7,10-Tetraazacyclododecane 1,4,7-T | 16 | 0.80 |
| GD | ion | Gadolinium Atom | 16 | 0.80 |
| IOD | ion | Iodide Ion | 15 | 1.10 |
| QPT | ligand | Carboplatin | 15 | 1.60 |
Parsed from the free text 1,426 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 1,517
entries that recorded anything at all.
Median pH 4.6
(range 3.0 to 10.0).
1,698 entries carry a wwPDB validation report: 1,104 clean, 434 worth a check and 160 with something to explain. Median clashscore 5.03, median RSRZ outliers 1.55%, median R-free minus R-work 0.036. 1,462 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Gallus gallus | 1,390 | 0.65 | 307 | 100% |
| Homo sapiens | 219 | 1.06 | 5 | 100% |
| Mus musculus | 14 | 1.90 | 12 | 98% |
| Meleagris gallopavo | 13 | 1.12 | 1 | 100% |
| Bos taurus | 9 | 1.20 | 1 | 100% |
| Anas platyrhynchos | 7 | 1.11 | 0 | 100% |
| Oncorhynchus mykiss | 7 | 1.60 | 3 | 98% |
| Capra hircus | 5 | 1.60 | 0 | 86% |
| Canis lupus familiaris | 5 | 1.85 | 0 | 100% |
| Asplenium bulbiferum subsp. bulbiferum | 3 | 1.31 | 0 | 100% |
| Colinus virginianus | 3 | 1.90 | 0 | 100% |
| Musca domestica | 3 | 1.90 | 0 | 92% |
129 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 | Protein Recognition and Amyloid Remodeling Governed by Paddlewheel Diruthenium Coordination Chemistry. Inorg.Chem. doi:10.1021/acs.inorgchem.6c02947 |
| 2026 | Unconventional chalcogen-containing azolylidene metal complexes as potential anticancer therapeutics. Chem Sci doi:10.1039/d5sc05555e |
| 2026 | Speciation, Protein Binding, Biotransformation, and Cytotoxicity of a VV-Lactate Complex. Inorg.Chem. doi:10.1021/acs.inorgchem.6c02377 |
| 2026 | Optimizing the connectivity of protein conformations to untangle ensemble refinement Biorxiv doi:10.64898/2026.09.17.752399 |
| 2026 | A new macromolecular crystallography endstation at NanoTerasu for accelerating structural biology and drug discovery. Acta Crystallogr D Struct Biol doi:10.1107/S2059798325011234 |
| 2026 | Binding of Aqueous-Stable, Lipophilic, Hemocompatible Anticancer V V O 2 Metallodrugs with Biological Molecules: X-ray Structures of the Adduct of the V V -hydrazonato Complex with Hen Egg White Lysozyme. Inorg.Chem. doi:10.1021/acs.inorgchem.5c05201 |
| 2026 | Tuning Au Reactivity Beyond Canonical Targets: Ligand-Driven Au(I) Metalation of Lysine Residues in Hen Egg White Lysozyme. Inorg.Chem. doi:10.1021/acs.inorgchem.6c01884 |
| 2026 | Unfolding of hen egg-white lysozyme - is there a unique starting point? J.Biomol.Struct.Dyn. doi:10.1080/07391102.2025.2475230 |
| 2026 | A user-friendly goniometer-compatible fixed-target platform for macromolecular crystallography at synchrotrons. J.Appl.Crystallogr. doi:10.1107/S1600576725011513 |
| 2026 | AI-Guided Droplet Microreactors Enable Rapid and Reproducible Protein Crystallization Small doi:10.1002/smll.202510977 |
| 2026 | Drop-on-fixed-target reaction initiation approach for serial and time-resolved crystallography. Iucrj doi:10.1107/S2052252526003489 |
| 2026 | Compact tape-driven sample delivery system for serial femtosecond crystallography. J.Appl.Crystallogr. doi:10.1107/S1600576726000063 |
| 2026 | Guanosine hydrogel as a new injection matrix for protein serial X-ray crystallography Acta Crystallogr.,Sect.D doi:10.1107/S1600576725011276 |
| 2026 | Strategies for mitigating radiation damage and improving data completeness in 3D electron diffraction of protein crystals. Acta Crystallogr D Struct Biol doi:10.1107/S2059798325011258 |
| 2026 | Covalently constrained 'Di-Gembodies' enable parallel structure solutions by cryo-EM. Nat.Chem.Biol. doi:10.1038/s41589-025-01972-7 |
