Homo sapiens · seed P31749 · 480 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P31749 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.30.200.20 CATH 1.10.167.10 CATH 1.10.510.10 CATH 2.60.120.10 CATH 1.10.287.1270 SCOP 8040941 SCOP 8034489 SCOP 8062547 SCOP 8042948 SCOP 8040369 SCOP 8062446 SCOP 8099168 SCOP 8062400 SCOP 8098222 SCOP 8044505 SCOP 8039914 SCOP 8040503 SCOP 8033774 SCOP 8043734 SCOP 8062368 SCOP 8062553 SCOP 8069143 SCOP 8067255 SCOP 8101058 RCSB 3CQW 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.
3CQW, 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.
597 distinct constructs across 1,606 entries. 1,097 polymer entities differ from the UniProt canonical sequence in some way, 92 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 |
|---|---|---|---|---|
| 155 | 353 | 1.12 | 5N1F | matches the canonical sequence |
| 40 | 350 | 1.55 | 4HPU | residues 2-351 |
| 28 | 484 | 1.88 | 3NYV | residues 27-507; 3-residue insertion after 29 |
| 26 | 351 | 1.61 | 5VHB | matches the canonical sequence |
| 24 | 293 | 1.40 | 5AV4 | residues 1-293; R286L, K287E, A288H +5 more |
| 23 | 351 | 1.58 | 3OVV | matches the canonical sequence |
| 21 | 265 | 1.69 | 5ORL | residues 127-391; C290A |
| 19 | 350 | 1.60 | 1XH8 | residues 2-351 |
| 18 | 351 | 1.90 | 4AXA | V105T, V124A, L174M +1 more |
| 17 | 279 | 1.85 | 4J8M | residues 123-401; T287D |
| 17 | 311 | 1.09 | 5LVO | residues 49-359; P49G, Y288G, Q292A |
| 17 | 415 | 2.45 | 5WNF | residues 1-415; M1G, T3L, G4H +1 more |
| 17 | 598 | 2.50 | 8UAP | His6; D311N |
| 16 | 285 | 1.67 | 5L8L | residues 119-403; K119G, N120A, E121M +2 more |
| 16 | 310 | 1.50 | 4QMT | residues 9-315; 1 internal deletion; 6-residue insertion after 9; L10M, L12H, N13S +7 more |
| 14 | 285 | 2.25 | 6Z4Y | residues 119-403; K119G, N120A, E121M |
| 14 | 356 | 1.55 | 4IAI | His5; M1H |
| 13 | 294 | 1.40 | 4YPD | residues 2-295; R286S, K287A, A288W +4 more |
| 12 | 268 | 1.85 | 6X5G | residues 7-274; D135N, Q223K |
| 12 | 306 | 1.47 | 8QLT | residues 3-308; S3M, R302A, Y303H +5 more |
| 12 | 445 | 1.90 | 9TMV | residues 1-446; 1 internal deletion; M1G, E114A, E115A +5 more |
| 10 | 312 | 1.99 | 3QD0 | residues 48-359 |
| 10 | 327 | 1.75 | 6ZJF | residues 4-329; 1-residue insertion after 24; R4M, R5H, F6H +15 more |
| 10 | 446 | 1.90 | 7NH5 | residues 1-446; M1G, E114A, E115A +1 more |
| 9 | 503 | 3.27 | 6E4U | residues 10-559; 1 internal deletion; M10G, I481A, T482S +5 more |
Showing the 25 most-used of 597.
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 | 897 | 55.9% |
| dimeric | 2 | 591 | 36.8% |
| trimeric | 3 | 67 | 4.2% |
| tetrameric | 4 | 27 | 1.7% |
| dodecameric | 12 | 8 | 0.5% |
| pentameric | 5 | 3 | 0.2% |
| heptameric | 7 | 3 | 0.2% |
| hexameric | 6 | 2 | 0.1% |
1,159 entries have the depositor's assembly corroborated by PISA, 352 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. 85 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1KWP, 1NXK, 1NY3, 2H9V, 2HAK, 2I0E, 2OU7, 2OWB, 2PE2, 2PZY, 2R5T, 2RKU, 3A7G, 3A7H, 3A8W, 3A8X, 3AG9, 3D0E, 3DAE, 3DJ5.
