Protein profile

KP13_04217

Thioredoxin reductase

Genome: KpKP13

Gene: trxB AHE45448.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQX9

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Amino acids 331

Annotations 8

Features 28

PDB binders 5

Druggability 0.892

Overview

Basic information about this protein and its source genome.

Accession: KP13_04217
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: trxB AHE45448.1
Status: annotated
Amino acids: 331
Structure source: AlphaFold + ColabFold

1.8.1.9

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 24.747
Human E-value: 6.64e-06
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 84.953
DEG E-value: 0.0
Localization: Unknown
ColabFold pLDDT: 93.0

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its 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

Normalized 0.128

Sequence

Primary amino-acid sequence viewer.

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 Features

Domain/signature hits 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; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GQX9	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_04217	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
2				0.892
3				0.359
18				0.357

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	11.85	0.628
2	5.93	0.291
3	5.27	0.247
4	2.41	0.064

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.939

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	11.69	0.621
2	6.21	0.31
3	5.25	0.246
4	3.81	0.148
5	1.55	0.023

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	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	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	6BPY	A0A229Y1X4	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MLT	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	P0A9P4	8.00	478.3 Da LogP 2.69 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCCCCCn1[se]c2ccccc2c1=O`
CHEMBL2035461	P0A9P4	7.40	436.2 Da LogP 1.52 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCCn1[se]c2ccccc2c1=O`
CHEMBL2035460	P0A9P4	7.30	422.2 Da LogP 1.13 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCn1[se]c2ccccc2c1=O`
CHEMBL3655713	P0A9P4	6.60	322.7 Da LogP 3.01 TPSA 22.0	✓ Ro5	✓ Clean	`Cc1cc(Cl)ccc1-n1[se]c2ccccc2c1=O`
CHEMBL3655720	P0A9P4	6.60	320.2 Da LogP 1.35 TPSA 78.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ncccc1[N+](=O)[O-]`
CHEMBL51085	P0A9P4	6.52	274.2 Da LogP 2.05 TPSA 22.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ccccc1`
CHEMBL3926452	C4LW95	6.41	361.4 Da LogP 4.48 TPSA 58.7	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccccn2)S/C(=N\c2ccccc2)N1Cc1ccco1`
CHEMBL5395264	P0A9P4	6.30	476.3 Da LogP 3.86 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1nn(CC[Se][Se]CCn2nc(C)c3ccccc32)c2ccccc12`
CHEMBL3655712	P0A9P4	6.26	308.6 Da LogP 2.70 TPSA 22.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ccc(Cl)cc1`
CHEMBL3913125	C4LW95	6.17	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	C4LW95	6.16	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	P0A9P4	6.16	538.3 Da LogP 3.06 TPSA 121.9	1 viol.	✓ Clean	`O=[N+]([O-])c1ccc2c(cnn2CC[Se][Se]CCn2ncc3cc([N…`
CHEMBL5416840	P0A9P4	6.16	473.2 Da LogP 3.48 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1nn(CC[Se][Se]CCn2nc(C)c(Cl)c2C)c(C)c1Cl`
CHEMBL5440854	P0A9P4	6.16	506.3 Da LogP 1.74 TPSA 74.8	1 viol.	✓ Clean	`O=C1c2ccccc2C(=O)N1CC[Se][Se]CCN1C(=O)c2ccccc2C…`
CHEMBL3976958	C4LW95	6.14	376.4 Da LogP 4.79 TPSA 66.0	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccc(O)cc2)S/C(=N\c2ccccc2)N1Cc1ccco1`
CHEMBL3655716	P0A9P4	6.00	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	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	1.000	376.4 Da LogP 4.79 TPSA 66.0	✓ Ro5	✓ Clean	`O=C1C(=Cc2ccc(O)cc2)SC(=Nc2ccccc2)N1Cc1ccco1`
ZINC238950253	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	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	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	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	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	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	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	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	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	0.769	434.5 Da LogP 4.82 TPSA 73.5	✓ Ro5	✓ Clean	`COc1cc2c(cc1/C=C1/SC(=Nc3ccccc3)N(Cc3ccco3)C1=O…`
ZINC13546520	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	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	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	0.750	207.2 Da LogP 0.94 TPSA 81.2	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc2c(cnn2CCO)c1`
ZINC4526109	0.741	350.4 Da LogP 4.68 TPSA 59.0	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccco2)S/C(=N\c2ccccc2)N1Cc1ccco1`
ZINC1014076	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	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	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	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	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	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	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	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	0.708	320.3 Da LogP 1.58 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1c2ccccc2C(=O)N1CCN1C(=O)c2ccccc2C1=O`
ZINC13739257	0.705	361.4 Da LogP 3.70 TPSA 51.9	✓ Ro5	Alert	`COc1ccc(/C=C2\SC(=S)N(Cc3ccco3)C2=O)cc1OC`
ZINC1532902	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	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	0.696	302.4 Da LogP 3.08 TPSA 46.3	✓ Ro5	Alert	`O=C1/C(=C\c2ccccn2)SC(=S)N1Cc1ccco1`
ZINC1065238	0.696	302.4 Da LogP 3.08 TPSA 46.3	✓ Ro5	Alert	`O=C1/C(=C/c2ccccn2)SC(=S)N1Cc1ccco1`
ZINC2141838	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	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	0.673	317.4 Da LogP 3.39 TPSA 53.7	✓ Ro5	Alert	`O=C1/C(=C/c2ccc(O)cc2)SC(=S)N1Cc1ccco1`
ZINC12436467	0.673	317.4 Da LogP 3.39 TPSA 53.7	✓ Ro5	Alert	`O=C1/C(=C\c2ccc(O)cc2)SC(=S)N1Cc1ccco1`
ZINC4660314	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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.