Protein target profile

VK055_3135

fatty oxidation complex, alpha subunit FadB

Genome: KpATCC43816 Gene: fadB AIK81707.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 5 reactions UniProt A0A0H3GPY7

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Length 729

Pocket druggability 0.91

Metabolic reactions 5

Chokepoint No

Direct ligand evidence 0 58 total records

Functional annotation 0 EC 14 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

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.91, P2Rank 0.86). Use the 3D pocket comparison to verify whether they identify the same site. Central metabolic position More central than 97.1% of genes in this genome. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.91. This is a computational pocket signal, not binding validation. 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: Hit
Human identity (%): 42.742 Lower values reduce human off-target concern.
Human E-value: 6.27e-25
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 55.804 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.55 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 0.91

Structure A0A0H3GPY7

Pocket Pocket 1

P2Rank 0.861

Structure A0A0H3GPY7

Pocket Pocket 1

ColabFold model

FPocket 0.919 · Pocket 1

P2Rank 0.822 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 143 / 4744 genomes with a hit

Prevalence 3.0%

Cross-references

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

Sequence

UniProt A0A0H3GPY7

Pathways

KEGG R06942 BioCyc RXN-2425 BioCyc RXN0-5393 BioCyc RXN-17780 BioCyc RXN-2002 BioCyc RXN-17776

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 97.1% of genes in this genome.

Relative network centrality 97.1% more central than 97.1% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGHALDVLEKQSDLKGLLLRSEKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTISAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDVGADQALKIGLVDGVVAAEKLRDGALAILRQAMNGDLDWKAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARLGREEALVLENKSFVPLAHTNEARALVGIFLNDQYVKAKAKKLTKDVETPKHAAVLGAGIMGGGIAYQSAWKGVPVVMKDISDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIQPTLEYSGFDRVDVVVEAVVENPKVKKAVLAETEAKVRPDTVLASNTSTIPISELASVLQRPENFCGMHFFNPVHRMPLVEVIRGEKTSDNTIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKDDSKGKPKKEEDAAVDSLLADVSQPKRDFSDEEIIARMMIPMVNEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTIGSAKYLDMAQQYQHLGPLYEVPAGLRDKARHNEAYYPQVEPARPVGALKTA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

14 GO

Gene Ontology (GO)

GO:0003857 Catalysis of the reaction: a (3S)-3-hydroxyacyl-CoA + NAD+ = a 3-oxoacyl-CoA + NADH + H+.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
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:0008692 Catalysis of the reaction: (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
GO:0004300 Catalysis of the reaction: a 3-hydroxy-fatty acyl-CoA = a enoyl-CoA + H2O. This reaction usually occurs in the reverse direction, leading to the reduction of the double bound of enoyl-CoA in position 2 or 3. Specific reactions catalyzed include: a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O and a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O.
GO:0036125 A multienzyme complex possessing three kinds of enzymes that catalyze the chain reactions in the fatty acid beta-oxidation cycle, enoyl-CoA hydratase (ECH), 3-hydroxyacyl-CoA dehydrogenase (HACD), and acetyl-CoA C-acyltransferase (KACT).
GO:0009062 The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0070403 Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
GO:0004165 Catalysis of the reactions: a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA or a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA.
GO:0018812 Catalysis of the reaction: a 3-hydroxy-fatty acyl-CoA = a (2E)-enoyl-CoA + H2O.
GO:0016509 Catalysis of the reaction: a long-chain (3S)-3-hydroxy fatty acyl-CoA + NAD+ = a long-chain 3-oxo-fatty acyl-CoA + H+ + NADH. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons.
GO:0006635 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
496	592	Pfam	PF00725	3-hydroxyacyl-CoA dehydrogenase, C-terminal domain
496	592	InterPro	IPR006108	3-hydroxyacyl-CoA dehydrogenase, C-terminal
627	691	Pfam	PF00725	3-hydroxyacyl-CoA dehydrogenase, C-terminal domain
627	691	InterPro	IPR006108	3-hydroxyacyl-CoA dehydrogenase, C-terminal
1	714	NCBIfam	TIGR02437	fatty acid oxidation complex subunit alpha FadB
1	714	InterPro	IPR012799	Fatty oxidation complex, alpha subunit FadB
1	312	FunFam	G3DSA:3.90.226.10:FF:000018	Fatty acid oxidation complex subunit alpha
499	714	FunFam	G3DSA:1.10.1040.50:FF:000001	Fatty acid oxidation complex subunit alpha
14	203	CDD	cd06558	crotonase-like
1	715	Hamap	MF_01621	Fatty acid oxidation complex subunit alpha [fadB].
1	715	InterPro	IPR012799	Fatty oxidation complex, alpha subunit FadB
622	714	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
622	714	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
493	517	ProSitePatterns	PS00067	3-hydroxyacyl-CoA dehydrogenase signature.
493	517	InterPro	IPR006180	3-hydroxyacyl-CoA dehydrogenase, conserved site
106	126	ProSitePatterns	PS00166	Enoyl-CoA hydratase/isomerase signature.
106	126	InterPro	IPR018376	Enoyl-CoA hydratase/isomerase, conserved site
4	714	PANTHER	PTHR43612	TRIFUNCTIONAL ENZYME SUBUNIT ALPHA
313	498	FunFam	G3DSA:3.40.50.720:FF:000009	Fatty oxidation complex, alpha subunit
313	498	Gene3D	G3DSA:3.40.50.720	-
314	495	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
314	495	InterPro	IPR036291	NAD(P)-binding domain superfamily
316	494	Pfam	PF02737	3-hydroxyacyl-CoA dehydrogenase, NAD binding domain
316	494	InterPro	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
3	303	SUPERFAMILY	SSF52096	ClpP/crotonase
3	303	InterPro	IPR029045	ClpP/crotonase-like domain superfamily
1	312	Gene3D	G3DSA:3.90.226.10	-
499	718	Gene3D	G3DSA:1.10.1040.50	-
14	206	Pfam	PF00378	Enoyl-CoA hydratase/isomerase
14	206	InterPro	IPR001753	Enoyl-CoA hydratase/isomerase
495	638	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
495	638	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily

