Homo sapiens · seed P24941 · 298 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P24941 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.30.200.20 CATH 1.10.510.10 SCOP 8040310 SCOP 8032654 SCOP 8039449 SCOP 8033039 SCOP 8036628 SCOP 8039362 SCOP 8036604 SCOP 8062460 SCOP 8036640 SCOP 8036635 SCOP 8036019 SCOP 8079151 RCSB 9HJ1 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.
9HJ1, 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.
443 distinct constructs across 1,974 entries. 1,140 polymer entities differ from the UniProt canonical sequence in some way, 387 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 |
|---|---|---|---|---|
| 185 | 298 | 1.38 | 7RXO | matches the canonical sequence |
| 104 | 306 | 1.00 | 6Q49 | matches the canonical sequence |
| 59 | 360 | 1.66 | 8YD9 | matches the canonical sequence |
| 57 | 360 | 1.44 | 5R97 | matches the canonical sequence |
| 56 | 328 | 1.09 | 8AEC | residues 2-329; R21S, K74A, K75A +1 more |
| 55 | 299 | 1.26 | 4EK4 | matches the canonical sequence |
| 55 | 368 | 1.12 | 8AOJ | His6 |
| 38 | 302 | 1.99 | 6GUE | matches the canonical sequence |
| 38 | 352 | 1.51 | 5OTO | residues 1-329; M1S, R21S |
| 33 | 364 | 1.46 | 3QYZ | His6 |
| 30 | 364 | 0.83 | 6TGU | His6; C336S |
| 29 | 344 | 2.98 | 8BU1 | residues 709-1052; Y709G, E711G, K965R |
| 28 | 335 | 1.50 | 3BQC | residues 1-335 |
| 25 | 303 | 1.47 | 9UAU | matches the canonical sequence |
| 25 | 360 | 1.60 | 4EHV | M1G |
| 22 | 361 | 1.50 | 5LAR | matches the canonical sequence |
| 21 | 299 | 1.60 | 9FR2 | matches the canonical sequence |
| 21 | 349 | 1.70 | 8P79 | matches the canonical sequence |
| 19 | 332 | 1.24 | 4RLK | matches the canonical sequence |
| 19 | 336 | 1.25 | 4KWP | residues 1-336 |
| 18 | 360 | 1.59 | 3SA0 | matches the canonical sequence |
| 17 | 338 | 2.10 | 6QY7 | residues 1-337 |
| 17 | 360 | 1.50 | 3LFF | M1G, C119S, C162S +2 more |
| 17 | 366 | 1.70 | 2QD9 | M1H |
| 17 | 372 | 1.70 | 3FMK | His6 |
Showing the 25 most-used of 443.
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 | 1,425 | 72.2% |
| dimeric | 2 | 366 | 18.5% |
| trimeric | 3 | 120 | 6.1% |
| tetrameric | 4 | 34 | 1.7% |
| pentameric | 5 | 6 | 0.3% |
| heptameric | 7 | 4 | 0.2% |
| hexameric | 6 | 3 | 0.2% |
| 40-meric | 40 | 2 | 0.1% |
1,347 entries have the depositor's assembly corroborated by PISA, 533 carry the depositor's word alone and 94 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: 1G3N, 1H24, 1H25, 1H26, 1H27, 1JST, 2F49, 2JLD, 2PK9, 2WMA, 2WMB, 2X1N, 3E3B, 3F5X, 3H30, 3MTL, 3NIZ, 3PUP, 3SD0, 3U9C.
