Protein target profile

VK055_2170

FAD binding domain protein

Genome: KpATCC43816 Gene: AIK80775.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GP09

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Length 561

Pocket druggability 1

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

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: No hit
Gut microbiome similarity: 0.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 35.201 Higher values support similarity to known essential genes.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 95.33 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 1

Structure A0A0H3GP09

Pocket Pocket 1

P2Rank 0.995

Structure A0A0H3GP09

Pocket Pocket 1

ColabFold model

FPocket 1 · Pocket 1

P2Rank 0.995 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 20 / 4744 genomes with a hit

Prevalence 0.4%

Cross-references

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

Sequence

UniProt A0A0H3GP09

Sequence

Primary amino-acid sequence viewer.

MKVDVLVVGSGAAGLSAAVTAAMHGASVMVAEKASVLGGTSAWSGGWLWIPRNPLARAEGIDEAADAPLTYLQHEMGGEAADIRLQTFLRYGPEMVEFFHQRTAVQFLSGSAMPDFHPSPGAANGGRSVTAQPYDGRLLGDWLHRLRPPLETISLGGMGIAGGADMAHFFNATRSPRSALYAARRLLRHGWQRLRAGRGQHLVNGNALVARLLRSALDAGVRFQLNAPVVRLLQGPPGVSGAVLRSDGGEIHVEAGAVVLACGGFPHDRQRLAQVVPHAAEGYGHFSAAPPDNQGEGIRLGESVGGQFDTSLRHPLAWAPVSRVTLASGQQLMFPHLVERAKPGVIAVLPNGKRFVNEADSYHDFIAALLAATPAGDTPQAWLLADRRALRRYGLGHARPFPFTPTAWLRTSYLQRGNTLAELAKQCAIDANALAETVERFNHFASAGEDVDFHRGASAYNRAQGDHQVTLGPLREGPFYAVRILPGSLGTFSGLQTDEHARVLDEQQQPIPGLYAIGNDMSSVMRGYYPSGGITLGPAMTFGYLVGKNLAKKTNINNNIA

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:0008202 The chemical reactions and pathways involving steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
4	536	InterPro	IPR003953	FAD-dependent oxidoreductase 2, FAD binding domain
3	553	PANTHER	PTHR43400	FUMARATE REDUCTASE
4	26	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
511	526	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
314	495	SUPERFAMILY	SSF56425	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
314	495	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
5	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	553	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
1	553	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
5	27	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
4	536	Pfam	PF00890	FAD binding domain
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
22	561	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
432	552	Gene3D	G3DSA:3.50.50.60	-
432	552	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	381	Gene3D	G3DSA:3.50.50.60	-
1	381	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
17	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region

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

1.0

Likely same site as P2Rank 1 1.2 Å 73 shared residues 87% 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

0.995

Likely same site as FPocket 1 1.2 Å 73 shared residues 87% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.429

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Surrounding area

Site 3 P2Rank #3

0.15

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Surrounding area

Site 4 P2Rank #4

0.099

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Surrounding area

Site 5 P2Rank #5

0.027

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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

0.995

Likely same site as FPocket 1 1.4 Å 73 shared residues 88% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.315

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Surrounding area

Site 3 P2Rank #3

0.071

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Surrounding area

Site 4 P2Rank #4

0.034

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Surrounding area

Site 5 P2Rank #5

0.025

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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_A0A0H3GP09	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2170	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 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ANB PDB via homolog 284.4 Da · LogP 3.86 · TPSA 34.1 Open detail RCSB PDB

