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 (%)
- 61.391 Lower values reduce human off-target concern.
- Human E-value
- 6.2e-178
- Gut microbiome similarity
- 19.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 61.739 Higher values support similarity to known essential genes.
- DEG E-value
- 0.0 Smaller values mean stronger essential-gene similarity.
Localization
- Localization
- Cytoplasmic
Structure confidence
- ColabFold pLDDT
- 97.32 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelThe selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.
Sequence
Sequence
Primary amino-acid sequence viewer.
MTTHRSEKDSMGAIEVPADKLWGAQTQRSLEHFRISTEKMPGELIYALALTKRAAAKVNQDLGLLTAEKAGAIVAAADEVLAGKHAQEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGERGMARKIHPNDDVNKSQSSNDVFPTAMHVAALIALREKVIPSLQALRATLNEKAVAFRDIVKIGRTHLQDATPLTLGQEISGWVAMLDHSLKHIEASQPHLAELALGGTAVGTGLNTHPEYAVRVAAELASLSGQPFVTAPNKFEALATVDALVHAHGALKGLAASLMKIANDVRWLASGPRCGIGEIAIPENEPGSSIMPGKVNPTQCEALTMVCCQVMGNDVAVNIGGASGNFELNVYRPMVIHNFLQSVRLLADGMASFNEHCAVGIEPNRERISQLLNESLMLVTALNTHIGYDKAAEIAKKAHHEGLTLKASALALGYLTEAEFDSWVRPEEMVGSLAIR
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
9- GO:0006106 The chemical reactions and pathways involving fumarate, the anion of trans-1,2-ethenedicarboxylic acid, the diastereoisomer of maleate. It is a key intermediate in metabolism and is formed in the TCA cycle from succinate and converted into malate.
- GO:0004333 Catalysis of the reaction: (S)-malate = fumarate + H2O.
- GO:0045239 Any of the heteromeric enzymes that act in the TCA cycle.
- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
- GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0042802 Binding to an identical protein or proteins.
- GO:0006108 The chemical reactions and pathways involving malate, the anion of hydroxybutanedioic acid, a chiral hydroxydicarboxylic acid. The (+) enantiomer is an important intermediate in metabolism as a component of both the TCA cycle and the glyoxylate cycle.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 3 | 461 | PANTHER | PTHR11444 | ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE |
| 3 | 461 | InterPro | IPR005677 | Fumarate hydratase, class II |
| 12 | 342 | Pfam | PF00206 | Lyase |
| 12 | 342 | InterPro | IPR022761 | Fumarate lyase, N-terminal |
| 5 | 459 | SUPERFAMILY | SSF48557 | L-aspartase-like |
| 5 | 459 | InterPro | IPR008948 | L-Aspartase-like |
| 317 | 326 | ProSitePatterns | PS00163 | Fumarate lyases signature. |
| 317 | 326 | InterPro | IPR020557 | Fumarate lyase, conserved site |
| 408 | 464 | Gene3D | G3DSA:1.10.40.30 | - |
| 5 | 459 | CDD | cd01362 | Fumarase_classII |
| 5 | 459 | InterPro | IPR005677 | Fumarate hydratase, class II |
| 139 | 407 | Gene3D | G3DSA:1.20.200.10 | Fumarase/aspartase (Central domain) |
| 5 | 138 | Gene3D | G3DSA:1.10.275.10 | - |
| 5 | 138 | InterPro | IPR024083 | Fumarase/histidase, N-terminal |
| 4 | 462 | Hamap | MF_00743 | Fumarate hydratase class II [fumC]. |
| 4 | 462 | InterPro | IPR005677 | Fumarate hydratase, class II |
| 407 | 464 | FunFam | G3DSA:1.10.40.30:FF:000002 | Fumarate hydratase class II |
| 4 | 461 | NCBIfam | TIGR00979 | class II fumarate hydratase |
| 4 | 461 | InterPro | IPR005677 | Fumarate hydratase, class II |
| 139 | 406 | FunFam | G3DSA:1.20.200.10:FF:000001 | Fumarate hydratase, mitochondrial |
| 408 | 460 | Pfam | PF10415 | Fumarase C C-terminus |
| 408 | 460 | InterPro | IPR018951 | Fumarase C, C-terminal |
| 134 | 152 | PRINTS | PR00149 | Fumarate lyase superfamily signature |
| 134 | 152 | InterPro | IPR000362 | Fumarate lyase family |
| 271 | 298 | PRINTS | PR00149 | Fumarate lyase superfamily signature |
| 271 | 298 | InterPro | IPR000362 | Fumarate lyase family |
| 180 | 198 | PRINTS | PR00149 | Fumarate lyase superfamily signature |
