Homo sapiens · seed P07900 · 732 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt P07900 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.30.565.10 CATH 3.30.230.80 CATH 3.40.50.11260 CATH 1.20.120.790 SCOP 8041007 SCOP 8042891 SCOP 8070946 SCOP 8070952 SCOP 8041505 SCOP 8070970 SCOP 8070964 SCOP 8056863 RCSB 5LO5 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.
5LO5, 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.
173 distinct constructs across 675 entries. 645 polymer entities differ from the UniProt canonical sequence in some way, 137 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 |
|---|---|---|---|---|
| 91 | 237 | 1.38 | 7HBS | residues 8-244; Q8M, E237L, K238E +6 more |
| 39 | 236 | 1.40 | 1UYL | residues 1-236 |
| 24 | 228 | 1.20 | 3T0H | residues 9-236 |
| 21 | 236 | 1.50 | 2GQP | residues 65-337; 1 internal deletion; Q65G, I66S, R67H +5 more |
| 19 | 256 | 1.47 | 3O0I | His6; Thrombin site; residues 1-236 |
| 16 | 249 | 1.66 | 2XJX | His6; residues 1-236; 1 internal deletion; M1V, E3R, E4G +3 more |
| 15 | 252 | 1.55 | 2YEF | His10; residues 1-236; M1I, P2D, E3D +5 more |
| 14 | 214 | 1.50 | 2IWX | residues 1-214 |
| 14 | 229 | 1.44 | 5LO5 | residues 8-236; Q8G |
| 13 | 237 | 1.45 | 7S9H | residues 1-236 |
| 11 | 230 | 1.70 | 4B7P | residues 7-236; T7G, Q8P |
| 11 | 233 | 1.65 | 4NH8 | residues 4-236; E4G, T5S, Q6L +2 more |
| 9 | 209 | 1.32 | 2YK9 | residues 15-223; E15G, E16H, V17M |
| 9 | 226 | 1.55 | 3EKO | residues 8-233; Q8M, R226L, D227E +6 more |
| 9 | 229 | 1.30 | 3WHA | residues 8-236; Q8M |
| 9 | 259 | 1.20 | 4XE2 | His6+T7; Enterokinase site; residues 1-223 |
| 8 | 238 | 1.61 | 4YKR | residues 1-236; M1A |
| 8 | 502 | 2.40 | 5Y3N | residues 60-561 |
| 7 | 220 | 1.80 | 1AH6 | residues 1-220 |
| 7 | 232 | 1.56 | 9MSU | residues 1-232; E219N, V220L, P221Y +11 more |
| 7 | 256 | 1.34 | 6GR5 | His6; Thrombin site; residues 1-236; K112R |
| 7 | 256 | 1.48 | 6GPO | His6; Thrombin site; residues 1-236; K112A |
| 7 | 705 | 2.71 | 6XLG | matches the canonical sequence |
| 7 | 732 | 2.56 | 7KRJ | matches the canonical sequence |
| 6 | 215 | 1.33 | 7D1V | residues 10-224 |
Showing the 25 most-used of 173.
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 | 488 | 72.3% |
| dimeric | 2 | 139 | 20.6% |
| tetrameric | 4 | 24 | 3.6% |
| trimeric | 3 | 9 | 1.3% |
| hexameric | 6 | 8 | 1.2% |
| pentameric | 5 | 5 | 0.7% |
| 70-meric | 70 | 1 | 0.1% |
| eicosameric | 20 | 1 | 0.1% |
305 entries have the depositor's assembly corroborated by PISA, 320 carry the depositor's word alone and 48 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 44 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 1TC0, 1TC6, 2AKP, 2IOP, 3B24, 3B25, 3B26, 3B28, 3EKO, 3EKR, 3HJC, 3HYY, 3HZ1, 3HZ5, 3K98, 3K99, 3PEH, 3PEJ, 3R4N, 3R4O.
