Homo sapiens · seed P0DP23 · 149 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P0DP23 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 1.10.238.10 CATH 2.40.155.10 CATH 3.30.200.20 SCOP 8032568 SCOP 8093724 SCOP 8104309 SCOP 8039032 SCOP 8034158 SCOP 8033359 SCOP 8062903 SCOP 8032925 SCOP 8037367 SCOP 8062368 SCOP 8062366 SCOP 8033438 SCOP 8032926 RCSB 9NVO 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.
9NVO, 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.
448 distinct constructs across 1,113 entries. 656 polymer entities differ from the UniProt canonical sequence in some way, 50 carry a recognised expression tag and 36 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 |
|---|---|---|---|---|
| 164 | 149 | 1.24 | 7BF1 | matches the canonical sequence |
| 91 | 148 | 1.08 | 2O5G | residues 2-149 |
| 29 | 151 | 2.00 | 1W7J | residues 58-208; V58M |
| 28 | 484 | 1.88 | 3NYV | residues 27-507; 3-residue insertion after 29 |
| 20 | 161 | 4.90 | 9MOW | matches the canonical sequence |
| 14 | 161 | 4.63 | 9YAQ | matches the canonical sequence |
| 14 | 177 | 2.50 | 7XNN | His8; Thrombin site |
| 12 | 89 | 1.37 | 3SD6 | residues 1-89 |
| 11 | 145 | 70.00 | 1M8Q | residues 21-165; Q23E, Q25E, Q27E +6 more |
| 11 | 147 | 70.00 | 1M8Q | residues 4-150; P5K, D6A, E7A +6 more |
| 11 | 149 | 2.20 | 2X51 | matches the canonical sequence |
| 11 | 156 | 2.00 | 1WDC | residues 2-157 |
| 10 | 156 | 2.00 | 1WDC | residues 2-157 |
| 10 | 492 | 1.84 | 9NTZ | residues 52-538; 5-residue insertion after 54; G54S, E55H, R56H +11 more |
| 9 | 146 | 2.77 | 9ZRQ | residues 3-148 |
| 9 | 170 | 1.70 | 4F0Z | matches the canonical sequence |
| 9 | 172 | 2.35 | 2GGM | matches the canonical sequence |
| 9 | 188 | 3.00 | 9YP9 | matches the canonical sequence |
| 8 | 164 | 2.61 | 8FMO | C35S, C84S, D115E |
| 7 | 148 | 2.70 | 9CFV | residues 1-148 |
| 7 | 149 | 3.58 | 8Y40 | E32A, E68A, E105A +1 more |
| 7 | 160 | 4.80 | 6KN8 | residues 2-161; E115D |
| 7 | 169 | 3.00 | 9YP9 | matches the canonical sequence |
| 6 | 90 | 1.75 | 1AVS | residues 2-91 |
| 6 | 129 | residues 53-180; 2 internal deletions; 9-residue insertion after 98; L53G, L54D, Q55D +60 more |
Showing the 25 most-used of 448.
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 | 347 | 31.2% |
| dimeric | 2 | 292 | 26.2% |
| trimeric | 3 | 113 | 10.2% |
| octameric | 8 | 89 | 8.0% |
| tetrameric | 4 | 54 | 4.9% |
| hexameric | 6 | 43 | 3.9% |
| dodecameric | 12 | 42 | 3.8% |
| pentameric | 5 | 21 | 1.9% |
523 entries have the depositor's assembly corroborated by PISA, 568 carry the depositor's word alone and 22 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 40 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1CM1, 1IWQ, 1K90, 1M46, 1NIW, 1PK0, 1QX2, 1QX7, 1XFW, 1YTZ, 1YV0, 1ZUZ, 2AAO, 2BE6, 2F2O, 2F2P, 2NXQ, 2PQ3, 3B32, 3BXL.