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

0.91

Likely same site as P2Rank 2 1.6 Å 21 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #28

0.262

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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

0.861

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Surrounding area

Site 2 P2Rank #2

0.795

Likely same site as FPocket 1 1.6 Å 21 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.515

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Surrounding area

Site 4 P2Rank #4

0.266

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Surrounding area

Site 5 P2Rank #5

0.056

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Surrounding area

Residue sets

UniProt: Active site:450-450 For 3-hydroxyacyl-CoA dehydrogenase activity

UniProt: Binding site:296-296

UniProt: Binding site:324-324

UniProt: Binding site:343-343

UniProt: Binding site:400-402

UniProt: Binding site:407-407

UniProt: Binding site:429-429

UniProt: Binding site:453-453

UniProt: Binding site:500-500

UniProt: Binding site:660-660

UniProt: Site:119-119 Important for catalytic activity

UniProt: Site:139-139 Important for catalytic activity

Binding pockets · FPocket

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

Site 1 FPocket #1

0.919

Likely same site as P2Rank 2 1.8 Å 20 shared residues 95% of smaller site

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Surrounding area

Site 2 FPocket #10

0.549

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Surrounding area

Site 3 FPocket #47

0.459

Likely same site as P2Rank 2 7.8 Å 9 shared residues 64% of smaller site

Unusual size

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Surrounding area

Site 4 FPocket #48

0.318

Likely same site as P2Rank 1 3.2 Å 20 shared residues 91% 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

0.822

Likely same site as FPocket 48 3.2 Å 20 shared residues 91% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.774

Likely same site as FPocket 1 1.8 Å 20 shared residues 95% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.318

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Surrounding area

Site 4 P2Rank #4

0.144

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Surrounding area

Site 5 P2Rank #5

0.051

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Surrounding area

Residue sets

UniProt: Active site:450-450 For 3-hydroxyacyl-CoA dehydrogenase activity

UniProt: Binding site:296-296

UniProt: Binding site:324-324

UniProt: Binding site:343-343

UniProt: Binding site:400-402

UniProt: Binding site:407-407

UniProt: Binding site:429-429

UniProt: Binding site:453-453

UniProt: Binding site:500-500

UniProt: Binding site:660-660

UniProt: Site:119-119 Important for catalytic activity

UniProt: Site:139-139 Important for catalytic activity

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_A0A0H3GPY7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3135	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.

58 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 50 similarity-based ZINC candidates

Best available ligand signal

3H9 PDB via homolog 877.7 Da · LogP -3.31 · TPSA 395.2 Open detail RCSB PDB

3HC PDB via homolog Detail RCSB PDB

CAA PDB via homolog Detail RCSB PDB

HSC PDB via homolog Detail RCSB PDB

N8E 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
3H9 RCSB PDB	3ZWA	P07896	877.7 Da LogP -3.31 TPSA 395.2	3 viol.	✓ Clean	`CCC[C@@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)…`
3HC RCSB PDB	1F12	Q16836	853.6 Da LogP -1.56 TPSA 383.9	3 viol.	✓ Clean	`CC(CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](…`
CAA RCSB PDB	4KUH	C4IEM5	851.6 Da LogP -1.36 TPSA 380.7	3 viol.	✓ Clean	`CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
HSC RCSB PDB	3ZWC	P07896	933.8 Da LogP -1.75 TPSA 395.2	3 viol.	✓ Clean	`CCCCCCC[C@@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C…`
N8E RCSB PDB	1WDL	P28793	350.5 Da LogP 2.42 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCOCCO`
T1G RCSB PDB	3ZW9	P07896	863.6 Da LogP -3.85 TPSA 395.2	3 viol.	✓ Clean	`C[C@@H]([C@H](C)O)C(=O)SCCNC(=O)CCNC(=O)[C@@H](…`
TC6 RCSB PDB	3ZWB	P07896	859.6 Da LogP -2.51 TPSA 374.9	2 viol.	✓ Clean	`CCC/C=C/C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP…`
ZOZ RCSB PDB	5OMO	P07896	935.8 Da LogP 0.98 TPSA 380.7	3 viol.	✓ Clean	`CCCCCCCC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(…`

