Promising target candidate with multiple supporting evidence streams.
Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.
Main supporting evidence
Risks to review
Terms and data sources used on this page
PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.
AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.
ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.
pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.
FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.
Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.
PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.
ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.
ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.
LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.
Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.
DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.
Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.
EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.
KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.
Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.
Prioritization evidence
Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.
Off-target risk
- Human off-target
- No hit
- Gut microbiome similarity
- 2.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- N
- DEG identity (%)
- 0.0 Higher values support similarity to known essential genes.
Structure confidence
- ColabFold pLDDT
- 94.54 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelP2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MSTAKLVKSKASNLVYTRNDVADSEKKATIELLNRQVIQFIDLSLITKQAHWNMRGANFIAVHEMLDGFRTALTEHLDTMAERAVQLGGVALGTTQVINSKTPLQSYPLDIHHVQDHLKALADRYAVVANDVRKAIDEAKDEDTADIFTAASRDLDKFLWFIEANIE
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Subcellular localization
- Localization
- Cytoplasmic
Enzyme Commission (EC)
1Gene Ontology (GO)
7- GO:0008199 Binding to a ferric iron ion, Fe(III).
- GO:0016722 Catalysis of an oxidation-reduction in which the oxidation state of metal ion is altered.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0009295 The region of a virus, bacterial cell, mitochondrion or chloroplast to which the nucleic acid is confined.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0030261 The progressive compaction of dispersed interphase chromatin into threadlike chromosomes prior to mitotic or meiotic nuclear division, or during apoptosis, in eukaryotic cells.
- GO:0006879 A homeostatic process involved in the maintenance of a steady state level of iron ions within a cell.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 30 | 166 | Pfam | PF00210 | Ferritin-like domain |
| 30 | 166 | InterPro | IPR008331 | Ferritin/DPS protein domain |
| 10 | 167 | SUPERFAMILY | SSF47240 | Ferritin-like |
| 10 | 167 | InterPro | IPR009078 | Ferritin-like superfamily |
| 8 | 167 | PIRSF | PIRSF005900 | Dps |
| 8 | 167 | InterPro | IPR002177 | DNA-binding protein Dps |
| 77 | 91 | ProSitePatterns | PS00819 | Dps protein family signature 2. |
| 77 | 91 | InterPro | IPR023188 | DNA-binding protein Dps, conserved site |
| 1 | 167 | Hamap | MF_01441 | DNA protection during starvation protein [dps]. |
| 1 | 167 | InterPro | IPR023067 | DNA protection during starvation protein, gammaproteobacteria |
| 51 | 67 | ProSitePatterns | PS00818 | Dps protein family signature 1. |
| 51 | 67 | InterPro | IPR023188 | DNA-binding protein Dps, conserved site |
| 1 | 166 | PANTHER | PTHR42932 | GENERAL STRESS PROTEIN 20U |
| 1 | 166 | InterPro | IPR002177 | DNA-binding protein Dps |
| 144 | 162 | PRINTS | PR01346 | Helicobacter neutrophil-activating protein A family signature |
| 144 | 162 | InterPro | IPR002177 | DNA-binding protein Dps |
| 51 | 67 | PRINTS | PR01346 | Helicobacter neutrophil-activating protein A family signature |
| 51 | 67 | InterPro | IPR002177 | DNA-binding protein Dps |
| 75 | 91 | PRINTS | PR01346 | Helicobacter neutrophil-activating protein A family signature |
| 75 | 91 | InterPro | IPR002177 | DNA-binding protein Dps |
| 2 | 167 | FunFam | G3DSA:1.20.1260.10:FF:000003 | DNA protection during starvation protein |
| 2 | 167 | Gene3D | G3DSA:1.20.1260.10 | - |
| 2 | 167 | InterPro | IPR012347 | Ferritin-like |
| 31 | 166 | CDD | cd01043 | DPS |
| 31 | 166 | InterPro | IPR002177 | DNA-binding protein Dps |
3D structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.
How colors and pocket overlays are used
Pocket details Inspect a specific pocket, or open the full viewer
- Method
- -
- Score
- -
- Visible layer
- -
- Residues
- -
- Pocket properties
- -
Selecting a pocket opens its details and centers the viewer without clearing other active layers. Use Focus this pocket when you want to hide the rest; use Surface for the wider residue environment.
Binding pockets · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Residue sets
Binding pockets · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
All structural evidence
Structural evidence
0 + 2Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold DB
AF_A0A0H3GQL3
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_04308
|
ColabFold | — | — | full sequence | — | Loaded |
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.
