Protein target profile

KP13_03439

Serine 3-dehydrogenase

Genome: KpKP13 Gene: AHE45815.1 sdh 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTM0

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Length 248

Pocket druggability 0.918

Direct ligand evidence 0 64 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

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.92, P2Rank 0.96). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.92. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.96. 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 (%): 43.478 Lower values reduce human off-target concern.
Human E-value: 7.57e-06
Gut microbiome similarity: 2.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 49.194 Higher values support similarity to known essential genes.
DEG E-value: 1.19e-83 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 98.28 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 0.918

Structure A0A0H3GTM0

Pocket Pocket 5

P2Rank 0.959

Structure A0A0H3GTM0

Pocket Pocket 1

ColabFold model

FPocket 0.417 · Pocket 1

P2Rank 0.962 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 97 / 4744 genomes with a hit

Prevalence 2.0%

Cross-references

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

Sequence

UniProt A0A0H3GTM0

Chemistry

ChEMBL CHEMBL456414 ChEMBL CHEMBL456619 ChEMBL CHEMBL456844 ChEMBL CHEMBL456845 ChEMBL CHEMBL459574 ChEMBL CHEMBL461471 ChEMBL CHEMBL514876 ChEMBL CHEMBL517425

Sequence

Primary amino-acid sequence viewer.

MFITGATSGFGEAAAQVFADAGWSLVLSGRRYPRLKALQDRLAARVPVHIIELDVRDSEAVAAAVASLPAPFADVTTLINNAGLALSPLPAQEVALEDWKTMIDTNVTGLVTMTHALLPTLIRHGAGASIINIGSIAGQWPYPGSHVYGASKAFVKQFSYNLRCDLLGTGVRVTDLAPGIAETEFTLVRTKGDQAASDKLYRGTTPLSAHDIAEQMFYIATLPAHMNINRVEVMPVRQAWQPFAIDRD

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: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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
2	241	PANTHER	PTHR42901	ALCOHOL DEHYDROGENASE
148	167	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
148	167	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
73	84	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
73	84	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
128	136	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
128	136	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
2	186	Pfam	PF00106	short chain dehydrogenase
2	186	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
135	163	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
135	163	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
1	238	FunFam	G3DSA:3.40.50.720:FF:000047	NADP-dependent L-serine/L-allo-threonine dehydrogenase
1	248	Gene3D	G3DSA:3.40.50.720	-
148	167	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
73	84	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
169	186	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
169	186	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
122	138	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
122	138	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
2	229	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
2	229	InterPro	IPR036291	NAD(P)-binding 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 #5

0.918

Likely same site as P2Rank 1 1.9 Å 39 shared residues 91% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.959

Likely same site as FPocket 5 1.9 Å 39 shared residues 91% of smaller site

Show in viewer

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_A0A0H3GTM0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03439	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.

64 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 14 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 8 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

8X3 PDB via homolog 126.1 Da · LogP -1.13 · TPSA 74.6 Open detail RCSB PDB

AC0 PDB via homolog Detail RCSB PDB

ADE PDB via homolog Detail RCSB PDB

P4C PDB via homolog Detail RCSB PDB

SS2 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
8X3 RCSB PDB	6IXJ	D3U1D9	126.1 Da LogP -1.13 TPSA 74.6	✓ Ro5	✓ Clean	`C(CS(=O)(=O)O)O`
AC0 RCSB PDB	1ZK1	Q84EX5	120.2 Da LogP 1.89 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccccc1`
ADE RCSB PDB	1YXM	Q9BY49	135.1 Da LogP -0.06 TPSA 80.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(ncn2)N`
P4C RCSB PDB	3EZL	Q3JRS9	324.4 Da LogP -0.72 TPSA 92.7	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCC=O)O`
SS2 RCSB PDB	1ZJY	Q84EX5	122.2 Da LogP 1.74 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@H](c1ccccc1)O`
TNE RCSB PDB	1XHL	Q19774	139.2 Da LogP 0.81 TPSA 20.3	✓ Ro5	✓ Clean	`CN1[C@H]2CC[C@@H]1CC(=O)C2`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL456414 ChEMBL	Q9BPW9	—	358.5 Da LogP 4.67 TPSA 63.6	✓ Ro5	Alert	`C=C1CC[C@@H]2C(C)(C)CCC[C@@]2(C)[C@@H]1CC1=C(O)…`
CHEMBL456619 ChEMBL	Q9BPW9	—	344.5 Da LogP 5.75 TPSA 49.7	1 viol.	Alert	`COc1ccc(O)c(O)c1/C=C1\[C@@H](C)CC[C@H]2C(C)(C)C…`
CHEMBL456844 ChEMBL	Q9BPW9	—	340.5 Da LogP 5.07 TPSA 35.5	1 viol.	✓ Clean	`CC1=CC[C@H]2C(C)(C)CCC[C@]2(C)[C@H]1/C=C1\C=C2O…`
CHEMBL456845 ChEMBL	Q9BPW9	—	384.5 Da LogP 5.58 TPSA 44.8	1 viol.	✓ Clean	`COc1c(C[C@H]2C(C)=CC[C@H]3C(C)(C)CCC[C@]23C)cc2…`
CHEMBL459574 ChEMBL	Q9BPW9	—	312.5 Da LogP 4.81 TPSA 34.1	✓ Ro5	Alert	`CC1=CC[C@@H]2C(C)(C)CCC[C@@]2(C)[C@@H]1CC1=CC(=…`
CHEMBL461471 ChEMBL	Q9BPW9	—	314.5 Da LogP 5.44 TPSA 40.5	1 viol.	✓ Clean	`C=C1CC[C@@H]2C(C)(C)CCC[C@@]2(C)[C@@H]1Cc1cc(O)…`
CHEMBL514876 ChEMBL	Q9BPW9	—	358.5 Da LogP 4.67 TPSA 63.6	✓ Ro5	Alert	`COC1=CC(=O)C(O)=C(/C=C2\[C@@H](C)CC[C@H]3C(C)(C…`
CHEMBL517425 ChEMBL	Q9BPW9	—	372.5 Da LogP 4.90 TPSA 52.6	✓ Ro5	Alert	`COC1=CC(=O)C(=O)C(C[C@@]2(C)C3=C(CC[C@@H]2C)C(C…`