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 | 179–272 | 1,483 |
| Regulator of G-protein Signalling 4, domain 2 | CATH 1.10.167.10 | 223–302 | 54 |
| Transferase(Phosphotransferase) domain 1 | CATH 1.10.510.10 | 247–436 | 1,404 |
| Jelly Rolls | CATH 2.60.120.10 | 293–414 | 35 |
| 1.10.287.1270 | CATH | 303–329 | 75 |
| PH domain-like | SCOP2B 8040941 | 4–117 | 24 |
| Protein kinase-like (PK-like) | SCOP2B 8034489 | 138–428 | 35 |
| Protein kinase-like (PK-like) | SCOP2B 8062547 | 145–445 | 32 |
| Protein kinase-like (PK-like) | SCOP2B 8042948 | 146–408 | 199 |
| Protein kinase-like (PK-like) | SCOP2B 8040369 | 146–477 | 16 |
| Protein kinase-like (PK-like) | SCOP2B 8062446 | 149–437 | 19 |
| Protein kinase-like (PK-like) | SCOP2B 8099168 | 152–429 | 31 |
ADP130 entries
ANP95 entries
ATP80 entries
STU43 entries
AMP37 entries
M7714 entries
RIP13 entries
SGV10 entries
ACP9 entries
DTD9 entries
5FI8 entries
T5L8 entries
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| MG | ion | Magnesium Ion | 213 | 1.13 |
| SO4 | ion | Sulfate Ion | 186 | 1.13 |
| EDO | cryoprotectant | 1,2-Ethanediol | 131 | 1.47 |
| ADP | cofactor | Adenosine-5'-Diphosphate | 130 | 1.24 |
| CL | ion | Chloride Ion | 129 | 1.09 |
| GOL | cryoprotectant | Glycerol | 129 | 1.13 |
| DMS | cryoprotectant | Dimethyl Sulfoxide | 118 | 1.09 |
| ANP | cofactor | Phosphoaminophosphonic Acid-Adenylate Ester | 95 | 1.35 |
| MPD | cryoprotectant | (4s)-2-Methyl-2,4-Pentanediol | 86 | 1.12 |
| ATP | cofactor | Adenosine-5'-Triphosphate | 80 | 1.09 |
| STU | ligand | Staurosporine | 43 | 1.78 |
| ZN | ion | Zinc Ion | 40 | 1.85 |
| AMP | cofactor | Adenosine Monophosphate | 37 | 1.31 |
| CA | ion | Calcium Ion | 31 | 1.55 |
| ACT | cryoprotectant | Acetate Ion | 31 | 1.30 |
| MN | ion | Manganese (Ii) Ion | 28 | 1.50 |
| PO4 | ion | Phosphate Ion | 25 | 1.26 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 25 | 1.41 |
| NA | ion | Sodium Ion | 24 | 1.13 |
| MES | buffer | 2-(N-Morpholino)-Ethanesulfonic Acid | 16 | 1.40 |
Parsed from the free text 1,465 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 1,481
entries that recorded anything at all.
Median pH 7.0
(range 3.8 to 10.5).
