Protein target profile

KP13_04217

Thioredoxin reductase

Genome: KpKP13 Gene: AHE45448.1 trxB 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GQX9

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Length 331

Pocket druggability 0.892

Direct ligand evidence 0 71 total records

Functional annotation 1 EC 7 GO

Target summary

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

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.89, P2Rank 0.85). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.89. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.85. Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

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 (%): 24.747 Lower values reduce human off-target concern.
Human E-value: 6.64e-06
Gut microbiome similarity: 12.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 84.953 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 93.0 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The 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.

FPocket 0.892

Structure A0A0H3GQX9

Pocket Pocket 2

P2Rank 0.85

Structure A0A0H3GQX9

Pocket Pocket 1

ColabFold model

FPocket 0.939 · Pocket 1

P2Rank 0.865 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 607 / 4744 genomes with a hit

Prevalence 12.8%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GQX9

Chemistry

ChEMBL CHEMBL2035464 ChEMBL CHEMBL2035461 ChEMBL CHEMBL2035460 ChEMBL CHEMBL3655713 ChEMBL CHEMBL3655720 ChEMBL CHEMBL51085 ChEMBL CHEMBL3926452 ChEMBL CHEMBL5395264 ChEMBL CHEMBL3655712 ChEMBL CHEMBL3913125 ChEMBL CHEMBL3968421 ChEMBL CHEMBL5397149 ChEMBL CHEMBL5416840 ChEMBL CHEMBL5440854 ChEMBL CHEMBL3976958 ChEMBL CHEMBL3655716

Sequence

Primary amino-acid sequence viewer.

MYANYYGDLMGTAKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHAAKFETEIIFDHISRVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDSFRAEKILIKRLMDKVASGNIVLHTDRTLEEVTGDQMGVSGLRLRDTKNSDNVESLEVAGLFVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADACK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1.8.1.9

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0019430 Any process, acting at the cellular level, involved in removing superoxide radicals (O2-) from a cell or organism, e.g. by conversion to dioxygen (O2) and hydrogen peroxide (H2O2).
GO:0004791 Catalysis of the reaction: thioredoxin-dithiol + NADP+ = thioredoxin-disulfide + H+ + NADPH.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0032991 A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
145	165	ProSitePatterns	PS00573	Pyridine nucleotide-disulphide oxidoreductases class-II active site.
145	165	InterPro	IPR008255	Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
248	269	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
71	81	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
138	150	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
116	124	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
153	177	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
286	304	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
50	65	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
208	224	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
17	39	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
11	324	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
11	324	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
157	175	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
18	37	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
115	133	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
276	298	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
246	262	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
14	324	PANTHER	PTHR48105	THIOREDOXIN REDUCTASE 1-RELATED-RELATED
127	254	Gene3D	G3DSA:3.50.50.60	-
127	254	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
18	323	Gene3D	G3DSA:3.50.50.60	-
18	323	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
127	254	FunFam	G3DSA:3.50.50.60:FF:000007	Alkyl hydroperoxide reductase, F subunit
17	309	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
17	309	InterPro	IPR023753	FAD/NAD(P)-binding domain
17	323	NCBIfam	TIGR01292	thioredoxin-disulfide reductase
17	323	InterPro	IPR005982	Thioredoxin reductase

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.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #2

0.892

Likely same site as P2Rank 2 2.4 Å 19 shared residues 79% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #3

0.359

Likely same site as P2Rank 4 1.4 Å 9 shared residues 90% of smaller site

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Surrounding area

Site 3 FPocket #18

0.357

Likely same site as P2Rank 3 4.9 Å 12 shared residues 80% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.85

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Surrounding area

Site 2 P2Rank #2

0.584

Likely same site as FPocket 2 2.4 Å 19 shared residues 79% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.496

Likely same site as FPocket 18 4.9 Å 12 shared residues 80% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.124

Likely same site as FPocket 3 1.4 Å 9 shared residues 90% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.084

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.865

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Surrounding area

Site 2 P2Rank #2

0.651

Likely same site as FPocket 1 2.6 Å 20 shared residues 80% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.437

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Surrounding area

Site 4 P2Rank #4

0.223

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Surrounding area

Site 5 P2Rank #5

0.06

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental 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_A0A0H3GQX9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04217	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.