| 180 | 198 | InterPro | IPR000362 | Fumarate lyase family |
| 317 | 333 | PRINTS | PR00149 | Fumarate lyase superfamily signature |
| 317 | 333 | InterPro | IPR000362 | Fumarate lyase family |
| 5 | 138 | FunFam | G3DSA:1.10.275.10:FF:000001 | Fumarate hydratase, mitochondrial |
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 · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Residue sets
Binding pockets · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
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_A0A0H3GWS1
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_31914
|
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 |
|---|---|---|---|---|---|---|
| APO RCSB PDB | P07954 | 169.1 Da LogP -1.42 TPSA 120.8 | ✓ Ro5 | ✓ Clean |
C([C@H](C(=O)O)N)P(=O)(O)O
|
|
| FLC RCSB PDB | P05042 | 189.1 Da LogP -5.25 TPSA 140.6 | ✓ Ro5 | ✓ Clean |
C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
|
|
| FUM RCSB PDB | Q65UJ3 | 116.1 Da LogP -0.29 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C(=C/C(=O)O)\C(=O)O
|
|
| LMR RCSB PDB | A0A3Q0KQY7 | 134.1 Da LogP -1.09 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
C([C@@H](C(=O)O)O)C(=O)O
|
|
| MLI RCSB PDB | Q9ZCQ4 | 102.0 Da LogP -3.12 TPSA 80.3 | ✓ Ro5 | ✓ Clean |
C(C(=O)[O-])C(=O)[O-]
|
|
| MLT RCSB PDB | P05042 | 134.1 Da LogP -1.09 TPSA 94.8 | ✓ Ro5 | ✓ Clean |
C([C@H](C(=O)O)O)C(=O)O
|
|
| PMA RCSB PDB | P05042 | 254.1 Da LogP 0.48 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
c1c(c(cc(c1C(=O)O)C(=O)O)C(=O)O)C(=O)O
|
|
| SIF RCSB PDB | P05042 | 190.3 Da LogP 1.25 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C[Si](C)(C)C(CC(=O)O)C(=O)O
|
|
| TLA RCSB PDB | P07954 | 150.1 Da LogP -2.12 TPSA 115.1 | ✓ Ro5 | ✓ Clean |
[C@@H]([C@H](C(=O)O)O)(C(=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 |
|---|---|---|---|---|---|
| ZINC391925 ZINC | 1.000 | 254.1 Da LogP 0.48 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1C(=O)O
|
| ZINC22204540 ZINC | 0.800 | 446.3 Da LogP 1.11 TPSA 240.9 | 1 viol. | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(C(=O)c2cc(C(=O)O)c(C(=O)O)c…
|
| ZINC4289585 ZINC | 0.706 | 226.1 Da LogP 0.49 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1O
|
| ZINC4863098 ZINC | 0.706 | 250.2 Da LogP 1.49 TPSA 108.7 | ✓ Ro5 | ✓ Clean |
CC(=O)c1cc(C(=O)O)c(C(C)=O)cc1C(=O)O
|
| ZINC95938319 ZINC | 0.706 | 252.2 Da LogP 0.85 TPSA 162.8 | 1 viol. | ✓ Clean |
N=C(O)c1cc(C(=N)O)c(C(=O)O)cc1C(=O)O
|
| ZINC1532902 ZINC | 0.700 | 206.2 Da LogP -0.86 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC2018106 ZINC | 0.700 | 206.2 Da LogP -0.86 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CC[C@](O)(CC(=O)O)C(=O)O
|
| ZINC12359024 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O
|
| ZINC13533920 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC1532740 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O
|
| ZINC1549593 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC2013424 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O
|
| ZINC3581021 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC3860635 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC5783661 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O
|
| ZINC6072527 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC225924 ZINC | 0.667 | 330.2 Da LogP 2.15 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(-c2ccc(C(=O)O)c(C(=O)O)c2)cc1C(=O)O
|
| ZINC391804 ZINC | 0.667 | 216.2 Da LogP 2.24 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc2ccccc2cc1C(=O)O
|
| ZINC4553176 ZINC | 0.667 | 289.0 Da LogP 1.54 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1Br
|
| ZINC59202638 ZINC | 0.667 | 244.6 Da LogP 1.43 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1Cl
|