1,602 entries carry a wwPDB validation report: 623 clean, 601 worth a check and 378 with something to explain. Median clashscore 4.62, median RSRZ outliers 3.76%, median R-free minus R-work 0.041. 1,544 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 1,043 | 0.98 | 917 | 100% |
| Cricetulus griseus | 159 | 1.12 | 151 | 61% |
| Bos taurus | 129 | 1.55 | 119 | 62% |
| Mus musculus | 109 | 1.26 | 89 | 72% |
| Toxoplasma gondii | 45 | 1.80 | 42 | 57% |
| Rattus norvegicus | 22 | 1.70 | 13 | 66% |
| Xenopus laevis | 14 | 1.49 | 12 | 59% |
| Arabidopsis thaliana | 9 | 1.90 | 2 | 56% |
| Saccharomyces cerevisiae | 9 | 2.20 | 2 | 63% |
| Danio rerio | 7 | 2.30 | 4 | 55% |
| Plasmodium vivax Sal-1 | 7 | 2.30 | 7 | 58% |
| Caenorhabditis elegans | 6 | 1.72 | 0 | 52% |
480 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 | Natural Product-like Fragments Unlock Novel Chemotypes for a Kinase Target─Exploring Options beyond the Flatland. J.Chem.Inf.Model. doi:10.1021/acs.jcim.5c01952 |
| 2026 | A PKA-selective inhibitor captures an open but more ordered conformation of the PKA catalytic subunit. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2536312123 |
| 2026 | Selective miniprotein inhibitors of Aurora-A kinase designed using interaction-motif scaffolding Biorxiv doi:10.64898/2026.07.12.737516 |
| 2026 | Lead Optimization of TgCDPK1 Inhibitors for the Treatment of Toxoplasmosis. J.Med.Chem. doi:10.1021/acs.jmedchem.6c00065 |
| 2026 | Isoform-Selective Targeting of Akt Through Covalent Allosteric Inhibition. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.3567206 |
| 2026 | Structure-Based Design of Potent and Highly Selective NUAK1 Inhibitors by Exploiting a Unique Glutamate Switch for the Prevention of Tumor Growth, Migration, and Invasion. J.Med.Chem. doi:10.1021/acs.jmedchem.5c03079 |
| 2026 | High-throughput discovery and characterisation of pentafluorobenzene sulfonamide modifiers of Aurora A kinase. Rsc Chem Biol doi:10.1039/d5cb00290g |
| 2026 | Bacterial ubiquitin ligase engineered for small molecule and protein target identification. Embo J. doi:10.1038/s44318-025-00665-0 |
| 2026 | Molecular basis of allosteric regulation and pharmaceutical targeting of protein kinase C beta. Nat Commun doi:10.1038/s41467-026-73413-5 |
| 2026 | Structural basis for the recruitment and selective phosphorylation of Akt by mTORC2. Science doi:10.1126/science.adv7111 |
| 2026 | An orally available PfPKG inhibitor blocks Plasmodium's infection of the liver. Plos Pathog. doi:10.1371/journal.ppat.1014322 |
| 2026 | High-resolution cryo-EM structures of small protein-ligand complexes near the theoretical size limit. Nat Commun doi:10.1038/s41467-026-71934-7 |
| 2026 | Selective targeting of endothelial and perivascular angiocrine ROCK2 treats liver fibrosis. Cell doi:10.1016/j.cell.2026.02.001 |
| 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 | Integrating Hydrogen Exchange with Molecular Dynamics for Improved Ligand Binding Predictions. J.Chem.Inf.Model. doi:10.1021/acs.jcim.5c00397 |
| 2025 | Targeting N-Myc in neuroblastoma with selective Aurora kinase A degraders. Cell Chem Biol doi:10.1016/j.chembiol.2024.12.006 |
| 2025 | Discovery of Potent, Selective and Efficacious Aminopyrazole Inhibitors of PLK4. J.Med.Chem. doi:10.1021/acs.jmedchem.5c02200 |
| 2025 | Identification of a p21-activated kinase 1 (PAK1) inhibitor with 10-fold selectivity against PAK2. Bioorg.Med.Chem.Lett. doi:10.1016/j.bmcl.2025.130307 |
