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
- Hit
- Human identity (%)
- 25.092 Lower values reduce human off-target concern.
- Human E-value
- 2.82e-20
- Gut microbiome similarity
- 3.0% 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
- 93.57 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.
MISAWSNKMAIAIGLDFGSDSVRALAVECASGAELATSVEWYPRWREGQYCDGANNRFRHHPRDYIESMEAALKSVLASLSAEQRADVVGIGVDSTGSTPAPVDAEGNVLALREEFADNPNAMFVLWKDHTAVEEAEAITRLCHQPGKEDYSRYIGGIYSSEWFWAKILHVTREDSAVAQAAASWVELCDWVPALLSGTTRPQDLRRGRCSAGHKSLWHESWGGLPPASFFDELDPIINQHLAWPLFTDTWTADVPVGTLSAEWAQRLGLSQTVAISGGAFDCHMGAVGAGAQPNALVKVIGTSTCDILIADKESVGERTVKGICGQVDGSVVPHFIGMEAGQSAFGDIYAWFGRILGWPLEQLAQQQPALREQIKASQKQLLPALTEAWANNPSLEHLPVVLDWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLIAATAFGARAIMECFTEQGIPVNNVMALGGIARKNQVIMQACCDVLNRPLQIVASDQCCALGAAIFAAVAAGVYEDIPAAQQRMASQVETTLQPRPAQAQRFEQLYQRYQQWSVSAEQHYLPSAAKAEKAPQSQAALTH
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Subcellular localization
- Localization
- Cytoplasmic
Enzyme Commission (EC)
1Gene Ontology (GO)
7- GO:0019569 The chemical reactions and pathways resulting in the breakdown of L-arabinose into D-xylulose 5-phosphate.
- GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
- GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
- GO:0008741 Catalysis of the reaction: ATP + L(or D)-ribulose = ADP + L(or D)-ribulose 5-phosphate.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0019150 Catalysis of the reaction: ATP + D-ribulose = ADP + D-ribulose 5-phosphate.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 344 | 544 | Gene3D | G3DSA:1.20.58.2240 | - |
| 11 | 555 | PANTHER | PTHR43435 | RIBULOKINASE |
| 293 | 550 | SUPERFAMILY | SSF53067 | Actin-like ATPase domain |
| 293 | 550 | InterPro | IPR043129 | ATPase, nucleotide binding domain |
| 299 | 509 | Pfam | PF02782 | FGGY family of carbohydrate kinases, C-terminal domain |
| 299 | 509 | InterPro | IPR018485 | Carbohydrate kinase, FGGY, C-terminal |
| 13 | 292 | SUPERFAMILY | SSF53067 | Actin-like ATPase domain |
| 13 | 292 | InterPro | IPR043129 | ATPase, nucleotide binding domain |
| 361 | 381 | Coils | Coil | Coil |
| 10 | 558 | NCBIfam | TIGR01234 | ribulokinase |
| 10 | 558 | InterPro | IPR005929 | Ribulokinase |
| 9 | 566 | Hamap | MF_00520 | Ribulokinase [araB]. |
| 9 | 566 | InterPro | IPR005929 | Ribulokinase |
| 10 | 522 | CDD | cd07781 | FGGY_RBK |
| 10 | 522 | InterPro | IPR005929 | Ribulokinase |
| 13 | 534 | Gene3D | G3DSA:3.30.420.40 | - |
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
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_A0A0H3GJ58
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01942
|
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 |
|---|---|---|---|---|---|---|
| BTB RCSB PDB | Q665C6 | 209.2 Da LogP -3.01 TPSA 104.4 | ✓ Ro5 | ✓ Clean |
C(CO)N(CCO)C(CO)(CO)CO
|
|
| QDK RCSB PDB | Q9KBQ3 | 150.1 Da LogP -2.74 TPSA 98.0 | ✓ Ro5 | ✓ Clean |
C([C@@H]([C@@H](C(=O)CO)O)O)O
|
|
| XUL RCSB PDB | Q665C6 | 150.1 Da LogP -2.74 TPSA 98.0 | ✓ Ro5 | ✓ Clean |