Structural ligand evidence is available for this target.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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 |
|---|---|---|---|---|---|---|
| FEO RCSB PDB | P83695 | 127.7 Da LogP -0.07 TPSA 9.2 | ✓ Ro5 | ✓ Clean |
O([Fe])[Fe]
|
|
| OFE RCSB PDB | Q1X6M4 | 71.8 Da LogP -0.12 TPSA 17.1 | ✓ Ro5 | ✓ Clean |
O=[Fe]
|
|
| SIN RCSB PDB | Q99YU7 | 118.1 Da LogP -0.06 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C(CC(=O)O)C(=O)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).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC1529497 ZINC | 0.615 | 230.3 Da LogP 3.06 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCC(=O)O
|
| ZINC1531045 ZINC | 0.615 | 202.2 Da LogP 2.28 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCC(=O)O
|
| ZINC1593115 ZINC | 0.615 | 216.3 Da LogP 2.67 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCC(=O)O
|
| ZINC1700020 ZINC | 0.615 | 244.3 Da LogP 3.45 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCC(=O)O
|
| ZINC3860440 ZINC | 0.615 | 258.4 Da LogP 3.84 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCCC(=O)O
|
| ZINC3861298 ZINC | 0.615 | 286.4 Da LogP 4.62 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCCCCC(=O)O
|
| ZINC5113062 ZINC | 0.615 | 272.4 Da LogP 4.23 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCCCCCCC(=O)O
|
| ZINC1572706 ZINC | 0.563 | 260.2 Da LogP -1.05 TPSA 132.8 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)NCCNC(=O)CCC(=O)O
|
| ZINC1703342 ZINC | 0.533 | 202.2 Da LogP 1.07 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCC(=O)CCCC(=O)O
|
| ZINC1728397 ZINC | 0.533 | 233.2 Da LogP -0.29 TPSA 115.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CCN(CCC(=O)O)CCC(=O)O
|
| ZINC2508031 ZINC | 0.533 | 230.3 Da LogP 1.85 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCC(=O)CCCCC(=O)O
|
| ZINC2517013 ZINC | 0.533 | 250.2 Da LogP 0.89 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
O=C(O)CCP(CCC(=O)O)CCC(=O)O
|
| ZINC1697439 ZINC | 0.529 | 219.5 Da LogP 1.79 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)C(Cl)(Cl)Cl
|
| ZINC35465466 ZINC | 0.529 | 244.3 Da LogP 2.24 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCC(=O)CCC(=O)O
|
| ZINC39208104 ZINC | 0.529 | 262.2 Da LogP -0.20 TPSA 127.2 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)OCCOC(=O)CCC(=O)O
|
| ZINC145743383 ZINC | 0.500 | 266.2 Da LogP 0.77 TPSA 129.0 | ✓ Ro5 | ✓ Clean |
O=C(O)CCP(=O)(CCC(=O)O)CCC(=O)O
|
| ZINC1542984448 ZINC | 0.500 | 470.5 Da LogP 0.07 TPSA 148.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CCOCCOCCOCCOCCOCCOCCOCCOCCC(=O)O
|
| ZINC1586444 ZINC | 0.500 | 210.2 Da LogP -0.65 TPSA 108.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCS(=O)(=O)CCC(=O)O
|
| ZINC1753095 ZINC | 0.500 | 238.3 Da LogP 1.40 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)CCSCCSCCC(=O)O
|
| ZINC22028383 ZINC | 0.500 | 204.2 Da LogP -0.88 TPSA 98.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCNCCNCCC(=O)O
|
| ZINC22576322 ZINC | 0.500 | 348.4 Da LogP -0.51 TPSA 155.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCN(CCC(=O)O)CCN(CCC(=O)O)CCC(=O)O
|
| ZINC26897400 ZINC | 0.500 | 286.4 Da LogP 3.41 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCC(=O)CCCCCCC(=O)O
|
| ZINC3074813 ZINC | 0.500 | 258.3 Da LogP 2.63 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCC(=O)CCCCCC(=O)O
|
| ZINC34423725 ZINC | 0.500 | 342.5 Da LogP 4.97 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O
|
| ZINC35977596 ZINC | 0.500 | 294.3 Da LogP 0.00 TPSA 111.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CCOCCOCCOCCOCCC(=O)O
|
| ZINC38682833 ZINC | 0.500 | 286.3 Da LogP -0.61 TPSA 115.2 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)N1CCN(C(=O)CCC(=O)O)CC1
|
| ZINC39383060 ZINC | 0.500 | 206.2 Da LogP -0.03 TPSA 93.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CCOCCOCCC(=O)O
|
| ZINC39427081 ZINC | 0.500 | 250.2 Da LogP -0.01 TPSA 102.3 | ✓ Ro5 | ✓ Clean |
O=C(O)CCOCCOCCOCCC(=O)O
|
| ZINC4181831 ZINC | 0.500 | 232.2 Da LogP -0.01 TPSA 129.0 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)C(CC(=O)O)CC(=O)O
|
| ZINC4822898 ZINC | 0.500 | 272.3 Da LogP 3.02 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCC(=O)CCCCCC(=O)O
|
| ZINC4822900 ZINC | 0.500 | 300.4 Da LogP 3.80 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O
|
| ZINC71257127 ZINC | 0.500 | 426.5 Da LogP 0.05 TPSA 139.2 | ✓ Ro5 | ✓ Clean |
O=C(O)CCOCCOCCOCCOCCOCCOCCOCCC(=O)O
|
| ZINC71257128 ZINC | 0.500 | 338.4 Da LogP 0.02 TPSA 120.8 | ✓ Ro5 | ✓ Clean |
O=C(O)CCOCCOCCOCCOCCOCCC(=O)O
|
| ZINC79016464 ZINC | 0.500 | 382.4 Da LogP 0.04 TPSA 130.0 | ✓ Ro5 | ✓ Clean |
O=C(O)CCOCCOCCOCCOCCOCCOCCC(=O)O
|
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.
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.