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 |
|---|---|---|---|
| EF-hand | CATH 1.10.238.10 | 15–117 | 553 |
| Green fluorescent protein | CATH 2.40.155.10 | 40–149 | 36 |
| Phosphorylase Kinase; domain 1 | CATH 3.30.200.20 | 61–149 | 101 |
| EF-hand | SCOP2B 8032568 | 4–148 | 26 |
| EF-hand | SCOP2B 8093724 | 4–149 | 21 |
| EF-hand | SCOP2B 8104309 | 4–149 | 18 |
| EF-hand | SCOP2B 8039032 | 4–147 | 13 |
| EF-hand | SCOP2B 8034158 | 5–148 | 14 |
| EF-hand | SCOP2B 8033359 | 6–149 | 16 |
| EF-hand | SCOP2B 8062903 | 7–149 | 12 |
| Myosin s1 fragment, N-terminal domain | SCOP2B 8032925 | 8–65 | 13 |
| EF-hand | SCOP2B 8037367 | 9–149 | 17 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| CA | ion | Calcium Ion | 664 | 1.00 |
| MG | ion | Magnesium Ion | 180 | 1.45 |
| ADP | cofactor | Adenosine-5'-Diphosphate | 131 | 1.96 |
| ZN | ion | Zinc Ion | 93 | 1.30 |
| SO4 | ion | Sulfate Ion | 63 | 1.08 |
| GOL | cryoprotectant | Glycerol | 44 | 1.15 |
| PO4 | ion | Phosphate Ion | 44 | 1.80 |
| K | ion | Potassium Ion | 43 | 2.50 |
| ATP | cofactor | Adenosine-5'-Triphosphate | 32 | 2.22 |
| EDO | cryoprotectant | 1,2-Ethanediol | 25 | 1.65 |
| FE | ion | Fe (Iii) Ion | 23 | 1.85 |
| ANP | cofactor | Phosphoaminophosphonic Acid-Adenylate Ester | 20 | 1.70 |
| CL | ion | Chloride Ion | 20 | 1.55 |
| CFF | ligand | Caffeine | 18 | 2.37 |
| ACT | cryoprotectant | Acetate Ion | 17 | 1.15 |
| NAG | cofactor | 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose | 16 | 2.60 |
| NA | ion | Sodium Ion | 15 | 1.65 |
| GTP | cofactor | Guanosine-5'-Triphosphate | 14 | 3.10 |
| GDP | cofactor | Guanosine-5'-Diphosphate | 14 | 3.10 |
| PIO | buffer | [(2r)-2-Octanoyloxy-3-[Oxidanyl-[(1r,2r,3s,4r,5r,6s)-2,3,6-Tris( | 13 | 2.50 |
Parsed from the free text 501 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 508
entries that recorded anything at all.
Median pH 7.0
(range 3.3 to 10.3).
1,094 entries carry a wwPDB validation report: 418 clean, 318 worth a check and 358 with something to explain. Median clashscore 8.66, median RSRZ outliers 4.73%, median R-free minus R-work 0.042. 1,044 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 535 | 1.17 | 224 | 100% |
| Gallus gallus | 81 | 1.08 | 11 | 100% |
| Mus musculus | 66 | 1.72 | 48 | 100% |
| Toxoplasma gondii | 48 | 1.80 | 41 | 100% |
| Rattus norvegicus | 44 | 1.30 | 15 | 100% |
| Bos taurus | 33 | 1.44 | 22 | 100% |
| Argopecten irradians | 18 | 2.00 | 16 | 97% |
| Sus scrofa | 23 | 3.65 | 18 | 99% |
| Xenopus laevis | 24 | 1.80 | 1 | 100% |
| Drosophila melanogaster | 21 | 1.70 | 4 | 100% |
| synthetic construct | 19 | 1.55 | 0 | 100% |
| Cryptosporidium parvum Iowa II | 16 | 1.84 | 15 | 98% |
149 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 | icBTnC2, a new green calcium indicator based on troponin C and mBaoJin, with enhanced photostability. Protein Sci. doi:10.1002/pro.70499 |
| 2026 | Lead Optimization of TgCDPK1 Inhibitors for the Treatment of Toxoplasmosis. J.Med.Chem. doi:10.1021/acs.jmedchem.6c00065 |
| 2026 | The clinical missense variant E282K in PPP3CA/calcineurin shifts substrate dephosphorylation by altering active site recruitment. Nat Commun doi:10.1038/s41467-026-69535-5 |
| 2026 | Structure-guided design of calcium-dependent protein kinase 1 (CDPK1) inhibitors for cryptosporidiosis. J.Infect.Dis. doi:10.1093/infdis/jiag242 |
| 2026 | Structural identification of the RY12 domain of RyR1 as an ADP sensor and the target of the malignant hyperthermia therapeutic dantrolene Nat Commun doi:10.1038/s41467-026-76519-y |
| 2026 | Phosphorylation of a conserved aspartate in the catalytic site of eukaryotic elongation factor 2 kinase. Protein Sci. doi:10.1002/pro.70442 |
| 2026 | Structural basis for the subtype-selectivity of K Ca 2.2 channel activators. Nat Commun doi:10.1038/s41467-025-67232-3 |
| 2026 | Structural basis for the subtype-selective activation of K Ca 3.1 channels. Structure doi:10.1016/j.str.2026.04.010 |
| 2026 | Structural mechanisms for inhibition and activation of human small-conductance Ca 2+ -activated potassium channel SK2. Nat Commun doi:10.1038/s41467-026-68475-4 |
