Protein target profile

KP13_03396

2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase

Genome: KpKP13 Gene: AHE45774.1 entA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GPR7

Export view

Length 251

Pocket druggability 0.876

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 3 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 0.88, P2Rank 0.91). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.88. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. Structure available AlphaFold DB model + ColabFold model 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 (%): 34.058 Lower values reduce human off-target concern.
Human E-value: 1.58e-15
Gut microbiome similarity: 1.8% 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.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.35 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 0.876

Structure A0A0H3GPR7

Pocket Pocket 1

P2Rank 0.914

Structure A0A0H3GPR7

Pocket Pocket 1

ColabFold model

FPocket 0.892 · Pocket 1

P2Rank 0.883 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 84 / 4744 genomes with a hit

Prevalence 1.8%

Cross-references

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

Sequence

UniProt A0A0H3GPR7

Sequence

Primary amino-acid sequence viewer.

MAALDFRGQTVWVTGAGKGIGYATALAFVEAGANVTGFDLAFDGESYPFATETLDVADADQVREACSRLLANTERLDVLVNAAGILRMGATDQLSAEDWQQTFAVNVGGAFNLFQQTMAQFRRQRGGAIVTVASDAAHTPRIGMSAYGASKAALKSLALTVGLELAGSGVRCNLVSPGSTDTDMQRTLWVSDDAEQQRIRGFGEQFKLGIPLGKIARPQEIANTILFLASSHASHITLQDIVVDGGSTLGA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

1.3.1.28

Gene Ontology (GO)

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:0019290 The chemical reactions and pathways resulting in the formation of siderophores, low molecular weight Fe(III)-chelating substances made by aerobic or facultatively anaerobic bacteria, especially when growing under iron deficient conditions. The complexes of Fe(3+)-siderophores have very high stability constants and are taken up by specific transport systems by microorganisms; the subsequent release of iron requires enzymatic action.
GO:0008667 Catalysis of the reaction: (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + NAD+ = 2,3-dihydroxybenzoate + H+ + NADH.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

31 records

Show feature table

Start	End	DB	Term	Name
1	249	FunFam	G3DSA:3.40.50.720:FF:000160	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
9	180	SMART	SM00822	This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
15	248	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
3	248	PANTHER	PTHR24321	DEHYDROGENASES, SHORT CHAIN
2	250	Gene3D	G3DSA:3.40.50.720	-
134	162	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
134	162	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
127	135	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
127	135	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
74	85	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
74	85	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
147	166	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
147	166	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
4	248	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
4	248	InterPro	IPR036291	NAD(P)-binding domain superfamily
11	251	CDD	cd05331	DH-DHB-DH_SDR_c
11	251	InterPro	IPR003560	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
15	32	PRINTS	PR01397	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature
15	32	InterPro	IPR003560	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
162	185	PRINTS	PR01397	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature
162	185	InterPro	IPR003560	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
201	220	PRINTS	PR01397	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature
201	220	InterPro	IPR003560	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
97	117	PRINTS	PR01397	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature
97	117	InterPro	IPR003560	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
77	94	PRINTS	PR01397	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature
77	94	InterPro	IPR003560	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
227	246	PRINTS	PR01397	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase signature
227	246	InterPro	IPR003560	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
11	250	NCBIfam	TIGR04316	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
11	250	InterPro	IPR003560	2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase

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 · FPocket

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

Site 1 FPocket #1

0.876

Likely same site as P2Rank 1 5.2 Å 34 shared residues 87% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.914

Likely same site as FPocket 1 5.2 Å 34 shared residues 87% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.013

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.011

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #1

0.892

Likely same site as P2Rank 2 6.4 Å 16 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #22

0.531

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.883

Likely same site as FPocket 1 6.7 Å 25 shared residues 74% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.341

Likely same site as FPocket 1 6.4 Å 16 shared residues 100% of smaller site

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_A0A0H3GPR7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03396	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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