71 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 21 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 16 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3AA PDB via homolog 716.4 Da · LogP -2.42 · TPSA 347.7 Open detail RCSB PDB

FDA PDB via homolog Detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

MLT PDB via homolog Detail RCSB PDB

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
3AA RCSB PDB	1F6M	P0A9P4	716.4 Da LogP -2.42 TPSA 347.7	3 viol.	✓ Clean	`c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P…`
FDA RCSB PDB	4JNQ	Q8YID2	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
FLC RCSB PDB	2WHD	A9LN30	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
MLI RCSB PDB	6BPY	A0A229Y1X4	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MLT RCSB PDB	6BPY	A0A229Y1X4	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL2035464 ChEMBL	P0A9P4	8.00 ~10.0 nM	478.3 Da LogP 2.69 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCCCCCn1[se]c2ccccc2c1=O`
CHEMBL2035461 ChEMBL	P0A9P4	7.40 ~39.8 nM	436.2 Da LogP 1.52 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCCn1[se]c2ccccc2c1=O`
CHEMBL2035460 ChEMBL	P0A9P4	7.30 ~50.1 nM	422.2 Da LogP 1.13 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCn1[se]c2ccccc2c1=O`
CHEMBL3655713 ChEMBL	P0A9P4	6.60 ~251.2 nM	322.7 Da LogP 3.01 TPSA 22.0	✓ Ro5	✓ Clean	`Cc1cc(Cl)ccc1-n1[se]c2ccccc2c1=O`
CHEMBL3655720 ChEMBL	P0A9P4	6.60 ~251.2 nM	320.2 Da LogP 1.35 TPSA 78.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ncccc1[N+](=O)[O-]`
CHEMBL51085 ChEMBL	P0A9P4	6.52 ~302.0 nM	274.2 Da LogP 2.05 TPSA 22.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ccccc1`
CHEMBL3926452 ChEMBL	C4LW95	6.41 ~389.0 nM	361.4 Da LogP 4.48 TPSA 58.7	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccccn2)S/C(=N\c2ccccc2)N1Cc1ccco1`
CHEMBL5395264 ChEMBL	P0A9P4	6.30 ~501.2 nM	476.3 Da LogP 3.86 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1nn(CC[Se][Se]CCn2nc(C)c3ccccc32)c2ccccc12`
CHEMBL3655712 ChEMBL	P0A9P4	6.26 ~549.5 nM	308.6 Da LogP 2.70 TPSA 22.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ccc(Cl)cc1`
CHEMBL3913125 ChEMBL	C4LW95	6.17 ~676.1 nM	420.5 Da LogP 5.10 TPSA 64.3	1 viol.	✓ Clean	`COc1ccc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C2=O)c…`
CHEMBL3968421 ChEMBL	C4LW95	6.16 ~691.8 nM	420.5 Da LogP 5.10 TPSA 64.3	1 viol.	✓ Clean	`COc1ccc(OC)c(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C…`
CHEMBL5397149 ChEMBL	P0A9P4	6.16 ~691.8 nM	538.3 Da LogP 3.06 TPSA 121.9	1 viol.	✓ Clean	`O=[N+]([O-])c1ccc2c(cnn2CC[Se][Se]CCn2ncc3cc([N…`
CHEMBL5416840 ChEMBL	P0A9P4	6.16 ~691.8 nM	473.2 Da LogP 3.48 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1nn(CC[Se][Se]CCn2nc(C)c(Cl)c2C)c(C)c1Cl`
CHEMBL5440854 ChEMBL	P0A9P4	6.16 ~691.8 nM	506.3 Da LogP 1.74 TPSA 74.8	1 viol.	✓ Clean	`O=C1c2ccccc2C(=O)N1CC[Se][Se]CCN1C(=O)c2ccccc2C…`
CHEMBL3976958 ChEMBL	C4LW95	6.14 ~724.4 nM	376.4 Da LogP 4.79 TPSA 66.0	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccc(O)cc2)S/C(=N\c2ccccc2)N1Cc1ccco1`
CHEMBL3655716 ChEMBL	P0A9P4	6.00 ~1.0 µM	198.1 Da LogP 0.59 TPSA 32.9	✓ Ro5	✓ Clean	`O=c1[nH][se]c2ccccc12`