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 |
|---|---|---|---|
| Histidine kinase-like ATPase, C-terminal domain | CATH 3.30.565.10 | 18–231 | 446 |
| 3.30.230.80 | CATH | 293–439 | 30 |
| 3.40.50.11260 | CATH | 448–547 | 24 |
| Heat shock protein 90, C-terminal domain | CATH 1.20.120.790 | 548–697 | 14 |
| GHKL (Gyrase, Hsp90, Histidine Kinase, MutL) domain-like | SCOP2B 8041007 | 18–225 | 427 |
| GHKL (Gyrase, Hsp90, Histidine Kinase, MutL) domain-like | SCOP2B 8042891 | 19–231 | 39 |
| GHKL (Gyrase, Hsp90, Histidine Kinase, MutL) domain-like | SCOP2B 8070946 | 19–230 | 16 |
| GHKL (Gyrase, Hsp90, Histidine Kinase, MutL) domain-like | SCOP2B 8070952 | 27–237 | 25 |
| GHKL (Gyrase, Hsp90, Histidine Kinase, MutL) domain-like | SCOP2B 8041505 | 35–250 | 24 |
| GHKL (Gyrase, Hsp90, Histidine Kinase, MutL) domain-like | SCOP2B 8070970 | 44–256 | 25 |
| GHKL (Gyrase, Hsp90, Histidine Kinase, MutL) domain-like | SCOP2B 8070964 | 52–262 | 8 |
| HSP90 middle pre-C-terminal domain | SCOP2B 8056863 | 463–547 | 6 |
ADP40 entries
ANP30 entries
ATP25 entries
GDM10 entries
42C6 entries
RDC5 entries
94M5 entries
NEC4 entries
2GJ4 entries
E0G4 entries
AGS4 entries
H713 entries
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| MG | ion | Magnesium Ion | 121 | 1.21 |
| GOL | cryoprotectant | Glycerol | 40 | 1.30 |
| ADP | cofactor | Adenosine-5'-Diphosphate | 40 | 1.34 |
| ANP | cofactor | Phosphoaminophosphonic Acid-Adenylate Ester | 30 | 1.50 |
| SO4 | ion | Sulfate Ion | 30 | 1.60 |
| ATP | cofactor | Adenosine-5'-Triphosphate | 25 | 2.19 |
| PG4 | cryoprotectant | Tetraethylene Glycol | 23 | 1.50 |
| DMS | cryoprotectant | Dimethyl Sulfoxide | 18 | 1.57 |
| EDO | cryoprotectant | 1,2-Ethanediol | 17 | 1.45 |
| CL | ion | Chloride Ion | 15 | 1.17 |
| K | ion | Potassium Ion | 14 | 1.50 |
| 1PE | cryoprotectant | Pentaethylene Glycol | 11 | 1.50 |
| PO4 | ion | Phosphate Ion | 11 | 1.55 |
| GDM | ligand | Geldanamycin | 10 | 1.50 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 7 | 1.50 |
| 42C | ligand | N,n-Dimethyl-7h-Purin-6-Amine | 6 | 1.82 |
| RDC | ligand | Radicicol | 5 | 1.60 |
| 94M | ligand | 6-Chloro-9-[(4-Methoxy-3,5-Dimethylpyridin-2-Yl)methyl]-9h-Purin | 5 | 1.79 |
| CO | ion | Cobalt (Ii) Ion | 5 | 2.29 |
| BEF | ion | Beryllium Trifluoride Ion | 5 | 2.35 |
Parsed from the free text 500 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 572
entries that recorded anything at all.
Median pH 7.0
(range 4.2 to 9.0).
673 entries carry a wwPDB validation report: 329 clean, 252 worth a check and 92 with something to explain. Median clashscore 4.39, median RSRZ outliers 3.35%, median R-free minus R-work 0.035. 656 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Homo sapiens | 496 | 1.17 | 461 | 100% |
| Saccharomyces cerevisiae | 46 | 1.50 | 33 | 93% |
| Canis lupus familiaris | 39 | 1.50 | 35 | 94% |
| Danio rerio | 10 | 1.75 | 11 | 92% |
| Candida albicans SC5314 | 10 | 1.64 | 9 | 30% |
| Dictyostelium discoideum | 9 | 1.20 | 5 | 30% |
| Escherichia coli | 9 | 1.65 | 3 | 92% |
| Mus musculus | 8 | 1.33 | 8 | 99% |
| Candida albicans | 7 | 1.56 | 7 | 30% |
| Saccharomyces cerevisiae S288C | 7 | 2.71 | 6 | 98% |
| Plasmodium falciparum 3D7 | 5 | 1.88 | 4 | 63% |
| Cryptococcus neoformans | 5 | 1.91 | 4 | 29% |
732 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 | Unperturbed hydration structure involves ADP recognition in the N-terminal domain of human heat shock protein 90 alpha. Protein Sci. doi:10.1002/pro.70619 |
| 2026 | The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle. Mol.Cell doi:10.1016/j.molcel.2025.12.002 |
| 2026 | Structural basis for chaperone-guided assembly of RNA-induced silencing complex. Nature doi:10.1038/s41586-026-10640-2 |
| 2026 | Structural basis of HSP90C, a highly active chloroplastic HSP90 chaperone from Arabidopsis thaliana. J.Mol.Biol. doi:10.1016/j.jmb.2026.169935 |
| 2026 | Structural basis of regulated N-glycosylation at the secretory translocon. Nature doi:10.1038/s41586-025-09756-8 |
| 2026 | Structural and binding studies of the mycobacterial heat shock protein reveal a silent state and offer insights into dendritic cell activation. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2026.151218 |
| 2026 | FKBP8 connects the Hsp70-Hsp90 chaperone machinery to the folding of membrane proteins. Nat Commun doi:10.1038/s41467-026-74519-6 |
| 2026 | Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation. Nat Commun doi:10.1038/s41467-026-73400-w |
| 2025 | Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening. Iucrj doi:10.1107/S2052252524012247 |