ASD PDB via homolog Detail RCSB PDB

FUM PDB via homolog Detail RCSB PDB

MEZ PDB via homolog Detail RCSB PDB

SIN 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
ANB RCSB PDB	4C3Y	Q9RA02	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@H]([C@@H]1CCC2=O)CCC4=CC(=O)C…`
ASD RCSB PDB	4AT2	Q0S4Q9	286.4 Da LogP 4.09 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12CCC(=O)C=C1CC[C@@H]3[C@@H]2CC[C@]4([C@H]…`
FUM RCSB PDB	1E39	P0C278	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
MEZ RCSB PDB	1Y0P	P0C278	130.1 Da LogP 0.10 TPSA 74.6	✓ Ro5	✓ Clean	`C/C(=C\C(=O)O)/C(=O)O`
SIN RCSB PDB	1D4D	P83223	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)O`
TEO RCSB PDB	1P2H	P0C278	132.1 Da LogP -3.14 TPSA 103.7	✓ Ro5	✓ Clean	`C(=C(\O)/[O-])\[C@H](C(=O)[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
ZINC156796 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@@]2(C)C…`
ZINC2100022 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@@]2(C)C…`
ZINC242548813 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@H]1[C@H]2CC[C@]2(C)C(=O…`
ZINC253502176 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)C=C[C@]43C)[C@…`
ZINC3881421 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@]2(C)C(…`
ZINC4023563 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43C)[…`
ZINC4023564 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@H]2CC[C@]2(C)C(=…`
ZINC4023565 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@]2(C)C(…`
ZINC4534007 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@]12C=CC(=O)C=C1CC[C@H]1[C@H]2CC[C@@]2(C)C(…`
ZINC58482279 ZINC	1.000	284.4 Da LogP 3.86 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@H]1[C@H]2CC[C@@]2(C)C(=…`
ZINC253499744 ZINC	0.791	282.4 Da LogP 4.85 TPSA 17.1	✓ Ro5	✓ Clean	`C=C1C=C[C@@]2(C)C(=C1)CC[C@@H]1[C@H]2CC[C@]2(C)…`
ZINC253499746 ZINC	0.791	282.4 Da LogP 4.85 TPSA 17.1	✓ Ro5	✓ Clean	`C=C1C=C[C@@]2(C)C(=C1)CC[C@@H]1[C@@H]2CC[C@]2(C…`
ZINC4024379 ZINC	0.791	282.4 Da LogP 4.85 TPSA 17.1	✓ Ro5	✓ Clean	`C=C1C=C[C@@]2(C)C(=C1)CC[C@H]1[C@@H]3CCC(=O)[C@…`
ZINC4024380 ZINC	0.791	282.4 Da LogP 4.85 TPSA 17.1	✓ Ro5	✓ Clean	`C=C1C=C[C@@]2(C)C(=C1)CC[C@@H]1[C@@H]2CC[C@]2(C…`
ZINC253617340 ZINC	0.767	286.4 Da LogP 2.59 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43O)[…`
ZINC253617341 ZINC	0.767	286.4 Da LogP 2.59 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)C=C[C@@]43O)[C…`
ZINC4292864 ZINC	0.767	286.4 Da LogP 2.59 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)C=C[C@@]43O)[C…`
ZINC4292866 ZINC	0.767	286.4 Da LogP 2.59 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43O)[…`
ZINC2386384549 ZINC	0.727	304.8 Da LogP 3.83 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43Cl)[…`
ZINC13513686 ZINC	0.674	300.4 Da LogP 2.83 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12C[C@H](O)[C@H]3[C@@H](CCC4=CC(=O)C=C[C@@…`
ZINC1730510 ZINC	0.674	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2C(=O)C[C@@]2…`
ZINC1857623168 ZINC	0.674	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2C(=O)C[C@@]2…`
ZINC1857623169 ZINC	0.674	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43…`
ZINC254071261 ZINC	0.674	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@H]1[C@H]2C(=O)C[C@@]2(C…`
ZINC254071263 ZINC	0.674	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@@H]3[C@H](CCC4=CC(=O)C=C[C@@]43…`
ZINC254071265 ZINC	0.674	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@@]12C=CC(=O)C=C1CC[C@H]1[C@H]2C(=O)C[C@]2(C…`
ZINC4533967 ZINC	0.674	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@@]12C=CC(=O)C=C1CC[C@H]1[C@H]2C(=O)C[C@@]2(…`
ZINC4706361 ZINC	0.674	300.4 Da LogP 2.83 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12C[C@@H](O)[C@H]3[C@@H](CCC4=CC(=O)C=C[C@…`
ZINC4897138 ZINC	0.674	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43…`
ZINC31623358 ZINC	0.673	328.4 Da LogP 3.16 TPSA 60.4	✓ Ro5	✓ Clean	`CC(=O)O[C@]12C=CC(=O)C=C1CC[C@H]1[C@@H]3CCC(=O)…`
ZINC118912522 ZINC	0.667	300.4 Da LogP 4.05 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@@]2(C)[…`
ZINC3875469 ZINC	0.667	300.4 Da LogP 4.05 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@@]2(C)[…`
ZINC4023051 ZINC	0.667	300.4 Da LogP 4.05 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@H]1[C@@H]3CC[C@](C)(O)[…`
ZINC4023052 ZINC	0.667	300.4 Da LogP 4.05 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@H]2CC[C@@]2(C)[C…`
ZINC4023053 ZINC	0.667	300.4 Da LogP 4.05 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@@]2(C)[…`
ZINC105025894 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)C=C[C@@]43C)[C…`
ZINC11592582 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)C=C[C@]43C)[C@…`
ZINC3831512 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@@]12CC[C@@H]3[C@H](CCC4=CC(=O)C=C[C@]43C)[C…`
ZINC3831513 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)C=C[C@]43C)[C@…`
ZINC3831514 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@@]12CC[C@H]3[C@H](CCC4=CC(=O)C=C[C@]43C)[C@…`
ZINC3831515 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@H](CCC4=CC(=O)C=C[C@]43C)[C@@…`
ZINC4081770 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43C)[…`
ZINC4081771 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43C)[C…`
ZINC4081773 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CCC4=CC(=O)C=C[C@@]43C)[…`
ZINC4081774 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@]2(C)OC…`
ZINC5529977 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)C=C[C@@]43C)[C…`
ZINC5530039 ZINC	0.660	300.4 Da LogP 3.59 TPSA 43.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@H](CCC4=CC(=O)C=C[C@@]43C)[C@…`
ZINC253618127 ZINC	0.652	286.4 Da LogP 3.66 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1CC[C@@H]1[C@@H]2CC[C@@]2(C)[…`
ZINC97975660 ZINC	0.652	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC(=O)C4=CC(=O)C=C[C@@]4…`
ZINC97975661 ZINC	0.652	298.4 Da LogP 3.04 TPSA 51.2	✓ Ro5	✓ Clean	`C[C@]12C=CC(=O)C=C1C(=O)C[C@@H]1[C@H]2CC[C@]2(C…`

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.