A6O PDB via homolog 314.4 Da · LogP 3.93 · TPSA 46.5 Open detail RCSB PDB

BUO PDB via homolog Detail RCSB PDB

ISN PDB via homolog Detail RCSB PDB

RM4 PDB via homolog Detail RCSB PDB

TAM 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
A6O RCSB PDB	6IHH	C0IR58	314.4 Da LogP 3.93 TPSA 46.5	✓ Ro5	✓ Clean	`CC[C@]1([C@H](CCC1=O)O)C/C=C/2\CCCc3c2ccc(c3)OC`
BUO RCSB PDB	5OJG	G5EGA6	86.1 Da LogP 0.16 TPSA 34.1	✓ Ro5	Alert	`CC(=O)C(=O)C`
ISN RCSB PDB	5OJI	G5EGA6	147.1 Da LogP 0.82 TPSA 46.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=O)C(=O)N2`
RM4 RCSB PDB	7DO7	C1DMX5	164.2 Da LogP -2.19 TPSA 90.2	✓ Ro5	✓ Clean	`C[C@H]1[C@@H]([C@H]([C@H]([C@H](O1)O)O)O)O`
TAM RCSB PDB	4BMN	C0IR58	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`
TLA RCSB PDB	5U9P	B4EEX4	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`
TNE RCSB PDB	1XHL	Q19774	139.2 Da LogP 0.81 TPSA 20.3	✓ Ro5	✓ Clean	`CN1[C@H]2CC[C@@H]1CC(=O)C2`

