Protein target profile

KP13_05499

3-oxoacyl-[acyl-carrier-protein] synthase 2

Genome: KpKP13 Gene: AHE44505.1 fabF 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTQ4

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Length 424

Pocket druggability 0.799

Direct ligand evidence 0 63 total records

Functional annotation 1 EC 5 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 0.80, P2Rank 0.85). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.80. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.85. 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 (%): 48.077 Lower values reduce human off-target concern.
Human E-value: 1.78e-10
Gut microbiome similarity: 1.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 50.939 Higher values support similarity to known essential genes.
DEG E-value: 4.19e-148 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.96 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 0.799

Structure A0A0H3GTQ4

Pocket Pocket 1

P2Rank 0.854

Structure A0A0H3GTQ4

Pocket Pocket 1

ColabFold model

FPocket 0.794 · Pocket 1

P2Rank 0.876 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 64 / 4744 genomes with a hit

Prevalence 1.3%

Cross-references

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

Sequence

UniProt A0A0H3GTQ4

Sequence

Primary amino-acid sequence viewer.

MGVSVKRIVVTGMGIVSPLGCGVQHVWQSLLAGKSGITRLSEQLVADIPCKVAGQVPSIESDPLHGFDPLATIPAKERKKMDRFIEFALVAAREALTQAGWSPASAAEQERTATVIATGIGGFSEIANAVHTTDERGPRRLSPFTIPSFLANLAAGHVSIAHGFRGPIGAPVTACAAGAQAIGDAARMIRSGEADIALCGGAEAAIHRVSLAGFAAARALSSASNDQPEAASRPFDRDRDGFVMGEGAGLIVIESLEHALARGATPLAELVGYGTSADAYHLTAGPEDGNGARRAMETAIRQAGVTVDEIDHINAHATSTQVGDKGELAAIKTLFGAHPVAITSTKSATGHLLGAAGGIEAIFTIQALRDQVVPPTLNLHHPDEEAAGLNLVALQARPQKMRYALSNGFGFGGVNASLLLKRWE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

2.3.1.179

Gene Ontology (GO)

GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
GO:0006633 The chemical reactions and pathways resulting in the formation 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:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
3	424	PIRSF	PIRSF000447	KAS_II
3	424	InterPro	IPR017568	3-oxoacyl-[acyl-carrier-protein] synthase 2
6	421	PANTHER	PTHR11712	POLYKETIDE SYNTHASE-RELATED
6	421	InterPro	IPR000794	Beta-ketoacyl synthase
166	182	ProSitePatterns	PS00606	Ketosynthase family 3 (KS3) active site signature.
166	182	InterPro	IPR018201	Beta-ketoacyl synthase, active site
6	264	SUPERFAMILY	SSF53901	Thiolase-like
6	264	InterPro	IPR016039	Thiolase-like
3	423	FunFam	G3DSA:3.40.47.10:FF:000009	3-oxoacyl-[acyl-carrier-protein] synthase 2
2	424	Gene3D	G3DSA:3.40.47.10	-
2	424	InterPro	IPR016039	Thiolase-like
8	423	SMART	SM00825	Beta-ketoacyl synthase
8	423	InterPro	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain
6	259	Pfam	PF00109	Beta-ketoacyl synthase, N-terminal domain
6	259	InterPro	IPR014030	Beta-ketoacyl synthase, N-terminal
5	422	ProSiteProfiles	PS52004	Ketosynthase family 3 (KS3) domain profile.
5	422	InterPro	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain
6	420	CDD	cd00834	KAS_I_II
6	420	InterPro	IPR000794	Beta-ketoacyl synthase
267	379	Pfam	PF02801	Beta-ketoacyl synthase, C-terminal domain
267	379	InterPro	IPR014031	Beta-ketoacyl synthase, C-terminal
227	423	SUPERFAMILY	SSF53901	Thiolase-like
227	423	InterPro	IPR016039	Thiolase-like
6	421	NCBIfam	TIGR03150	beta-ketoacyl-ACP synthase II
6	421	InterPro	IPR017568	3-oxoacyl-[acyl-carrier-protein] synthase 2

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

0.799

Likely same site as P2Rank 1 1.8 Å 25 shared residues 96% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #13