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
ZINC18246980 ZINC	1.000	376.4 Da LogP 4.79 TPSA 66.0	✓ Ro5	✓ Clean	`O=C1/C(=C\c2ccc(O)cc2)S/C(=N/c2ccccc2)N1Cc1ccco1`
ZINC2293355652 ZINC	1.000	376.4 Da LogP 4.79 TPSA 66.0	✓ Ro5	✓ Clean	`O=C1C(=Cc2ccc(O)cc2)SC(=Nc2ccccc2)N1Cc1ccco1`
ZINC238950253 ZINC	0.859	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950256 ZINC	0.859	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950259 ZINC	0.859	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950261 ZINC	0.859	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC15013521 ZINC	0.852	406.5 Da LogP 4.80 TPSA 75.3	✓ Ro5	✓ Clean	`COc1cc(/C=C2/S/C(=N/c3ccccc3)N(Cc3ccco3)C2=O)cc…`
ZINC9261465 ZINC	0.818	478.5 Da LogP 4.64 TPSA 90.6	✓ Ro5	✓ Clean	`COC(=O)COc1ccc(/C=C2/S/C(=N\c3ccccc3)N(Cc3ccco3…`
ZINC4660313 ZINC	0.780	368.5 Da LogP 4.33 TPSA 51.1	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccccc1`
ZINC100314562 ZINC	0.769	434.5 Da LogP 4.82 TPSA 73.5	✓ Ro5	✓ Clean	`COc1cc2c(cc1/C=C1/S/C(=N\c3ccccc3)N(Cc3ccco3)C1…`
ZINC17719664 ZINC	0.769	434.5 Da LogP 4.82 TPSA 73.5	✓ Ro5	✓ Clean	`COc1cc2c(cc1/C=C1/S/C(=N/c3ccccc3)N(Cc3ccco3)C1…`
ZINC245309458 ZINC	0.769	434.5 Da LogP 4.82 TPSA 73.5	✓ Ro5	✓ Clean	`COc1cc2c(cc1/C=C1/SC(=Nc3ccccc3)N(Cc3ccco3)C1=O…`
ZINC13546520 ZINC	0.759	405.4 Da LogP 4.99 TPSA 88.9	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccc([N+](=O)[O-])cc2)S/C(=N\c2ccccc…`
ZINC4664355 ZINC	0.759	368.5 Da LogP 4.33 TPSA 51.1	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2ccc(OC)c(OC)c2)S/C1=N/c1ccccc1`
ZINC13880821 ZINC	0.750	418.5 Da LogP 4.87 TPSA 72.1	✓ Ro5	✓ Clean	`COC(=O)c1ccc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C…`
ZINC49582222 ZINC	0.750	207.2 Da LogP 0.94 TPSA 81.2	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc2c(cnn2CCO)c1`
ZINC4526109 ZINC	0.741	350.4 Da LogP 4.68 TPSA 59.0	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccco2)S/C(=N\c2ccccc2)N1Cc1ccco1`
ZINC1014076 ZINC	0.738	382.5 Da LogP 4.72 TPSA 51.1	✓ Ro5	✓ Clean	`CCCN1C(=O)/C(=C/c2cc(OC)ccc2OC)S/C1=N\c1ccccc1`
ZINC4664262 ZINC	0.738	382.5 Da LogP 4.72 TPSA 51.1	✓ Ro5	✓ Clean	`CCCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N/c1ccccc1`
ZINC18246975 ZINC	0.733	445.5 Da LogP 4.92 TPSA 58.3	✓ Ro5	Alert	`O=C1/C(=C\c2ccc(N3CCOCC3)cc2)S/C(=N/c2ccccc2)N1…`
ZINC8816280 ZINC	0.729	477.5 Da LogP 4.35 TPSA 107.4	✓ Ro5	✓ Clean	`CCOc1cc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C2=O)c…`
ZINC2777124 ZINC	0.714	398.5 Da LogP 3.95 TPSA 60.4	✓ Ro5	✓ Clean	`COCCN1C(=O)/C(=C/c2cc(OC)ccc2OC)S/C1=N\c1ccccc1`