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
ZINC16974563 ZINC	0.727	238.2 Da LogP 2.50 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2C(=O)Nc2ccccc21`
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`
ZINC1845623 ZINC	0.673	312.4 Da LogP 4.13 TPSA 43.4	✓ Ro5	✓ Clean	`CCC1(C/C=C2\CCCc3cc(OC)ccc32)C(=O)CCC1=O`
ZINC1845624 ZINC	0.673	312.4 Da LogP 4.13 TPSA 43.4	✓ Ro5	✓ Clean	`CCC1(C/C=C2/CCCc3cc(OC)ccc32)C(=O)CCC1=O`
ZINC100014196 ZINC	0.667	262.3 Da LogP 2.81 TPSA 58.2	✓ Ro5	Alert	`O=C1/C(=C2\Nc3ccccc3C2=O)Nc2ccccc21`
ZINC100513617 ZINC	0.667	262.3 Da LogP 2.81 TPSA 58.2	✓ Ro5	Alert	`O=C1/C(=C2/Nc3ccccc3C2=O)Nc2ccccc21`
ZINC1857776489 ZINC	0.667	262.3 Da LogP 2.81 TPSA 58.2	✓ Ro5	Alert	`O=C1C(=C2Nc3ccccc3C2=O)Nc2ccccc21`
ZINC3126818 ZINC	0.667	210.2 Da LogP 3.00 TPSA 41.1	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2Nc2ccccc21`
ZINC32915988 ZINC	0.667	262.3 Da LogP 2.50 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2/C1=C1\C(=O)Nc2ccccc21`
ZINC34172946 ZINC	0.667	262.3 Da LogP 2.50 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2/C1=C1/C(=O)Nc2ccccc21`
ZINC45069786 ZINC	0.667	271.3 Da LogP 4.59 TPSA 29.1	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2-c2ccccc2-c2ccccc21`
ZINC6117582 ZINC	0.667	262.3 Da LogP 2.50 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2C1=C1C(=O)Nc2ccccc21`
ZINC401273 ZINC	0.652	238.2 Da LogP 2.50 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2NC(=O)c2ccccc21`
ZINC100015416 ZINC	0.643	262.3 Da LogP 2.66 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2/C1=C1\Nc2ccccc2C1=O`
ZINC1857626905 ZINC	0.643	262.3 Da LogP 2.66 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2C1=C1Nc2ccccc2C1=O`
ZINC18825333 ZINC	0.643	262.3 Da LogP 2.66 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2/C1=C1/Nc2ccccc2C1=O`
ZINC2575038 ZINC	0.625	205.3 Da LogP 0.00 TPSA 86.7	✓ Ro5	✓ Clean	`NC(CCCO)(CCCO)CCCO`
ZINC117753192 ZINC	0.600	203.2 Da LogP 1.65 TPSA 66.4	✓ Ro5	✓ Clean	`C/C(O)=C1\C(=O)Nc2ccccc2C1=O`
ZINC257166 ZINC	0.593	290.3 Da LogP 1.78 TPSA 82.9	✓ Ro5	Alert	`O=C1Nc2ccccc2/C1=N\N=C1\C(=O)Nc2ccccc21`
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`
ZINC85775 ZINC	0.583	210.2 Da LogP 3.31 TPSA 41.1	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2-c2ccccc2N1`
ZINC3023696 ZINC	0.571	257.2 Da LogP -0.24 TPSA 104.4	✓ Ro5	✓ Clean	`O=C1NC(=O)C(=C2C(=O)Nc3ccccc32)C(=O)N1`
ZINC36610867 ZINC	0.571	446.4 Da LogP 3.32 TPSA 116.4	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2/C1=C1\C(=O)Nc2cc3c(cc21)NC(=O)/C3…`
ZINC16948211 ZINC	0.567	223.2 Da LogP 2.49 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1Nc2ccc(-c3ccccc3)cc2C1=O`
ZINC35086915 ZINC	0.567	223.2 Da LogP 2.49 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1Nc2cc(-c3ccccc3)ccc2C1=O`
ZINC16946250 ZINC	0.563	257.7 Da LogP 3.14 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1Nc2ccc(-c3ccccc3Cl)cc2C1=O`
ZINC4644305 ZINC	0.552	277.3 Da LogP 2.41 TPSA 70.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2N/C1=C1\C(=O)Nc2ccccc21`
ZINC16946233 ZINC	0.545	237.3 Da LogP 2.80 TPSA 46.2	✓ Ro5	✓ Clean	`Cc1ccccc1-c1ccc2c(c1)C(=O)C(=O)N2`
ZINC16948184 ZINC	0.545	241.2 Da LogP 2.63 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1Nc2ccc(-c3ccccc3F)cc2C1=O`
ZINC1662285 ZINC	0.544	284.4 Da LogP 3.35 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc2c(c1)CC/C2=C\CC1(C)C(=O)CCC1=O`
ZINC17380200 ZINC	0.544	284.4 Da LogP 3.35 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc2c(c1)CC/C2=C/CC1(C)C(=O)CCC1=O`
ZINC145153554 ZINC	0.538	203.3 Da LogP 0.14 TPSA 54.5	✓ Ro5	✓ Clean	`CS(=O)(=O)N1[C@H]2CC[C@H]1CC(=O)C2`
ZINC101528567 ZINC	0.533	205.2 Da LogP 0.99 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)/C(O)=C1/C(=O)Nc2ccccc21`
ZINC104097396 ZINC	0.533	205.2 Da LogP 0.99 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)/C(O)=C1\C(=O)Nc2ccccc21`
ZINC1735953 ZINC	0.531	224.3 Da LogP 3.30 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccc2c(c1)Nc1ccccc1C(=O)N2`
ZINC63298372 ZINC	0.531	224.3 Da LogP 3.30 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccc2c(c1)NC(=O)c1ccccc1N2`
ZINC107464785 ZINC	0.529	264.3 Da LogP 2.82 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2C(=O)/C1=C\Nc1ccccc1`
ZINC1661289 ZINC	0.517	226.0 Da LogP 1.58 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1Nc2cc(Br)ccc2C1=O`
ZINC223812065 ZINC	0.517	305.3 Da LogP 1.91 TPSA 87.3	✓ Ro5	✓ Clean	`O=C1NC(=O)C(=C2c3ccccc3Nc3ccccc32)C(=O)N1`
ZINC5945548 ZINC	0.517	273.0 Da LogP 1.43 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1Nc2cc(I)ccc2C1=O`
ZINC5948252 ZINC	0.517	221.3 Da LogP 3.42 TPSA 29.1	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2C=Cc2ccccc21`

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.