C([C@H]([C@@H](C(=O)CO)O)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 |
|---|---|---|---|---|---|
| ZINC1615342 ZINC | 1.000 | 209.2 Da LogP -3.01 TPSA 104.4 | ✓ Ro5 | ✓ Clean |
OCCN(CCO)C(CO)(CO)CO
|
| ZINC100036265 ZINC | 0.682 | 210.2 Da LogP -4.02 TPSA 138.5 | 1 viol. | ✓ Clean |
O=C(CO)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO
|
| ZINC100071552 ZINC | 0.682 | 210.2 Da LogP -4.02 TPSA 138.5 | 1 viol. | ✓ Clean |
O=C(CO)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CO
|
| ZINC113074329 ZINC | 0.682 | 210.2 Da LogP -4.02 TPSA 138.5 | 1 viol. | ✓ Clean |
O=C(CO)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO
|
| ZINC13522679 ZINC | 0.682 | 210.2 Da LogP -4.02 TPSA 138.5 | 1 viol. | ✓ Clean |
O=C(CO)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)CO
|
| ZINC4353160 ZINC | 0.682 | 210.2 Da LogP -4.02 TPSA 138.5 | 1 viol. | ✓ Clean |
O=C(CO)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)CO
|
| ZINC8579422 ZINC | 0.682 | 210.2 Da LogP -4.02 TPSA 138.5 | 1 viol. | ✓ Clean |
O=C(CO)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO
|
| ZINC2334905 ZINC | 0.522 | 261.4 Da LogP 1.10 TPSA 63.9 | ✓ Ro5 | ✓ Clean |
CC(C)CCN(CCC(C)C)C(CO)(CO)CO
|
| ZINC3159953 ZINC | 0.522 | 261.4 Da LogP 1.38 TPSA 63.9 | ✓ Ro5 | ✓ Clean |
CCCCCN(CCCCC)C(CO)(CO)CO
|
| ZINC113364020 ZINC | 0.500 | 330.5 Da LogP 3.75 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCCC(=O)[C@@H](O)[C@@H](O)CO
|
| ZINC113364022 ZINC | 0.500 | 330.5 Da LogP 3.75 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCCC(=O)[C@H](O)[C@@H](O)CO
|
| ZINC113364024 ZINC | 0.500 | 330.5 Da LogP 3.75 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCCC(=O)[C@@H](O)[C@H](O)CO
|
| ZINC113364025 ZINC | 0.500 | 330.5 Da LogP 3.75 TPSA 77.8 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCCC(=O)[C@H](O)[C@H](O)CO
|
| ZINC1529626 ZINC | 0.500 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(CO)[C@H](O)[C@@H](O)COP(=O)(O)O
|
| ZINC1532567 ZINC | 0.500 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(CO)[C@H](O)[C@H](O)COP(=O)(O)O
|
| ZINC1532851 ZINC | 0.500 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(CO)[C@@H](O)[C@@H](O)COP(=O)(O)O
|
| ZINC30320708 ZINC | 0.500 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(CO)[C@@H](O)[C@H](O)COP(=O)(O)O
|
| ZINC31259596 ZINC | 0.500 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)CO
|
| ZINC31259600 ZINC | 0.500 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)CO
|
| ZINC3869804 ZINC | 0.500 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)CO
|
| ZINC3869805 ZINC | 0.500 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(COP(=O)(O)O)[C@H](O)[C@H](O)CO
|
| ZINC5297554 ZINC | 0.500 | 289.5 Da LogP 2.16 TPSA 63.9 | ✓ Ro5 | ✓ Clean |
CCCCCCN(CCCCCC)C(CO)(CO)CO
|
| ZINC97941822 ZINC | 0.500 | 317.5 Da LogP 2.94 TPSA 63.9 | ✓ Ro5 | ✓ Clean |
CCCCCCCN(CCCCCCC)C(CO)(CO)CO
|
| ZINC97942927 ZINC | 0.500 | 373.6 Da LogP 4.51 TPSA 63.9 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCN(CCCCCCCCC)C(CO)(CO)CO
|
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.