ZINC5660821 ZINC	0.714	398.5 Da LogP 3.95 TPSA 60.4	✓ Ro5	✓ Clean	`COCCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccccc1`
ZINC1184606 ZINC	0.710	361.4 Da LogP 3.70 TPSA 51.9	✓ Ro5	Alert	`COc1ccc(OC)c(/C=C2/SC(=S)N(Cc3ccco3)C2=O)c1`
ZINC13534752 ZINC	0.710	361.4 Da LogP 3.70 TPSA 51.9	✓ Ro5	Alert	`COc1ccc(OC)c(/C=C2\SC(=S)N(Cc3ccco3)C2=O)c1`
ZINC175473 ZINC	0.708	320.3 Da LogP 1.58 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1c2ccccc2C(=O)N1CCN1C(=O)c2ccccc2C1=O`
ZINC13739257 ZINC	0.705	361.4 Da LogP 3.70 TPSA 51.9	✓ Ro5	Alert	`COc1ccc(/C=C2\SC(=S)N(Cc3ccco3)C2=O)cc1OC`
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`
ZINC1065235 ZINC	0.696	302.4 Da LogP 3.08 TPSA 46.3	✓ Ro5	Alert	`O=C1/C(=C\c2ccccn2)SC(=S)N1Cc1ccco1`
ZINC1065238 ZINC	0.696	302.4 Da LogP 3.08 TPSA 46.3	✓ Ro5	Alert	`O=C1/C(=C/c2ccccn2)SC(=S)N1Cc1ccco1`
ZINC2141838 ZINC	0.694	398.5 Da LogP 3.95 TPSA 60.4	✓ Ro5	✓ Clean	`COCCN1C(=O)/C(=C/c2ccc(OC)c(OC)c2)S/C1=N\c1cccc…`
ZINC5879640 ZINC	0.694	398.5 Da LogP 3.95 TPSA 60.4	✓ Ro5	✓ Clean	`COCCN1C(=O)/C(=C\c2ccc(OC)c(OC)c2)S/C1=N\c1cccc…`
ZINC1187854 ZINC	0.673	317.4 Da LogP 3.39 TPSA 53.7	✓ Ro5	Alert	`O=C1/C(=C/c2ccc(O)cc2)SC(=S)N1Cc1ccco1`
ZINC12436467 ZINC	0.673	317.4 Da LogP 3.39 TPSA 53.7	✓ Ro5	Alert	`O=C1/C(=C\c2ccc(O)cc2)SC(=S)N1Cc1ccco1`
ZINC4660314 ZINC	0.672	354.4 Da LogP 3.94 TPSA 51.1	✓ Ro5	✓ Clean	`COc1ccc(OC)c(/C=C2/S/C(=N\c3ccccc3)N(C)C2=O)c1`
ZINC96592063 ZINC	0.672	354.4 Da LogP 3.94 TPSA 51.1	✓ Ro5	✓ Clean	`COc1ccc(OC)c(/C=C2/S/C(=N/c3ccccc3)N(C)C2=O)c1`
ZINC3871401 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871402 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3871403 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871404 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC4096223 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC4491584 ZINC	0.667	383.5 Da LogP 3.78 TPSA 54.4	✓ Ro5	✓ Clean	`COc1ccc(OC)c(/C=C2/S/C(=N\c3ccccc3)N(N(C)C)C2=O…`
ZINC4664352 ZINC	0.667	368.5 Da LogP 4.33 TPSA 51.1	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2ccc(OC)cc2OC)S/C1=N/c1ccccc1`
ZINC71773889 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`
ZINC71773890 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`
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`
ZINC101695107 ZINC	0.662	412.5 Da LogP 4.34 TPSA 60.4	✓ Ro5	✓ Clean	`CCOCCN1C(=O)/C(=C/c2ccc(OC)c(OC)c2)S/C1=N/c1ccc…`
ZINC4466315 ZINC	0.661	336.4 Da LogP 4.18 TPSA 52.9	✓ Ro5	✓ Clean	`C=CCN1C(=O)/C(=C\c2ccc(O)cc2)S/C1=N/c1ccccc1`
ZINC4672070 ZINC	0.656	382.5 Da LogP 4.64 TPSA 51.1	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccc(C)cc1`

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.