Protein target profile

VK055_0410

beta-D-hydroxybutyrate dehydrogenase

Genome: KpATCC43816 Gene: AIK79036.1 bdhA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GPA8

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Length 256

Pocket druggability 0.859

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 56 total records

Functional annotation 0 EC 2 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

No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Second pocket predictor agrees P2Rank predicted binding-site probability 0.90. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 8 structural and 0 bioactivity records.

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: Hit
Human identity (%): 38.202 Lower values reduce human off-target concern.
Human E-value: 4.17e-14
Gut microbiome similarity: 1.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 38.132 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.8 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 0.859

Structure A0A0H3GPA8

Pocket Pocket 1

P2Rank 0.897

Structure A0A0H3GPA8

Pocket Pocket 1

ColabFold model

FPocket 0.466 · Pocket 1

P2Rank 0.877 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 58 / 4744 genomes with a hit

Prevalence 1.2%

Cross-references

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

Sequence

UniProt A0A0H3GPA8

Pathways

KEGG R01361 BioCyc 3-HYDROXYBUTYRATE-DEHYDROGENASE-RXN

Metabolic context

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

Explore metabolic network

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MNLHGKTALVTGSTSGIGLGIAKVLAQAGAQLVLNGFGDSSHARAEVAALGKIPGYHDADLRDVGQIEAMMHYAESTFGGVDIVINNAGIQHVAPVEQFPVDKWNDILAINLSSVFHTTRLALPGMRQRNWGRIINIASVHGLVASKEKSAYVAAKHAVVGLTKTVALETARSGITCNAICPGWVLTPLVQQQIDKRIAEGVDPEQASAQLLAEKQPSGEFVTPQQLGEMALFLCSDAAAQVRGAAWNMDGGWVAQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

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:0003858 Catalysis of the reaction: (R)-3-hydroxybutanoate + NAD+ = acetoacetate + H+ + NADH.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
6	256	NCBIfam	TIGR01963	3-hydroxybutyrate dehydrogenase
6	256	InterPro	IPR011294	3-hydroxybutyrate dehydrogenase
1	255	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1	255	InterPro	IPR036291	NAD(P)-binding domain superfamily
139	167	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
139	167	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
1	256	Gene3D	G3DSA:3.40.50.720	-
79	90	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
79	90	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
7	24	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
7	24	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
173	190	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
173	190	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
152	171	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
152	171	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
126	142	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
126	142	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
217	237	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
217	237	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
1	256	FunFam	G3DSA:3.40.50.720:FF:000084	Short-chain dehydrogenase reductase
79	90	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
152	171	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
132	140	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
132	140	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
12	253	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
1	255	PANTHER	PTHR42879	3-OXOACYL-(ACYL-CARRIER-PROTEIN) 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 #1

0.859

Likely same site as P2Rank 1 0.4 Å 31 shared residues 100% of smaller site

Unusual size

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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

0.897

Likely same site as FPocket 1 0.4 Å 31 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.022

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Surrounding area

Site 3 P2Rank #3

0.014

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Surrounding area

Site 4 P2Rank #4

0.006

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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

0.877

Likely same site as FPocket 1 7.4 Å 17 shared residues 94% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.025

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Surrounding area

Site 3 P2Rank #3

0.018

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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_A0A0H3GPA8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0410	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 48 similarity-based ZINC candidates

