Overview
Basic information about this protein and its source genome.
- Accession
- KP13_00026
- Gene
- atpC AHE47135.1
- Status
- annotated
- Amino acids
- 139
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 97.122
- DEG E-value
- 8.4e-97
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 82.06
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)
6- GO:0045261 OBSOLETE. The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.
- 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.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 5 | 132 | PANTHER | PTHR13822 | ATP SYNTHASE DELTA/EPSILON CHAIN |
| 5 | 132 | InterPro | IPR001469 | ATP synthase, F1 complex, delta/epsilon subunit |
| 91 | 134 | Gene3D | G3DSA:1.20.5.440 | - |
| 91 | 134 | FunFam | G3DSA:1.20.5.440:FF:000001 | ATP synthase epsilon chain |
| 6 | 127 | CDD | cd12152 | F1-ATPase_delta |
| 6 | 127 | InterPro | IPR001469 | ATP synthase, F1 complex, delta/epsilon subunit |
| 3 | 90 | Gene3D | G3DSA:2.60.15.10 | - |
| 3 | 90 | InterPro | IPR036771 | F0F1 ATP synthase delta/epsilon subunit, N-terminal |
| 3 | 131 | Hamap | MF_00530 | ATP synthase epsilon chain [atpC]. |
| 3 | 131 | InterPro | IPR001469 | ATP synthase, F1 complex, delta/epsilon subunit |
| 88 | 137 | SUPERFAMILY | SSF46604 | Epsilon subunit of F1F0-ATP synthase C-terminal domain |
| 88 | 137 | InterPro | IPR036794 | ATP synthase delta/epsilon subunit, C-terminal domain superfamily |
| 6 | 84 | Pfam | PF02823 | ATP synthase, Delta/Epsilon chain, beta-sandwich domain |
| 6 | 84 | InterPro | IPR020546 | ATP synthase, F1 complex, delta/epsilon subunit, N-terminal |
| 3 | 90 | FunFam | G3DSA:2.60.15.10:FF:000001 | ATP synthase epsilon chain |
| 89 | 133 | Pfam | PF00401 | ATP synthase, Delta/Epsilon chain, long alpha-helix domain |
| 89 | 133 | InterPro | IPR020547 | ATP synthase epsilon subunit, C-terminal domain |
| 3 | 86 | SUPERFAMILY | SSF51344 | Epsilon subunit of F1F0-ATP synthase N-terminal domain |
| 3 | 86 | InterPro | IPR036771 | F0F1 ATP synthase delta/epsilon subunit, N-terminal |
| 4 | 133 | NCBIfam | TIGR01216 | ATP synthase F1 subunit epsilon |
| 4 | 133 | InterPro | IPR001469 | ATP synthase, F1 complex, delta/epsilon subunit |
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_A0A0H3H4X9
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_00026
|
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 |
|---|---|---|---|---|---|---|---|
| 4 | 0.499 |
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 | 0.23 |
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.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| CAC | A0R1Z9 | 137.0 Da LogP -0.52 TPSA 40.1 | ✓ Ro5 | ✓ Clean |
C[As](=O)(C)[O-]
|
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).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
No virtual-screening candidates for this protein.
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.