| ZINC71773891 ZINC | 0.667 | 206.1 Da LogP -1.77 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O
|
| ZINC3593496 ZINC | 0.652 | 206.2 Da LogP -1.16 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
COC(=O)C[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC3593497 ZINC | 0.652 | 206.2 Da LogP -1.16 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
COC(=O)C[C@](O)(CC(=O)O)C(=O)O
|
| ZINC20357711 ZINC | 0.647 | 323.9 Da LogP 2.61 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(Br)c(Br)cc1C(=O)O
|
| ZINC346796 ZINC | 0.647 | 202.1 Da LogP 1.36 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(F)c(F)cc1C(=O)O
|
| ZINC4428360 ZINC | 0.647 | 298.2 Da LogP 0.18 TPSA 186.5 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(C(=O)O)c(C(=O)O)c1C(=O)O
|
| ZINC56485 ZINC | 0.647 | 235.0 Da LogP 2.39 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(Cl)c(Cl)cc1C(=O)O
|
| ZINC105301 ZINC | 0.632 | 210.1 Da LogP 0.78 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(C(=O)O)c(C(=O)O)c1
|
| ZINC14686440 ZINC | 0.625 | 436.4 Da LogP -2.64 TPSA 247.9 | 1 viol. | ✓ Clean |
O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…
|
| ZINC14686442 ZINC | 0.625 | 436.4 Da LogP -2.64 TPSA 247.9 | 1 viol. | ✓ Clean |
O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…
|
| ZINC14686444 ZINC | 0.625 | 436.4 Da LogP -2.64 TPSA 247.9 | 1 viol. | ✓ Clean |
O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…
|
| ZINC388195 ZINC | 0.625 | 304.2 Da LogP 1.63 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(C(=O)O)c2c(C(=O)O)ccc(C(=O)O)c12
|
| ZINC25490549 ZINC | 0.611 | 323.9 Da LogP 2.61 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(Br)cc1Br
|
| ZINC642881320 ZINC | 0.611 | 378.3 Da LogP 3.38 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c2ccc3c(C(=O)O)cc(C(=O)O)c4cc…
|
| ZINC75852200 ZINC | 0.611 | 220.1 Da LogP 1.50 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(F)c(F)c1F
|
| ZINC133154 ZINC | 0.600 | 200.6 Da LogP 1.74 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(Cl)cc1C(=O)O
|
| ZINC1571173 ZINC | 0.600 | 245.0 Da LogP 1.85 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(Br)cc1C(=O)O
|
| ZINC1675303 ZINC | 0.600 | 292.0 Da LogP 1.69 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(I)cc1C(=O)O
|
| ZINC1995075 ZINC | 0.600 | 358.3 Da LogP 1.71 TPSA 166.3 | ✓ Ro5 | ✓ Clean |
O=C(c1ccc(C(=O)O)c(C(=O)O)c1)c1ccc(C(=O)O)c(C(=…
|
| ZINC39205416 ZINC | 0.600 | 266.3 Da LogP 3.39 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc2cc3ccccc3cc2cc1C(=O)O
|
| ZINC44069231 ZINC | 0.600 | 314.2 Da LogP 2.01 TPSA 129.0 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(C(=O)c2ccccc2)cc1C(=O)O
|
| ZINC1560405156 ZINC | 0.588 | 208.1 Da LogP -1.79 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC1560405157 ZINC | 0.588 | 208.1 Da LogP -1.79 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC2040496 ZINC | 0.588 | 254.1 Da LogP 0.48 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(C(=O)O)c(C(=O)O)c1C(=O)O
|
| ZINC3120959 ZINC | 0.579 | 255.1 Da LogP -0.13 TPSA 162.1 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(C(=O)O)nc1C(=O)O
|
| ZINC81217827 ZINC | 0.579 | 222.2 Da LogP 2.21 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CCc1cc(C(=O)O)c(C(=O)O)cc1CC
|
| ZINC13398039 ZINC | 0.577 | 234.2 Da LogP -0.38 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O
|
| ZINC2528012 ZINC | 0.577 | 234.2 Da LogP -0.38 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC100725222 ZINC | 0.571 | 358.3 Da LogP 2.89 TPSA 173.9 | ✓ Ro5 | Alert |
O=C(O)c1ccc(/N=N/c2ccc(C(=O)O)c(C(=O)O)c2)cc1C(…
|
| ZINC66325523 ZINC | 0.571 | 290.2 Da LogP 0.03 TPSA 166.3 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cc(C(=O)O)c(S(=O)(=O)O)cc1C(=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.