| 2025 | Exploring the potential of a bioassembler for protein crystallization in space. Npj Microgravity doi:10.1038/s41526-025-00477-w |
| 2025 | Structure and dynamics of the active site of hen egg-white lysozyme from atomic resolution neutron crystallography. Structure doi:10.1016/j.str.2024.10.030 |
| 2025 | Unexpected in crystallo reactivity of the potential drug bis (maltolato) oxidovanadium (IV) with lysozyme Inorg Chem Front doi:10.1039/D4QI01528B |
| 2025 | Sensitive detection of structural dynamics using a statistical framework for comparative crystallography. Sci Adv doi:10.1126/sciadv.adj2921 |
| 2025 | Speciation and structural transformation of a V V -malate complex in the absence and in the presence of a protein: from a dinuclear species to decavanadate. Inorg Chem Front doi:10.1039/d5qi01384d |
| 2025 | Finding the Key: Binding of Metal-Oxo Clusters to the Enzyme Active Site Enabled by "Click" (Bio)Conjugation. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202518349 |
| 2025 | Instrumentation and methods for efficient time-resolved X-ray crystallography of biomolecular systems with sub-10 ms time resolution. Iucrj doi:10.1107/S205225252500288X |
| 2025 | Automated gradient equilibration of macromolecular crystals to new solution conditions. Acta Crystallogr.,Sect.F doi:10.1107/S2053230X25008398 |
| 2025 | Combining MicroED and native mass spectrometry for structural discovery of enzyme-small molecule complexes. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2503780122 |
| 2025 | Impact of Diffraction Data Volume on Data Quality in Serial Crystallography Crystals doi:10.3390/cryst15020104 |
| 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 |
| 2025 | Protein crystallization and structure determination at room temperature in the CrystalChip. Febs Open Bio doi:10.1002/2211-5463.13932 |
| 2025 | Effects of Beam Center Position Shifts on Data Processing in Serial Crystallography Crystals doi:10.3390/cryst15020185 |
| 2025 | Laueprocess: a software package for processing Laue diffraction data. J.Appl.Crystallogr. doi:doi.org/10.1107/S1600576725005023 |
| 2025 | Does crossing the pond affect crystal quality? Biorxiv doi:10.1101/2025.06.12.659325 |
| 2025 | The structure of His15 acetamide-modified hen egg-white lysozyme: a nice surprise from an old friend. Acta Crystallogr.,Sect.F doi:10.1107/S2053230X2500010X |
| 2025 | Viscoelastic characterization of the lipid cubic phase provides insights into high-viscosity extrusion injection for XFEL experiments. Sci Rep doi:10.1038/s41598-025-25449-8 |
| 2025 | Discrete Hybrid Vanadium-oxo Cluster as a Targeted Tool for Selective Protein Oxidative Modifications and Cleavage. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202423078 |
| 2025 | Real-time data processing for serial crystallography experiments. Iucrj doi:10.1107/S2052252524011837 |
| 2025 | Formation of Mixed-Valence Cage-Like Polyoxidovanadates at 37°C Upon Reaction of V IV O(acetylacetonato) 2 With Lysozyme. Chemistry doi:10.1002/chem.202500488 |
| 2025 | Fast and selective protein modification with iron-substituted polyoxometalates via a radical pathway Inorg Chem Front doi:10.1039/D5QI01454A |
| 2025 | Protein Recognition and Assembly by a Phosphocavitand. J.Am.Chem.Soc. doi:10.1021/jacs.5c08121 |
| 2025 | Laueprocess: a software package for processing Laue diffraction data J.Appl.Crystallogr. doi:10.1107/S1600576725005023 |
| 2025 | Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron. Commun Chem doi:10.1038/s42004-024-01404-y |
| 2025 | Dirhodium Tetraacetate Binding to Lysozyme at Body Temperature. Int J Mol Sci doi:10.3390/ijms26146582 |