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 |
|---|---|---|---|
| Phosphorylase Kinase; domain 1 | CATH 3.30.200.20 | 19–114 | 1,605 |
| Transferase(Phosphotransferase) domain 1 | CATH 1.10.510.10 | 110–298 | 1,679 |
| Protein kinase-like (PK-like) | SCOP2B 8040310 | 2–298 | 502 |
| Protein kinase-like (PK-like) | SCOP2B 8032654 | 3–298 | 40 |
| Protein kinase-like (PK-like) | SCOP2B 8039449 | 4–298 | 281 |
| Protein kinase-like (PK-like) | SCOP2B 8033039 | 6–298 | 254 |
| Protein kinase-like (PK-like) | SCOP2B 8036628 | 6–298 | 122 |
| Protein kinase-like (PK-like) | SCOP2B 8039362 | 9–298 | 27 |
| Protein kinase-like (PK-like) | SCOP2B 8036604 | 11–298 | 21 |
| Protein kinase-like (PK-like) | SCOP2B 8062460 | 15–298 | 39 |
| Protein kinase-like (PK-like) | SCOP2B 8036640 | 23–298 | 77 |
| Protein kinase-like (PK-like) | SCOP2B 8036635 | 33–298 | 154 |
ANP60 entries
ADP47 entries
ATP44 entries
SB420 entries
GG519 entries
3NG18 entries
SF413 entries
SB210 entries
I4610 entries
IRG10 entries
AGS8 entries
NIO8 entries
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| SO4 | ion | Sulfate Ion | 424 | 1.12 |
| EDO | cryoprotectant | 1,2-Ethanediol | 254 | 0.83 |
| MG | ion | Magnesium Ion | 195 | 1.04 |
| CL | ion | Chloride Ion | 194 | 0.89 |
| GOL | cryoprotectant | Glycerol | 142 | 1.19 |
| ACT | cryoprotectant | Acetate Ion | 129 | 1.09 |
| DMS | cryoprotectant | Dimethyl Sulfoxide | 107 | 1.00 |
| BOG | lipid/detergent | Octyl Beta-D-Glucopyranoside | 79 | 1.45 |
| ANP | cofactor | Phosphoaminophosphonic Acid-Adenylate Ester | 60 | 1.04 |
| PO4 | ion | Phosphate Ion | 48 | 1.09 |
| ADP | cofactor | Adenosine-5'-Diphosphate | 47 | 1.19 |
| ATP | cofactor | Adenosine-5'-Triphosphate | 44 | 1.09 |
| NA | ion | Sodium Ion | 44 | 0.97 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 41 | 1.25 |
| ZN | ion | Zinc Ion | 39 | 2.00 |
| SGM | cryoprotectant | Monothioglycerol | 28 | 1.65 |
| SB4 | ligand | 4-(4-Fluorophenyl)-1-(4-Piperidinyl)-5-(2-Amino-4-Pyrimidinyl)-I | 20 | 1.22 |
| CA | ion | Calcium Ion | 20 | 1.22 |
| GG5 | ligand | 4-[3-(4-Fluorophenyl)-1h-Pyrazol-4-Yl]pyridine | 19 | 1.65 |
| 3NG | ligand | 5-[(3-Chlorophenyl)amino]benzo[C][2,6]naphthyridine-8-Carboxylic | 18 | 0.89 |
Parsed from the free text 1,797 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 1,828
entries that recorded anything at all.
Median pH 7.0
(range 4.0 to 9.5).
