Overview
Basic information about this protein and its source genome.
- Accession
- KP13_00850
- Gene
- AHE43214.1 fdx
- Status
- annotated
- Amino acids
- 111
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 41.121
- Human E-value
- 5e-14
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 91.892
- DEG E-value
- 4.15e-73
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 95.9
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:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
- GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
- GO:0140647 A electron transport chain in which one or more electron carriers operate to transfer electrons from donors to a cytochrome P450 protein or domain. Electron carriers operating in this chain include FAD-containing flavoproteins or domains, FMN domains, ferredoxins and cytochrome b5. The reduced cytochrome P450 functions as the terminal oxidase and participates in a wide range of biochemical pathways.
- GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0046872 Binding to a metal ion.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 111 | Gene3D | G3DSA:3.10.20.30 | - |
| 1 | 111 | InterPro | IPR012675 | Beta-grasp domain superfamily |
| 42 | 52 | ProSitePatterns | PS00814 | Adrenodoxin family, iron-sulfur binding region signature. |
| 42 | 52 | InterPro | IPR018298 | Adrenodoxin, iron-sulphur binding site |
| 2 | 111 | NCBIfam | TIGR02007 | ferredoxin, 2Fe-2S type, ISC system |
| 2 | 111 | InterPro | IPR011536 | Ferredoxin 2Fe-2S type, proteobacteria |
| 42 | 52 | PRINTS | PR00355 | Adrenodoxin signature |
| 42 | 52 | InterPro | IPR001055 | Adrenodoxin |
| 60 | 74 | PRINTS | PR00355 | Adrenodoxin signature |
| 60 | 74 | InterPro | IPR001055 | Adrenodoxin |
| 83 | 91 | PRINTS | PR00355 | Adrenodoxin signature |
| 83 | 91 | InterPro | IPR001055 | Adrenodoxin |
| 1 | 111 | FunFam | G3DSA:3.10.20.30:FF:000008 | Ferredoxin, 2Fe-2S type, ISC system |
| 4 | 109 | SUPERFAMILY | SSF54292 | 2Fe-2S ferredoxin-like |
| 4 | 109 | InterPro | IPR036010 | 2Fe-2S ferredoxin-like superfamily |
| 14 | 92 | Pfam | PF00111 | 2Fe-2S iron-sulfur cluster binding domain |
| 14 | 92 | InterPro | IPR001041 | 2Fe-2S ferredoxin-type iron-sulfur binding domain |
| 2 | 104 | ProSiteProfiles | PS51085 | 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. |
| 2 | 104 | InterPro | IPR001041 | 2Fe-2S ferredoxin-type iron-sulfur binding domain |
| 18 | 108 | PANTHER | PTHR23426 | FERREDOXIN/ADRENODOXIN |
| 18 | 108 | InterPro | IPR001055 | Adrenodoxin |
| 14 | 99 | CDD | cd00207 | fer2 |
| 14 | 99 | InterPro | IPR001041 | 2Fe-2S ferredoxin-type iron-sulfur binding domain |
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_A0A0H3GWP7
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_00850
|
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.563 | ||||||
| 5 | 0.004 | ||||||
| 2 | 0.001 | ||||||
| 3 | 0.0 |
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 | 0.47 | ||||||
| 2 | 0.012 | ||||||
| 3 | 0.011 | ||||||
| 4 | 0.005 |
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 |
|---|---|---|---|---|---|---|
| FES | P0A9R4 | 175.8 Da LogP 1.29 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
S1[Fe]S[Fe]1
|
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.