| 2026 | Cryo-EM structure of shutdown human nonmuscle myosin 2A. Sci Adv doi:10.1126/sciadv.aed1858 |
| 2026 | Cryo-EM reveals how cardiomyopathy therapeutic drugs modulate the myosin motors of the heart. Sci Adv doi:10.1126/sciadv.aed6472 |
| 2026 | Dynamics of the beta-cardiac myosin auto-inhibited state explain cardiomyopathy pathogenesis. Nat Commun doi:10.1038/s41467-026-73572-5 |
| 2026 | Visualization of stepwise derepression of TFIIH in global genome nucleotide excision repair. Sci Adv doi:10.1126/sciadv.aeb3506 |
| 2026 | Mechanism of lipid transfer by bridge-like protein VPS13A and the scramblase XK. Cell doi:10.1016/j.cell.2026.05.027 |
| 2026 | Atomic models of the Toxoplasma cell invasion machinery. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01728-w |
| 2026 | Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy. Nat Commun doi:10.1038/s41467-026-75392-z |
| 2026 | Structural and mechanistic insights into the UBR4-KCMF1-Calmodulin complex. Protein Cell doi:10.1093/procel/pwag036 |
| 2026 | Cryo-EM structure of soluble VPS13C suggests its regulation by a conformational switch and by calmodulin. Mol.Cell doi:10.1016/j.molcel.2026.06.028 |
| 2026 | Structural and kinetic mechanisms of state-dependent potassium channel inhibition Sci Adv |
| 2026 | Structural basis of nonmuscle myosin-2 autoinhibition mechanisms. Nat Commun doi:10.1038/s41467-026-74674-w |
| 2026 | Pre-incision structures reveal principles of DNA nucleotide excision repair. Nature doi:10.1038/s41586-026-10122-5 |
| 2026 | The structure of the native cardiac crossbridge in the rigor state. Sci Adv doi:10.1126/sciadv.aeg1209 |
| 2026 | Structural basis and functional analysis of NMDA receptor regulation by calmodulin. J.Biol.Chem. doi:10.1016/j.jbc.2026.111131 |
| 2026 | Structural Insights into L-Type Voltage-Gated Ca 2+ Channel (Ca V 1.2) Activation by CaBP1. Biochemistry doi:10.1021/acs.biochem.6c00032 |
| 2025 | Structural basis for the Ca 2+ /CaM-mediated regulation of CASK-CaMK. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2025.148495 |
| 2025 | Bipartite Genetically Encoded Biosensors to Sense Calcium Ion Dynamics at Membrane-Membrane Contact Sites. Anal.Chem. doi:10.1021/acs.analchem.5c03831 |
| 2025 | Potential Activation Mechanism of Calcium Indicator WHaloCaMP1a Revealed by the Crystal Structure and Molecular Dynamics Simulations. Biochemistry doi:10.1021/acs.biochem.5c00352 |
| 2025 | Structural insights into the dual Ca 2+ -sensor-mediated activation of the PPEF phosphatase family. Nat Commun doi:10.1038/s41467-025-58261-z |
| 2025 | The critical role of the C-terminal lobe of calmodulin in activating eukaryotic elongation factor 2 kinase. J.Biol.Chem. doi:10.1016/j.jbc.2025.110650 |
| 2025 | Phosphatidylinositol 4,5-bisphosphate activation mechanism of human KCNQ5. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2416738122 |
| 2025 | Targeting ryanodine receptors with allopurinol and xanthine derivatives for the treatment of cardiac and musculoskeletal weakness disorders. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2422082122 |
| 2025 | Visualizing insecticide control of insect TRP channel function and assembly. Nat Commun doi:10.1038/s41467-025-67287-2 |
| 2025 | High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2415457122 |
| 2025 | Mechanisms of KCNQ1 gating modulation by KCNE1/3 for cell-specific function. Cell Res. doi:10.1038/s41422-025-01152-1 |
| 2025 | Structural mechanisms of assembly, gating, and calmodulin modulation of human olfactory CNG channel. Nat Commun doi:10.1038/s41467-025-64436-5 |
| 2025 | Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gating. Cell Res. doi:10.1038/s41422-025-01182-9 |
| 2025 | Cryo-EM structures of the small-conductance Ca 2+ -activated K Ca 2.2 channel. Nat Commun doi:10.1038/s41467-025-59061-1 |
| 2025 | Small molecule inhibits KCNQ channels with a non-blocking mechanism. Nat.Chem.Biol. doi:10.1038/s41589-024-01834-8 |
| 2025 | Mechanism of SK2 channel gating and its modulation by the bee toxin apamin and small molecules. Elife doi:10.7554/eLife.107733 |
| 2025 | Architecture of the UBR4 complex, a giant E4 ligase central to eukaryotic protein quality control. Science doi:10.1126/science.adv9309 |