1,974 entries carry a wwPDB validation report: 494 clean, 849 worth a check and 631 with something to explain. Median clashscore 5.45, median RSRZ outliers 6.21%, median R-free minus R-work 0.04. 1,886 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 1,650 | 0.83 | 1507 | 100% |
| Mus musculus | 133 | 1.22 | 120 | 98% |
| Rattus norvegicus | 80 | 1.34 | 58 | 98% |
| Zea mays | 41 | 1.24 | 40 | 97% |
| Arabidopsis thaliana | 12 | 1.25 | 7 | 97% |
| Saccharomyces cerevisiae | 10 | 1.55 | 6 | 98% |
| Plasmodium falciparum | 4 | 1.90 | 2 | 97% |
| Saccharomyces cerevisiae S288C | 4 | 1.95 | 3 | 97% |
| Toxoplasma gondii RH | 3 | 2.10 | 3 | 99% |
| Cryptococcus neoformans Bt85 | 4 | 2.28 | 4 | 97% |
| Cryptosporidium parvum Iowa II | 4 | 2.37 | 3 | 97% |
| Leishmania major | 3 | 1.95 | 1 | 99% |
298 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 | Crystallographic Fragment Screening with CK2 alpha', an Isoform of Human Protein Kinase CK2 Catalytic Subunit, and Its Use to Obtain a CK2 alpha'/Heparin Complex Structure Kinases Phosphatases doi:10.3390/kinasesphosphatases4010001 |
| 2026 | Targeting Human Protein Kinase CK2 by a Library of Indeno[1,2-b]Indoles: Contribution of Thermal Shift Assay to Pre-Screening and Co-Crystallization to Post-Screening. Arch Pharm doi:10.1002/ardp.70312 |
| 2026 | Discovery and characterization of a novel class of cyclic peptidic compounds inhibiting the subunit interaction of the protein kinase CK2 alpha 2 beta 2 holoenzyme Rsc Chem Biol doi:10.1039/D6CB00095A |
| 2026 | Discovery of Supra-Bivalent GSK3 beta Inhibitory Peptides Containing an ATP-Mimetic Amino Acid. J.Am.Chem.Soc. doi:10.1021/jacs.5c13788 |
| 2026 | Discovery of INCB127443: A Potent and Orally Available Inhibitor of Cyclin-Dependent Kinase 2 J.Med.Chem. doi:10.1021/acs.jmedchem.6c01506 |
| 2026 | Switching off CK2-mediated activation of survivin offers new therapeutic opportunities in neuroblastoma. Exp.Mol.Med. doi:10.1038/s12276-025-01628-5 |
| 2026 | Utilizing Molecular Dynamics and Mechanistic Pharmacokinetic Studies in the Design of Selective CDK2 Inhibitors. J.Med.Chem. doi:10.1021/acs.jmedchem.5c03803 |
| 2026 | Conformation-Specific Design: Engineering Extracellular Signal-Regulated Kinase 2 Variants with Bias toward Active or Inactive States. Acs Omega doi:10.1021/acsomega.6c01185 |
| 2026 | Nanoscale Direct-to-Biology Optimization of Cdk2 Inhibitors. J.Med.Chem. doi:10.1021/acs.jmedchem.5c03614 |
| 2026 | Discovery of BMS-159, an Orally Active Imidazotriazine Pan-CK2 Inhibitor for the Treatment of Cancer. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.6c00089 |
| 2026 | Molecular basis of mitogen-activated protein kinase ERK2 activation by its upstream kinase MEK1. Biorxiv doi:10.64898/2026.01.19.700303 |
| 2026 | Functional characterization of 42 CK2 alpha de novo variants associated with Okur-Chung neurodevelopmental syndrome. Febs J. doi:10.1111/febs.70538 |
| 2026 | A Polypharmacology-Driven Approach to Alzheimer's Disease and Tauopathies: Rational Design, Synthesis and Characterization of Amino-Pyrazole-Based Multikinase (GSK-3 beta /FYN-alpha /DYRK1A) Inhibitors. J.Med.Chem. doi:10.1021/acs.jmedchem.5c01810 |
| 2026 | Cryo-EM structures of the CDK11-cyclin L-SAP30BP complex reveal mechanisms of CDK11 regulation. Nat Commun doi:10.1038/s41467-026-72329-4 |
| 2026 | Selective CDK2 Degradation via Noncanonical Recruitment. J.Med.Chem. doi:10.1021/acs.jmedchem.6c01264 |
| 2026 | Mechanistic insight into the phosphorylation of ERK by MEK Biorxiv doi:10.64898/2026.03.13.710243 |
| 2026 | Structural basis of the cyclin Y/14-3-3 protein-mediated activation of CDK16. Nat Commun doi:10.1038/s41467-026-70778-5 |