| 2025 | Selective Inhibition of hsp90 Paralogs: Uncovering the Role of Helix 1 in Grp94-Selective Ligand Binding. Proteins doi:10.1002/prot.26756 |
| 2025 | Structural Insights into Selectively Targeting Candida albicans Hsp90. Biochemistry doi:10.1021/acs.biochem.5c00015 |
| 2025 | Chaperone directed heterobifunctional molecules circumvent KRAS G12C inhibitor resistance. Cancer Lett. doi:10.1016/j.canlet.2025.217691 |
| 2024 | Accurate Characterization of Binding Kinetics and Allosteric Mechanisms for the HSP90 Chaperone Inhibitors Using AI-Augmented Integrative Biophysical Studies. Jacs Au doi:10.1021/jacsau.4c00123 |
| 2024 | Crystal structure of the N-terminal domain of Candida glabrata Hsp90 Biodesign doi:10.34184/kssb.2024.12.2.13 |
| 2024 | Aminomethyl Salicylaldehydes Lock onto a Surface Lysine by Forming an Extended Intramolecular Hydrogen Bond Network. J.Am.Chem.Soc. doi:10.1021/jacs.4c04314 |
| 2024 | Structural Insights into the Activation of Human Aryl Hydrocarbon Receptor by the Environmental Contaminant Benzo[a]pyrene and Structurally Related Compounds. J.Mol.Biol. doi:10.1016/j.jmb.2023.168411 |
| 2024 | Structural dynamics of RAF1-HSP90-CDC37 and HSP90 complexes reveal asymmetric client interactions and key structural elements. Commun Biol doi:10.1038/s42003-024-05959-3 |
| 2024 | Structural basis for the dynamic chaperoning of disordered clients by Hsp90. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01337-z |
| 2024 | Modelling protein complexes with crosslinking mass spectrometry and deep learning Nat. Commun. doi:10.1038/s41467-024-51771-2 |
| 2023 | Elucidation of novel TRAP1-Selective inhibitors that regulate mitochondrial processes. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2023.115531 |
| 2023 | Pan-HSP90 ligand binding reveals isoform-specific differences in plasticity and water networks. Protein Sci. doi:10.1002/pro.4629 |
| 2023 | Targeting Borrelia burgdorferi HtpG with a berserker molecule, a strategy for anti-microbial development. Cell Chem Biol doi:10.1016/j.chembiol.2023.10.004 |
| 2023 | The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the Prognosis of Alzheimer's Disease. Biomolecules doi:10.3390/biom13071051 |
| 2023 | Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor. Nat.Struct.Mol.Biol. doi:10.1038/s41594-023-01128-y |
| 2023 | Unique interface and dynamics of the complex of HSP90 with a specialized cochaperone AIPL1. Structure doi:10.1016/j.str.2022.12.014 |
| 2023 | Cryo-EM structure of the cytosolic AhR complex. Structure doi:10.1016/j.str.2022.12.013 |
| 2023 | Hsp90 provides a platform for kinase dephosphorylation by PP5. Nat Commun doi:10.1038/s41467-023-37659-7 |
| 2023 | Structural insight into guanylyl cyclase receptor hijacking of the kinase-Hsp90 regulatory mechanism. Elife doi:10.7554/eLife.86784 |
| 2022 | Water Networks Repopulate Protein-Ligand Interfaces with Temperature. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202112919 |
| 2022 | Structure-Activity Relationship Study of Tertiary Alcohol Hsp90 alpha-Selective Inhibitors with Novel Binding Mode. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.2c00327 |
| 2022 | Structural Characterization of Human Heat Shock Protein 90 N-Terminal Domain and Its Variants K112R and K112A in Complex with a Potent 1,2,3-Triazole-Based Inhibitor. Int J Mol Sci doi:10.3390/ijms23169458 |
| 2022 | Structural basis of the key residue W320 responsible for Hsp90 conformational change. J.Biomol.Struct.Dyn. doi:10.1080/07391102.2022.2146197 |
| 2022 | Dipyridamole interacts with the N-terminal domain of HSP90 and antagonizes the function of the chaperone in multiple cancer cell lines. Biochem Pharmacol doi:10.1016/j.bcp.2022.115376 |
| 2022 | Cryo-EM structure of the agonist-bound Hsp90-XAP2-AHR cytosolic complex. Nat Commun doi:10.1038/s41467-022-34773-w |
| 2022 | Structure of the RAF1-HSP90-CDC37 complex reveals the basis of RAF1 regulation. Mol.Cell doi:10.1016/j.molcel.2022.08.012 |
| 2022 | HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation. Nat Commun doi:10.1038/s41467-022-35143-2 |
| 2022 | Crystal structure of the middle and C-terminal domains of Hsp90 alpha labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target. Acta Crystallogr D Struct Biol doi:10.1107/S2059798322002261 |
| 2022 | Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism. Nature doi:10.1038/s41586-021-04252-1 |
| 2022 | Visualizing the transiently populated closed-state of human HSP90 ATP binding domain. Nat Commun doi:10.1038/s41467-022-35399-8 |
| 2021 | Design and Synthesis of TRAP1 Selective Inhibitors: H-Bonding with Asn171 Residue in TRAP1 Increases Paralog Selectivity. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.1c00213 |