Overview
Basic information about this protein and its source genome.
- Accession
- KP13_00022
- Gene
- atpH AHE47131.1
- Status
- annotated
- Amino acids
- 177
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 24.118
- Human E-value
- 2.5e-10
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 88.136
- DEG E-value
- 6.309999999999999e-115
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 75.85
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)
5- GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- GO:0015986 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a membrane to generate an electrochemical gradient (proton-motive force).
- GO:0046933 Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + phosphate + 5 H+(out) => ATP + H2O + 4 H+(in).
- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
- GO:0045259 A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 74 | 85 | PRINTS | PR00125 | ATP synthase delta subunit signature |
| 74 | 85 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 85 | 99 | PRINTS | PR00125 | ATP synthase delta subunit signature |
| 85 | 99 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 7 | 26 | PRINTS | PR00125 | ATP synthase delta subunit signature |
| 7 | 26 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 150 | 168 | PRINTS | PR00125 | ATP synthase delta subunit signature |
| 150 | 168 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 135 | 150 | PRINTS | PR00125 | ATP synthase delta subunit signature |
| 135 | 150 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 3 | 177 | Hamap | MF_01416 | ATP synthase subunit delta [atpD]. |
| 3 | 177 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 137 | 156 | ProSitePatterns | PS00389 | ATP synthase delta (OSCP) subunit signature. |
| 137 | 156 | InterPro | IPR020781 | ATPase, OSCP/delta subunit, conserved site |
| 2 | 106 | FunFam | G3DSA:1.10.520.20:FF:000001 | ATP synthase subunit delta |
| 3 | 104 | SUPERFAMILY | SSF47928 | N-terminal domain of the delta subunit of the F1F0-ATP synthase |
| 3 | 104 | InterPro | IPR026015 | F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily |
| 7 | 175 | NCBIfam | TIGR01145 | ATP synthase F1 subunit delta |
| 7 | 175 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 7 | 174 | Pfam | PF00213 | ATP synthase delta (OSCP) subunit |
| 7 | 174 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 6 | 176 | PANTHER | PTHR11910 | ATP SYNTHASE DELTA CHAIN |
| 6 | 176 | InterPro | IPR000711 | ATPase, OSCP/delta subunit |
| 2 | 106 | Gene3D | G3DSA:1.10.520.20 | - |
| 2 | 106 | InterPro | IPR026015 | F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily |
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_A0A0H3GXU5
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_00022
|
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 |
|---|---|---|---|---|---|---|---|
| 3 | 0.66 | ||||||
| 7 | 0.444 |
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.678 | ||||||
| 2 | 0.468 |
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 | P48047 | 7.69 | 503.5 Da LogP 5.75 TPSA 97.6 | 2 viol. | ✓ Clean |
Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…
|
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 |
|---|---|---|---|---|---|
| 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)…
|
| 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.