| 2026 | The +1 nucleosome functions in RNA Pol II transcription initiation and the transition to elongation. Mol.Cell doi:10.1016/j.molcel.2026.06.042 |
| 2025 | Novel fluoro-brominated benzotriazoles as potential CK2 inhibitors. How does fluorination affect the properties of benzotriazoles? Bioorg.Chem. doi:10.1016/j.bioorg.2025.109446 |
| 2025 | Exploring the biological potential of the brominated indenoindole MC11 and its interaction with protein kinase CK2. Biol.Chem. doi:10.1515/hsz-2024-0160 |
| 2025 | Exploiting the Cryptic alpha D Pocket of Casein Kinase 2 alpha (CK2 alpha ) to Deliver Highly Potent and Selective Type 1 Inhibitors. J.Med.Chem. doi:10.1021/acs.jmedchem.5c01807 |
| 2025 | Discovery of AZD8421: A Potent CDK2 Inhibitor with Selectivity Against Other CDK Family Members and the Human Kinome. J.Med.Chem. doi:10.1021/acs.jmedchem.5c01478 |
| 2025 | Targeting Casein Kinase 2 and Histone Deacetylase with a Dual Inhibitor Effectively Reduces Tumor Growth in a Triple-Negative Breast Cancer Xenograft Model. Acs Pharmacol Transl Sci doi:10.1021/acsptsci.5c00192 |
| 2025 | A CK2 alpha ' mutant indicating why CK2 alpha and CK2 alpha ', the isoforms of the catalytic subunit of human protein kinase CK2, deviate in affinity to CK2 beta. Biol.Chem. doi:10.1515/hsz-2024-0157 |
| 2025 | Targeting bacterial kinases as a strategy to counteract antibiotic resistance. Commun Chem doi:10.1038/s42004-025-01794-7 |
| 2025 | Fulcrum Occupancy-Leverage Perturbation Strategy Enables Rapid Discovery of Potent CDK2-Cyclin A2 Interaction Inhibitors. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202513542 |
| 2025 | Discovery of Atirmociclib (PF-07220060): A Potent and Selective CDK4 Inhibitor. J.Med.Chem. doi:10.1021/acs.jmedchem.5c02137 |
| 2025 | An allosteric cyclin E-CDK2 site mapped by paralog hopping with covalent probes. Nat.Chem.Biol. doi:10.1038/s41589-024-01738-7 |
| 2025 | Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions. J.Biol.Chem. doi:10.1016/j.jbc.2025.108348 |
| 2025 | Targeting Neuroinflammation and Cognitive Decline: First-in-Class Dual Butyrylcholinesterase and p38 alpha Mitogen-Activated Protein Kinase Inhibitors. J.Med.Chem. doi:10.1021/acs.jmedchem.5c00933 |
| 2025 | CDK4 selective inhibition improves preclinical anti-tumor efficacy and safety. Cancer Cell doi:10.1016/j.ccell.2025.02.006 |
| 2025 | Structural and functional characterization of TgGSK3, a druggable kinase in Toxoplasma gondii. Nat Commun doi:10.1038/s41467-025-64701-7 |
| 2025 | A first-in-class selective inhibitor of ERK1/2 and ERK5 overcomes drug resistance with a single-molecule strategy. Signal Transduct Target Ther doi:10.1038/s41392-025-02169-z |
| 2025 | Discovery of KDX1381, a Bivalent CK2 alpha Inhibitor for the Treatment of Solid Tumors as a Single Agent or in Combination. J.Med.Chem. doi:10.1021/acs.jmedchem.5c00695 |
| 2025 | CDK2-based CDK7 mimic as a tool for structural analysis: Biochemical validation and crystal structure with SY5609. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2024.139117 |
| 2025 | Crystallographic fragment screening of CDK2-cyclin A: FragLites map sites of protein-protein interaction. Structure doi:10.1016/j.str.2025.07.016 |
| 2025 | Binding-Site Switch for Protein Kinase CK2 Inhibitors. Chemmedchem doi:10.1002/cmdc.202400868 |
| 2025 | TFIIH kinase CDK7 drives cell proliferation through a common core transcription factor network. Sci Adv doi:10.1126/sciadv.adr9660 |
| 2025 | Resistance to CDK7 inhibitors directed by acquired mutation of a conserved residue in cancer cells. Embo J. doi:10.1038/s44318-025-00554-6 |
| 2025 | Picomolar bivalent inhibitors of protein kinase CK2 active against beta-coronavirus replication. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2025.117826 |