0.252

Likely same site as P2Rank 3 7.5 Å 3 shared residues 43% of smaller site

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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

0.854

Likely same site as FPocket 1 1.8 Å 25 shared residues 96% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.09

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Surrounding area

Site 3 P2Rank #3

0.076

Likely same site as FPocket 13 7.5 Å 3 shared residues 43% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.02

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Surrounding area

Site 5 P2Rank #5

0.009

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Surrounding area

Residue sets

UniProt: Active site:175-175 For beta-ketoacyl synthase activity

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.876

Likely same site as FPocket 1 1.5 Å 27 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.108

Likely same site as FPocket 1 7.9 Å 7 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.085

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Surrounding area

Site 4 P2Rank #4

0.023

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Surrounding area

Site 5 P2Rank #5

0.013

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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_A0A0H3GTQ4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05499	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.

63 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 13 records from similar proteins

Structural ligands 13 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1LR PDB via homolog 257.2 Da · LogP 2.34 · TPSA 86.6 Open detail RCSB PDB

1X9 PDB via homolog Detail RCSB PDB

1XG PDB via homolog Detail RCSB PDB

840 PDB via homolog Detail RCSB PDB

CER 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
1LR RCSB PDB	4JPF	G3XDA2	257.2 Da LogP 2.34 TPSA 86.6	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)Nc2cccc(c2O)C(=O)O`
1X9 RCSB PDB	4LS7	O34340	223.3 Da LogP 1.11 TPSA 72.7	✓ Ro5	✓ Clean	`C/C=C/C/C=C/CCC(=O)[C@@H]1[C@@H](O1)C(=O)N`
1XG RCSB PDB	4LS8	O34340	225.3 Da LogP 1.09 TPSA 80.4	✓ Ro5	✓ Clean	`C/C=C/C/C=C/CCC(=O)[C@@H](CC(=O)N)O`
840 RCSB PDB	3I8P	P0AAI5	455.5 Da LogP 1.96 TPSA 153.4	✓ Ro5	✓ Clean	`C[C@@]1([C@H]2[C@@]34C[C@]35CC2(C=CC1=O)[C@H]([…`
CER RCSB PDB	1B3N	P0AAI5	225.3 Da LogP 1.09 TPSA 80.4	✓ Ro5	✓ Clean	`C\C=C\C\C=C\CCC(=O)[C@H](CC(=O)N)O`
DAO RCSB PDB	2GFY	P0AAI5	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
MRJ RCSB PDB	6OLT	P0AAI5	523.6 Da LogP 2.14 TPSA 174.3	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C)…`
MU4 RCSB PDB	6OKG	P0AAI5	579.7 Da LogP 3.70 TPSA 174.3	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C…`
N32 RCSB PDB	4F32	A4JL30	425.5 Da LogP 4.02 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@]1([C@@H]2C[C@@H]3CC[C@]2(CC3=C)C=CC1=O)CC…`
N3A RCSB PDB	3HO9	P0AAI5	441.5 Da LogP 2.99 TPSA 144.2	✓ Ro5	✓ Clean	`C[C@@]1([C@@H]2C[C@@H]3C[C@H]([C@]2(CC3=C)C=CC1…`
P9A RCSB PDB	3G0Y	P0AAI5	443.5 Da LogP 3.46 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@@]12C[C@@]34CCC(=O)[C@@]([C@@H]3[C@@H](O1)C…`
P9C RCSB PDB	3G11	P0AAI5	519.6 Da LogP 4.85 TPSA 133.2	1 viol.	✓ Clean	`C[C@]12C[C@]34C[C@H]1C[C@@H]([C@H]3[C@](C(=O)C[…`
PMN RCSB PDB	2GFX	P0AAI5	441.5 Da LogP 3.23 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@]12C[C@]34C[C@H]1C[C@@H]([C@H]3[C@](C(=O)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
ZINC1429478 ZINC	1.000	257.2 Da LogP 2.34 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1ccccc1`
ZINC1529498 ZINC	1.000	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
ZINC1530417 ZINC	1.000	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
ZINC1628119 ZINC	1.000	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
ZINC168677815 ZINC	1.000	441.5 Da LogP 3.23 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@@]1(CCC(=O)Nc2c(O)ccc(C(=O)O)c2O)C(=O)C=C[C…`
ZINC256352556 ZINC	1.000	441.5 Da LogP 3.23 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@@]1(CCC(=O)Nc2c(O)ccc(C(=O)O)c2O)C(=O)C=C[C…`
ZINC29050726 ZINC	1.000	441.5 Da LogP 3.23 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@]12C[C@@]34C=CC(=O)[C@@](C)(CCC(=O)Nc5c(O)c…`
ZINC29050858 ZINC	1.000	425.5 Da LogP 4.02 TPSA 123.9	✓ Ro5	✓ Clean	`C=C1C[C@@]23C=CC(=O)[C@@](C)(CCC(=O)Nc4c(O)ccc(…`
ZINC138457918 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCC(=O)O`
ZINC138458029 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCC(=O)O`
ZINC144395054 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCC(=O)O`
ZINC14619628 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCCCC(=O)O`
ZINC196749828 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCC(=O)O`
ZINC2113934076 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCC(=O)O`
ZINC2113934082 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCC(=O)O`
ZINC2113934083 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCC(=O)O`
ZINC2243670 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCC(=O)O`
ZINC2569203 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCC(=O)O`
ZINC4798470 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC5973005 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCC(=O)O`
ZINC71418182 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)CCCCC(=O)O`
ZINC79244776 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCCC(=O)O`
ZINC86037082 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC86037089 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCCCC(=O)O`
ZINC86039283 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCC(=O)O`
ZINC3160730 ZINC	0.810	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCC(=O)O`
ZINC4582907 ZINC	0.810	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCC(=O)O`
ZINC4727003 ZINC	0.810	312.4 Da LogP 4.69 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCC(=O)CCCCCCCC(=O)O`
ZINC86037074 ZINC	0.810	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)CCCC(=O)O`
ZINC2378801 ZINC	0.800	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCC(=O)O`
ZINC1429482 ZINC	0.771	291.7 Da LogP 3.00 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1ccc(Cl)cc1`
ZINC1429492 ZINC	0.771	271.3 Da LogP 2.65 TPSA 86.6	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)Nc2cccc(C(=O)O)c2O)cc1`
ZINC1432221 ZINC	0.771	275.2 Da LogP 2.48 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1ccc(F)cc1`
ZINC2113934081 ZINC	0.762	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCCCCCC(=O)O`
ZINC2243668 ZINC	0.762	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCC(=O)O`
ZINC2378799 ZINC	0.762	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCC(=O)O`
ZINC33820423 ZINC	0.762	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCCCC(=O)O`
ZINC1429473 ZINC	0.750	313.4 Da LogP 3.64 TPSA 86.6	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C(=O)Nc2cccc(C(=O)O)c2O)cc1`
ZINC97718 ZINC	0.742	241.2 Da LogP 2.64 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1C(=O)O)c1ccccc1`
ZINC2387442 ZINC	0.739	246.4 Da LogP 4.34 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCSCCCCC(=O)O`
ZINC31778284 ZINC	0.739	310.4 Da LogP 4.47 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)/C=C\C(=O)CCCCCCCC(=O)O`
ZINC5540108 ZINC	0.739	310.4 Da LogP 4.47 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)/C=C/C(=O)CCCCCCCC(=O)O`
ZINC64633397 ZINC	0.739	226.4 Da LogP 4.55 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC(=O)O`
ZINC1429487 ZINC	0.730	336.1 Da LogP 3.11 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1cccc(Br)c1`
ZINC1432220 ZINC	0.730	275.2 Da LogP 2.48 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1cccc(F)c1`
ZINC59545317 ZINC	0.727	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCC(=O)O`
ZINC59545320 ZINC	0.727	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)CCC(=O)O`
ZINC59545336 ZINC	0.727	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCC(=O)O`
ZINC104125601 ZINC	0.722	271.3 Da LogP 2.43 TPSA 75.6	✓ Ro5	✓ Clean	`COC(=O)c1cccc(NC(=O)c2ccccc2)c1O`
ZINC4593317 ZINC	0.714	291.7 Da LogP 3.00 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1ccccc1Cl`

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.