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
ZINC100014200 ZINC	1.000	494.7 Da LogP 4.02 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC100070166 ZINC	1.000	290.4 Da LogP 3.17 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCO`
ZINC100310628 ZINC	1.000	478.7 Da LogP 4.78 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC100365196 ZINC	1.000	302.5 Da LogP 4.71 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCO`
ZINC101772322 ZINC	1.000	434.7 Da LogP 4.76 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC103600921 ZINC	1.000	466.7 Da LogP 3.24 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC14880431 ZINC	1.000	378.6 Da LogP 3.20 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC14881140 ZINC	1.000	306.4 Da LogP 2.41 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCO`
ZINC16051619 ZINC	1.000	350.5 Da LogP 2.42 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCOCCO`
ZINC2584424 ZINC	1.000	218.3 Da LogP 2.37 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCO`
ZINC4521877 ZINC	1.000	234.3 Da LogP 1.61 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCO`
ZINC5273610 ZINC	1.000	322.4 Da LogP 1.64 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCOCCOCCO`
ZINC58538366 ZINC	1.000	392.6 Da LogP 3.59 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC58631420 ZINC	1.000	422.6 Da LogP 3.22 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC59441819 ZINC	1.000	318.5 Da LogP 3.95 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCO`
ZINC59622400 ZINC	1.000	274.4 Da LogP 3.93 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCO`
ZINC71788551 ZINC	1.000	334.5 Da LogP 3.19 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCO`
ZINC71788564 ZINC	1.000	262.4 Da LogP 2.39 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCO`
ZINC71788567 ZINC	1.000	406.6 Da LogP 3.98 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC8214594 ZINC	1.000	362.6 Da LogP 3.97 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCO`
ZINC88260008 ZINC	1.000	390.6 Da LogP 4.75 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCO`
ZINC95784968 ZINC	1.000	450.7 Da LogP 4.00 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC95863931 ZINC	1.000	464.7 Da LogP 4.39 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC1849711 ZINC	0.950	202.3 Da LogP 3.14 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCO`
ZINC1850542 ZINC	0.950	216.4 Da LogP 3.53 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCOCCO`
ZINC2555269 ZINC	0.950	220.3 Da LogP 1.22 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCOCCOCCOCCO`
ZINC59660505 ZINC	0.950	244.4 Da LogP 4.31 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCO`
ZINC8437287 ZINC	0.950	230.4 Da LogP 3.92 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCO`
ZINC85733754 ZINC	0.950	258.4 Da LogP 4.70 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCO`
ZINC1644613 ZINC	0.810	206.3 Da LogP 0.83 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCO`
ZINC59545536 ZINC	0.773	258.4 Da LogP 4.70 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCCO`
ZINC95831576 ZINC	0.773	230.4 Da LogP 3.92 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCCCO`
ZINC1627284 ZINC	0.700	214.4 Da LogP 4.94 TPSA 9.2	✓ Ro5	✓ Clean	`CCCCCCCOCCCCCCC`
ZINC2564179 ZINC	0.700	214.4 Da LogP 4.94 TPSA 9.2	✓ Ro5	✓ Clean	`CCCCCCCCOCCCCCC`
ZINC100302699 ZINC	0.600	332.5 Da LogP 3.48 TPSA 65.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCOCCOCCO`
ZINC101013974 ZINC	0.600	273.5 Da LogP 3.90 TPSA 44.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCN`
ZINC101367966 ZINC	0.600	232.3 Da LogP 1.90 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOCCO`
ZINC44583812 ZINC	0.600	380.6 Da LogP 3.49 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCCCCCCCCCCS`
ZINC44583816 ZINC	0.600	468.7 Da LogP 3.52 TPSA 75.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCCCCCCCCCCS`
ZINC6620298 ZINC	0.600	336.5 Da LogP 3.47 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCCCCCCCCCCS`
ZINC86039630 ZINC	0.600	288.4 Da LogP 3.46 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCOCCO`
ZINC100684628 ZINC	0.586	330.6 Da LogP 4.77 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC[N+](C)(C)CCOCCO`
ZINC4978403 ZINC	0.583	248.4 Da LogP 2.00 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCCOCCCOCCCO`
ZINC100090646 ZINC	0.571	448.6 Da LogP 4.86 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCC(=O)O`
ZINC100645716 ZINC	0.571	273.5 Da LogP 4.60 TPSA 35.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCC(N)=S`
ZINC100970335 ZINC	0.571	331.5 Da LogP 3.44 TPSA 70.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCC(N)=O`
ZINC2041048 ZINC	0.571	218.3 Da LogP 2.64 TPSA 27.7	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCCC`
ZINC1697133 ZINC	0.565	214.4 Da LogP 4.94 TPSA 9.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCC`
ZINC5650743 ZINC	0.565	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.565	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`

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.