| 2025 | Mutant-selective AKT inhibition through lysine targeting and neo-zinc chelation. Nature doi:10.1038/s41586-024-08176-4 |
| 2025 | Probing the Protein Kinases' Cysteinome by Covalent Fragments. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202419736 |
| 2025 | Polo-like kinase 1-inhibitor co-complex structures via the surface-entropy reduction approach and a DARPin-assisted approach. Acta Crystallogr D Struct Biol doi:10.1107/S2059798325009325 |
| 2025 | Discovery of RP-1664: A First-in-Class Orally Bioavailable, Selective PLK4 Inhibitor. J.Med.Chem. doi:10.1021/acs.jmedchem.5c00529 |
| 2025 | A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation. Nat Commun doi:10.1038/s41467-025-63249-w |
| 2025 | Structural basis for MEKK2 dimerization and substrate recognition. Nat Commun doi:10.1038/s41467-025-66884-5 |
| 2025 | Mechanism and cellular actions of the potent AMPK inhibitor BAY-3827. Sci Adv doi:10.1126/sciadv.adx2434 |
| 2025 | Cell-Active, Arginine-Targeting Irreversible Covalent Inhibitors for Non-Kinases and Kinases. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202422372 |
| 2025 | Capture, mutual inhibition and release mechanism for aPKC-Par6 and its multisite polarity substrate Lgl. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01425-0 |
| 2025 | Structural insights into the catalytic cycle of G protein-coupled receptor kinase 5 and a possible regulatory site for potassium ion. J.Biol.Chem. doi:10.1016/j.jbc.2025.110309 |
| 2025 | Crystal structures of PAK2 reveal new insights into its autoinhibitory mechanism. Structure doi:10.1016/j.str.2025.07.008 |
| 2025 | Harnessing free energy calculations for kinome-wide selectivity in drug discovery campaigns with a Wee1 case study. Nat Commun doi:10.1038/s41467-025-62722-w |
| 2025 | Design, synthesis, and X-ray structural studies of a series of highly potent, selective, and drug-like G protein-coupled receptor kinase 5 inhibitors. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2024.117024 |
| 2025 | Chemical Evolution of Aplithianine Class of Serine/Threonine Kinase Inhibitors. J.Med.Chem. doi:10.1021/acs.jmedchem.5c00649 |
| 2025 | O -Cyanobenzaldehydes Irreversibly Modify Both Buried and Exposed Lysine Residues in Live Cells. J.Am.Chem.Soc. doi:10.1021/jacs.4c18006 |
| 2025 | Optimization of Novel Quinazolines as Potent Aurora Kinase Inhibitors for Triple-Negative Breast Cancer Treatment. J.Med.Chem. doi:10.1021/acs.jmedchem.5c00107 |
| 2025 | Discovery and Optimization of Selective Inhibitors of Large Tumor Suppressor Kinases LATS1 and 2 for In Vivo Investigation of the Hippo-YAP Pathway in Tissue Regeneration. J.Med.Chem. doi:10.1021/acs.jmedchem.5c00350 |
| 2025 | A twist in the tale: shifting from covalent targeting of a tyrosine in JAK3 to a lysine in MK2. Rsc Med Chem doi:10.1039/d5md00440c |
| 2025 | Polarity protein Par6 facilitates the processive phosphorylation of Lgl via a dynamic interaction with aPKC. Commun Biol doi:10.1038/s42003-025-08401-4 |
| 2025 | Penetrant PKC beta mutation in ATLL displays a mixed gain-of-function. Biochem.J. doi:10.1042/BCJ20253384 |
| 2025 | N3A motifs in RI beta mediate allosteric crosstalk between cAMP and ATP in PKA activation. Protein Sci. doi:10.1002/pro.70332 |
| 2025 | Multiplicity of Regulatory Subunit Conformations Defines Structural Ensemble of Reset Protein Kinase A Holoenzyme. J.Am.Chem.Soc. doi:10.1021/jacs.4c16269 |