Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01980
- Gene
- AHE46418.1 dnaJ
- Status
- annotated
- Amino acids
- 377
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 61.29
- Human E-value
- 4.18e-07
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 80.637
- DEG E-value
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 84.59
Selected Druggability evidence
AlphaFold / UniProt modelSelected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
9- GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
- GO:0031072 Binding to a heat shock protein, a protein synthesized or activated in response to heat shock.
- GO:0051082 Binding to an unfolded protein.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0009408 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0008270 Binding to a zinc ion (Zn).
- GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
- GO:0042026 The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 7 | 25 | PRINTS | PR00625 | DnaJ domain signature |
| 7 | 25 | InterPro | IPR001623 | DnaJ domain |
| 42 | 62 | PRINTS | PR00625 | DnaJ domain signature |
| 42 | 62 | InterPro | IPR001623 | DnaJ domain |
| 62 | 81 | PRINTS | PR00625 | DnaJ domain signature |
| 62 | 81 | InterPro | IPR001623 | DnaJ domain |
| 25 | 40 | PRINTS | PR00625 | DnaJ domain signature |
| 25 | 40 | InterPro | IPR001623 | DnaJ domain |
| 4 | 62 | SMART | SM00271 | dnaj_3 |
| 4 | 62 | InterPro | IPR001623 | DnaJ domain |
| 5 | 70 | ProSiteProfiles | PS50076 | dnaJ domain profile. |
| 5 | 70 | InterPro | IPR001623 | DnaJ domain |
| 47 | 66 | ProSitePatterns | PS00636 | Nt-dnaJ domain signature. |
| 47 | 66 | InterPro | IPR018253 | DnaJ domain, conserved site |
| 5 | 67 | Pfam | PF00226 | DnaJ domain |
| 5 | 67 | InterPro | IPR001623 | DnaJ domain |
| 253 | 356 | Gene3D | G3DSA:2.60.260.20 | - |
| 1 | 113 | Gene3D | G3DSA:1.10.287.110 | DnaJ domain |
| 1 | 113 | InterPro | IPR036869 | Chaperone J-domain superfamily |
| 252 | 360 | FunFam | G3DSA:2.60.260.20:FF:000004 | Molecular chaperone DnaJ |
| 2 | 371 | Hamap | MF_01152 | Chaperone protein DnaJ [dnaJ]. |
| 2 | 371 | InterPro | IPR012724 | Chaperone DnaJ |
| 132 | 210 | ProSiteProfiles | PS51188 | Zinc finger CR-type profile. |
| 132 | 210 | InterPro | IPR001305 | Heat shock protein DnaJ, cysteine-rich domain |
| 145 | 205 | CDD | cd10719 | DnaJ_zf |
| 145 | 205 | InterPro | IPR001305 | Heat shock protein DnaJ, cysteine-rich domain |
| 5 | 350 | PANTHER | PTHR43096 | DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED |
| 137 | 210 | FunFam | G3DSA:2.10.230.10:FF:000002 | Molecular chaperone DnaJ |
| 118 | 331 | Pfam | PF01556 | DnaJ C terminal domain |
| 118 | 331 | InterPro | IPR002939 | Chaperone DnaJ, C-terminal |
| 5 | 348 | NCBIfam | TIGR02349 | molecular chaperone DnaJ |
| 5 | 348 | InterPro | IPR012724 | Chaperone DnaJ |
| 5 | 59 | CDD | cd06257 | DnaJ |
| 5 | 59 | InterPro | IPR001623 | DnaJ domain |
| 112 | 260 | SUPERFAMILY | SSF49493 | HSP40/DnaJ peptide-binding domain |
| 112 | 260 | InterPro | IPR008971 | HSP40/DnaJ peptide-binding |
| 1 | 107 | SUPERFAMILY | SSF46565 | Chaperone J-domain |
| 1 | 107 | InterPro | IPR036869 | Chaperone J-domain superfamily |
| 1 | 113 | FunFam | G3DSA:1.10.287.110:FF:000003 | Molecular chaperone DnaJ |
| 145 | 205 | Pfam | PF00684 | DnaJ central domain |
| 116 | 334 | CDD | cd10747 | DnaJ_C |
| 114 | 250 | Gene3D | G3DSA:2.60.260.20 | - |
| 132 | 209 | SUPERFAMILY | SSF57938 | DnaJ/Hsp40 cysteine-rich domain |
| 132 | 209 | InterPro | IPR036410 | Heat shock protein DnaJ, cysteine-rich domain superfamily |
| 257 | 342 | SUPERFAMILY | SSF49493 | HSP40/DnaJ peptide-binding domain |
| 257 | 342 | InterPro | IPR008971 | HSP40/DnaJ peptide-binding |
| 137 | 210 | Gene3D | G3DSA:2.10.230.10 | - |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GIZ3
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01980
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 29 | 0.047 | ||||||
| 26 | 0.013 | ||||||
| 7 | 0.012 | ||||||
| 1 | 0.002 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 1.22 | 0.01 | ||||||
| 2 | 1.05 | 0.006 |
Ligand evidence
Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.
No PDB ligands found through similar proteins.
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
| Ligand | UniProt (homolog) | pchembl | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| DWT | Q9NXW2 | 9.09 | 503.5 Da LogP 5.75 TPSA 97.6 | 2 viol. | ✓ Clean |
Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…
|
| CHEMBL4129274 | O75190 | — | 851.5 Da LogP 4.76 TPSA 183.3 | 3 viol. | Alert |
C=CC(=O)Nc1ccccc1Nc1nc(Nc2ccc(N3CCN(CCOCCOCCOCC…
|
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC71842002 | 0.552 | 445.6 Da LogP 2.04 TPSA 76.7 | ✓ Ro5 | ✓ Clean |
O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NCCCN1CC…
|
| ZINC220133900 | 0.538 | 398.3 Da LogP 3.77 TPSA 85.1 | ✓ Ro5 | ✓ Clean |
Cc1nc2nc(-c3cccnc3)nn2cc1C(=O)Nc1cccc(C(F)(F)F)…
|
| ZINC20148987 | 0.532 | 414.4 Da LogP 4.50 TPSA 97.1 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C(=O)Nc2cccc(C(F)(F)F)c2)cc1Nc1cncc(C(N)…
|
| ZINC914431236 | 0.531 | 464.0 Da LogP 4.49 TPSA 85.4 | ✓ Ro5 | Alert |
C=CC(=O)Nc1ccccc1Nc1nc(Nc2ccc(N3CCN(C)CC3)cc2)n…
|
| ZINC9306398 | 0.512 | 398.3 Da LogP 3.77 TPSA 85.1 | ✓ Ro5 | ✓ Clean |
Cc1c(C(=O)Nc2cccc(C(F)(F)F)c2)cnc2nc(-c3cccnc3)…
|
| ZINC5049572 | 0.507 | 336.3 Da LogP 4.22 TPSA 58.2 | ✓ Ro5 | ✓ Clean |
CC(=O)Nc1cc(C(=O)Nc2cccc(C(F)(F)F)c2)ccc1C
|
PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.