Best available ligand signal

3HL PDB via homolog 104.1 Da · LogP -0.16 · TPSA 57.5 Open detail RCSB PDB

3HR PDB via homolog Detail RCSB PDB

AAE PDB via homolog Detail RCSB PDB

DXX PDB via homolog Detail RCSB PDB

EMO 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
3HL RCSB PDB	2ZTL	Q5KST5	104.1 Da LogP -0.16 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)O)O`
3HR RCSB PDB	3VDR	D0VWQ0	104.1 Da LogP -0.16 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](CC(=O)O)O`
AAE RCSB PDB	6ZZQ	A0A1E3M3N6	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CC(=O)O`
DXX RCSB PDB	3W8D	D0VWQ0	118.1 Da LogP -0.21 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C(=O)O)C(=O)O`
EMO RCSB PDB	2RH4	P16544	270.2 Da LogP 1.89 TPSA 94.8	✓ Ro5	Alert	`Cc1cc2c(c(c1)O)C(=O)c3c(cc(cc3O)O)C2=O`
ISZ RCSB PDB	1XR3	P16544	135.1 Da LogP 1.25 TPSA 66.2	✓ Ro5	Alert	`[H]/N=N/C(=O)c1ccncc1`
MLA RCSB PDB	3W8F	D0VWQ0	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
QT8 RCSB PDB	6ZZS	A0A1E3M3N6	116.1 Da LogP 0.44 TPSA 54.4	✓ Ro5	✓ Clean	`CCC(=O)CC(=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
ZINC3824868 ZINC	1.000	270.2 Da LogP 1.89 TPSA 94.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC4095655 ZINC	0.735	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)cc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC3978794 ZINC	0.697	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)c2c(c1)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC3861630 ZINC	0.688	254.2 Da LogP 2.18 TPSA 74.6	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cccc(O)c1C2=O`
ZINC14760847 ZINC	0.667	286.2 Da LogP 1.59 TPSA 115.1	✓ Ro5	Alert	`Cc1cc2c(c(O)c1O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC5277130 ZINC	0.656	238.2 Da LogP 2.48 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1ccccc1C2=O`
ZINC4098655 ZINC	0.629	304.7 Da LogP 2.54 TPSA 94.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)c(Cl)c(O)c1C2=O`
ZINC5461939 ZINC	0.618	286.2 Da LogP 1.59 TPSA 115.1	✓ Ro5	Alert	`Cc1cc(O)c2c(c1O)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC14814143 ZINC	0.595	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1c(O)ccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13481200 ZINC	0.594	240.2 Da LogP 1.87 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)cc(O)cc21`
ZINC3977762 ZINC	0.588	300.2 Da LogP 1.28 TPSA 132.1	✓ Ro5	Alert	`O=C(O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC5812872 ZINC	0.588	286.2 Da LogP 1.07 TPSA 115.1	✓ Ro5	Alert	`O=C1c2cc(O)cc(O)c2C(=O)c2c(O)cc(CO)cc21`
ZINC6070245 ZINC	0.588	256.3 Da LogP 2.25 TPSA 77.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)Cc1cc(O)cc(O)c1C2=O`
ZINC14760863 ZINC	0.579	300.3 Da LogP 1.90 TPSA 104.1	✓ Ro5	Alert	`COc1c(O)c(C)cc2c1C(=O)c1c(O)cc(O)cc1C2=O`
ZINC6070262 ZINC	0.579	314.2 Da LogP 1.59 TPSA 132.1	✓ Ro5	Alert	`Cc1cc2c(c(O)c1C(=O)O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC14819806 ZINC	0.568	314.3 Da LogP 1.50 TPSA 115.1	✓ Ro5	Alert	`C[C@@H](O)Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC14819808 ZINC	0.568	314.3 Da LogP 1.50 TPSA 115.1	✓ Ro5	Alert	`C[C@H](O)Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC31163880 ZINC	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@@H](O)[C@@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc…`
ZINC31163884 ZINC	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@H](O)[C@@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(…`
ZINC31163888 ZINC	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@@H](O)[C@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(…`
ZINC31163892 ZINC	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@H](O)[C@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(O…`
ZINC13334425 ZINC	0.564	268.3 Da LogP 2.48 TPSA 63.6	✓ Ro5	Alert	`COc1cccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13546016 ZINC	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@@H](C)CC(=O)O`
ZINC13546018 ZINC	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@@H](C)CC(=O)O`
ZINC257400894 ZINC	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@H](C)CC(=O)O`
ZINC257400895 ZINC	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@H](C)CC(=O)O`
ZINC14760819 ZINC	0.553	300.3 Da LogP 1.90 TPSA 104.1	✓ Ro5	Alert	`COc1cc(O)c2c(c1O)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC5412537 ZINC	0.553	316.3 Da LogP 1.60 TPSA 124.3	✓ Ro5	Alert	`COc1c(O)c(O)c2c(c1O)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC20111521 ZINC	0.550	327.3 Da LogP 1.95 TPSA 98.1	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)c(CN(C)C)c(O)c1C2=O`
ZINC77257242 ZINC	0.538	316.3 Da LogP 1.43 TPSA 124.3	✓ Ro5	Alert	`COCc1c(O)cc2c(c1O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC1637808 ZINC	0.528	267.1 Da LogP 2.36 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)C=C(Br)C2=O`
ZINC14811261 ZINC	0.512	300.3 Da LogP 1.37 TPSA 104.1	✓ Ro5	Alert	`COc1cc(CO)cc2c1C(=O)c1c(O)cc(O)cc1C2=O`
ZINC137596932 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@H]3O[C@@H](CO…`
ZINC2053539354 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@H]3O[C@H](CO)…`
ZINC2080144947 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@H]3O[C@H](CO)…`
ZINC2080147051 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O…`
ZINC238733159 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O[C@H]2O[C@@H](CO)[C@H](O)[C@@H](O)[C@@H]…`
ZINC238774329 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@@H]3O[C@H](CO…`
ZINC253593197 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@@H]3O[C@@H](C…`
ZINC253598174 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O[C@@H]2O[C@@H](CO)[C@H](O)[C@@H](O)[C@@H…`
ZINC33832450 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O[C@@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2…`
ZINC4098672 ZINC	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@@H]3O[C@H](CO…`
ZINC14814264 ZINC	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@@H]3O[C@H](C)[C@@H…`
ZINC14814268 ZINC	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@H]3O[C@H](C)[C@@H]…`
ZINC2332918206 ZINC	0.500	388.8 Da LogP 2.98 TPSA 107.0	✓ Ro5	Alert	`CC(=O)Oc1cc2c(c(OC(C)=O)c1Cl)C(=O)c1c(O)cc(C)cc…`
ZINC253477263 ZINC	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@@H]3O[C@H](C)[C@H]…`
ZINC31425373 ZINC	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@H]3O[C@@H](C)[C@H]…`
ZINC4098673 ZINC	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@@H]3O[C@@H](C)[C@H…`

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.