KpATCC43816 Protein target profile

thioredoxin-disulfide reductase

Accession: VK055_1566

Gene: AIK80186.1 trxB 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GQX9

Export view

Length 322

Pocket druggability (P2Rank · AlphaFold DB model) 0.85

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 71 total records

Functional annotation 1 EC 7 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Central metabolic position More central than 98.9% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: 12.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 84.639 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.79 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank'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.

Druggability (P2Rank) 0.85

Structure A0A0H3GQX9

Pocket Pocket 1

Druggability (FPocket) 0.892

Structure A0A0H3GQX9

Pocket Pocket 2

ColabFold model

P2Rank 0.885 · Pocket 1

FPocket 0.578 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 590 / 4744 genomes with a hit

Prevalence 12.4%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: more central than 98.9% of genes in this genome, no human homolog detected.

Relative network centrality 98.9% more central than 98.9% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MGTAKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHAAKFETEIIFDHISRVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDSFRAEKILIKRLMDKVASGNIVLHTDRTLEEVTGDQMGVSGLRLRDTKNSDNVESLEVAGLFVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSISGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADACK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Unknown

Enzyme Commission (EC)

1.8.1.9

Gene Ontology (GO)

GO:0004791 Catalysis of the reaction: thioredoxin-dithiol + NADP+ = thioredoxin-disulfide + H+ + NADPH.
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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.

33 records

Show feature table

Start	End	DB	Term	Name
5	315	PANTHER	PTHR48105	THIOREDOXIN REDUCTASE 1-RELATED-RELATED
8	300	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
8	300	InterPro	IPR023753	FAD/NAD(P)-binding domain
1	25	Phobius	SIGNAL_PEPTIDE	Signal peptide region
106	124	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
9	28	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
267	289	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
237	253	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
148	166	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
26	322	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
8	314	NCBIfam	TIGR01292	thioredoxin-disulfide reductase
8	314	InterPro	IPR005982	Thioredoxin reductase
136	156	ProSitePatterns	PS00573	Pyridine nucleotide-disulphide oxidoreductases class-II active site.
136	156	InterPro	IPR008255	Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
3	315	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
3	315	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
8	30	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
129	141	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
62	72	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
277	295	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
239	260	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
107	115	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
41	56	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
199	215	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
144	168	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
118	245	Gene3D	G3DSA:3.50.50.60	-
118	245	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
118	245	FunFam	G3DSA:3.50.50.60:FF:000007	Alkyl hydroperoxide reductase, F subunit
9	17	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
9	314	Gene3D	G3DSA:3.50.50.60	-
9	314	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	8	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
18	25	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.85

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.584

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

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.496

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

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.124

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

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.084

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #2

0.892 Unusual size

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

Show in viewer

Surrounding area

Pocket 2 FPocket #3

0.359

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

Show in viewer

Surrounding area

Pocket 3 FPocket #18

0.357

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

Show in viewer

Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.885

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.843

Likely same site as FPocket 1 7.7 Å 22 shared residues 58% of smaller site

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.136

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.058

Show in viewer

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 VK055_1566	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.

Cross-references

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

thioredoxin-disulfide reductase

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways