Protein target profile

KP13_01032

3-oxoacyl-[acyl-carrier-protein] synthase 1

Genome: KpKP13 Gene: fabB AHE43440.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GR90

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Length 406

Pocket druggability 0.588

Direct ligand evidence 0 67 total records

Functional annotation 1 EC 4 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.59. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.74. 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 (%): 33.81 Lower values reduce human off-target concern.
Human E-value: 4.69e-62
Gut microbiome similarity: 4.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 97.27 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: 97.66 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 0.588

Structure A0A0H3GR90

Pocket Pocket 11

P2Rank 0.742

Structure A0A0H3GR90

Pocket Pocket 1

ColabFold model

FPocket 0.777 · Pocket 1

P2Rank 0.832 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 199 / 4744 genomes with a hit

Prevalence 4.2%

Cross-references

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

Sequence

UniProt A0A0H3GR90

Sequence

Primary amino-acid sequence viewer.

MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAYLSMEQAVADAGLAPEAYQNNPRVGLIAGSGGGSPKFQVFGADAMRSPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDANRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMQMAMHGVDTPIDYLNSHGTSTPVGDVKELGAIREVFGDNSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINVEELDEQAAGLNIVTKPTDAKLTTVMSNSFGFGGTNATLVMRKYNA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

2.3.1.41

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: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.

29 records

Show feature table

Start	End	DB	Term	Name
254	361	Pfam	PF02801	Beta-ketoacyl synthase, C-terminal domain
254	361	InterPro	IPR014031	Beta-ketoacyl synthase, C-terminal
1	253	SUPERFAMILY	SSF53901	Thiolase-like
1	253	InterPro	IPR016039	Thiolase-like
6	259	Gene3D	G3DSA:3.40.47.10	-
6	259	InterPro	IPR016039	Thiolase-like
25	406	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	403	ProSiteProfiles	PS52004	Ketosynthase family 3 (KS3) domain profile.
1	403	InterPro	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
215	404	SUPERFAMILY	SSF53901	Thiolase-like
215	404	InterPro	IPR016039	Thiolase-like
154	170	ProSitePatterns	PS00606	Ketosynthase family 3 (KS3) active site signature.
154	170	InterPro	IPR018201	Beta-ketoacyl synthase, active site
16	24	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
260	405	FunFam	G3DSA:3.40.47.10:FF:000005	3-oxoacyl-[acyl-carrier-protein] synthase I
4	406	SMART	SM00825	Beta-ketoacyl synthase
4	406	InterPro	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain
6	259	FunFam	G3DSA:3.40.47.10:FF:000006	3-oxoacyl-[acyl-carrier-protein] synthase I
1	24	Phobius	SIGNAL_PEPTIDE	Signal peptide region
2	404	PANTHER	PTHR11712	POLYKETIDE SYNTHASE-RELATED
2	404	InterPro	IPR000794	Beta-ketoacyl synthase
3	246	Pfam	PF00109	Beta-ketoacyl synthase, N-terminal domain
3	246	InterPro	IPR014030	Beta-ketoacyl synthase, N-terminal
4	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
260	406	Gene3D	G3DSA:3.40.47.10	-
260	406	InterPro	IPR016039	Thiolase-like
2	401	CDD	cd00834	KAS_I_II
2	401	InterPro	IPR000794	Beta-ketoacyl synthase

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 #11

0.588

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Surrounding area

Site 2 FPocket #1

0.466

Likely same site as P2Rank 1 0.8 Å 17 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

0.742

Likely same site as FPocket 1 0.8 Å 17 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.523

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Surrounding area

Site 3 P2Rank #3

0.031

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Surrounding area

Site 4 P2Rank #4

0.004

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Surrounding area

Site 5 P2Rank #5

0.003

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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

0.832

Likely same site as FPocket 1 1.9 Å 20 shared residues 87% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.478

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Surrounding area

Site 3 P2Rank #3

0.027

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Surrounding area

Site 4 P2Rank #4

0.014

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Surrounding area

Site 5 P2Rank #5

0.005

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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_A0A0H3GR90	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01032	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.

67 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 17 records from similar proteins

Structural ligands 17 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

07K PDB via homolog 158.2 Da · LogP 2.13 · TPSA 38.9 Open detail RCSB PDB

07L PDB via homolog Detail RCSB PDB

1LR PDB via homolog Detail RCSB PDB

1X9 PDB via homolog Detail RCSB PDB

1XG 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
07K RCSB PDB	3U0E	Q2YQQ9	158.2 Da LogP 2.13 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1cccc2c1nccc2N`
07L RCSB PDB	3U0F	Q2YQQ9	162.1 Da LogP 1.50 TPSA 50.4	✓ Ro5	✓ Clean	`c1cc2c(cc1O)OC(=O)C=C2`
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`
3MQ RCSB PDB	3MQD	Q2YQQ9	181.2 Da LogP 1.90 TPSA 46.3	✓ Ro5	✓ Clean	`c1cc(sc1)c2cc(no2)CO`
6W5 RCSB PDB	5KOF	P0A953	395.3 Da LogP -1.59 TPSA 174.3	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)O)[C@@H](C(=O)NCCC(=O)NCCNC(=O)…`
CER RCSB PDB	1FJ8	P0A953	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	1EK4	P0A953	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
DKA RCSB PDB	1F91	P0A953	172.3 Da LogP 3.21 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)O`
MRJ RCSB PDB	6OKC	P0A953	523.6 Da LogP 2.14 TPSA 174.3	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(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…`
NH4 RCSB PDB	2BUH	P0A953	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
OCA RCSB PDB	2BUI	P0A953	144.2 Da LogP 2.43 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCC(=O)O`
TL5 RCSB PDB	2AQ7	P0A953	224.3 Da LogP 3.37 TPSA 37.3	✓ Ro5	✓ Clean	`C\C=C\C(=C\[C@@]1(C(=C(C(=O)S1)C)O)C)\C`
TL6 RCSB PDB	2AQB	P0A953	196.3 Da LogP 2.59 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C([C@@](SC1=O)(C)\C=C\C=C)O`
TLM RCSB PDB	1FJ4	P0A953	210.3 Da LogP 2.98 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C([C@@](SC1=O)(C)\C=C(/C)\C=C)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
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`
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(…`
ZINC4099011 ZINC	1.000	210.3 Da LogP 2.98 TPSA 37.3	✓ Ro5	✓ Clean	`C=C/C(C)=C/[C@@]1(C)SC(=O)C(C)=C1O`
ZINC53021620 ZINC	1.000	210.3 Da LogP 2.98 TPSA 37.3	✓ Ro5	✓ Clean	`C=C/C(C)=C/[C@]1(C)SC(=O)C(C)=C1O`
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`
ZINC1429477 ZINC	0.711	287.3 Da LogP 2.35 TPSA 95.9	✓ Ro5	✓ Clean	`COc1ccc(C(=O)Nc2cccc(C(=O)O)c2O)cc1`

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.