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
ZINC3200262 ZINC	0.842	252.3 Da LogP 2.95 TPSA 51.2	✓ Ro5	Alert	`CC(=O)c1ccc(C(=O)C(=O)c2ccccc2)cc1`
ZINC36456728 ZINC	0.800	224.3 Da LogP 3.12 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C(=O)c2ccccc2)cc1`
ZINC1039926 ZINC	0.625	220.3 Da LogP 3.29 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C#Cc2ccccc2)cc1`
ZINC143028 ZINC	0.625	228.3 Da LogP 4.04 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(Sc2ccccc2)cc1`
ZINC1440490 ZINC	0.625	222.3 Da LogP 4.06 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(/C=C/c2ccccc2)cc1`
ZINC14981993 ZINC	0.625	224.3 Da LogP 3.12 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1cccc(C(=O)c2ccccc2)c1`
ZINC1562037 ZINC	0.625	210.3 Da LogP 3.48 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(Cc2ccccc2)cc1`
ZINC1675845 ZINC	0.625	230.3 Da LogP 3.89 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@@H](O)c1ccc(Sc2ccccc2)cc1`
ZINC1675948 ZINC	0.625	226.3 Da LogP 3.33 TPSA 41.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(NNc2ccccc2)cc1`
ZINC1732765 ZINC	0.625	246.3 Da LogP -2.20 TPSA 108.7	✓ Ro5	✓ Clean	`O=S(=O)(CCO)CCS(=O)(=O)CCO`
ZINC1845686 ZINC	0.625	224.3 Da LogP 3.67 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(CCc2ccccc2)cc1`
ZINC2045615 ZINC	0.625	230.3 Da LogP 3.89 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@H](O)c1ccc(Sc2ccccc2)cc1`
ZINC21999250 ZINC	0.625	211.3 Da LogP 3.63 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(Nc2ccccc2)cc1`
ZINC261810 ZINC	0.625	212.2 Da LogP 3.68 TPSA 26.3	✓ Ro5	✓ Clean	`CC(=O)c1ccc(Oc2ccccc2)cc1`
ZINC35632288 ZINC	0.625	214.3 Da LogP 3.53 TPSA 29.5	✓ Ro5	✓ Clean	`C[C@H](O)c1ccc(Oc2ccccc2)cc1`
ZINC35632289 ZINC	0.625	214.3 Da LogP 3.53 TPSA 29.5	✓ Ro5	✓ Clean	`C[C@@H](O)c1ccc(Oc2ccccc2)cc1`
ZINC4798948 ZINC	0.625	224.3 Da LogP 4.30 TPSA 41.8	✓ Ro5	Alert	`CC(=O)c1ccc(/N=N/c2ccccc2)cc1`
ZINC1765221 ZINC	0.619	212.3 Da LogP 3.20 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@H](O)C(c1ccccc1)c1ccccc1`
ZINC2032454 ZINC	0.619	212.3 Da LogP 3.20 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@@H](O)C(c1ccccc1)c1ccccc1`
ZINC50452 ZINC	0.615	240.3 Da LogP 3.11 TPSA 43.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(OC(=O)c2ccccc2)cc1`
ZINC586797 ZINC	0.615	239.3 Da LogP 3.14 TPSA 46.2	✓ Ro5	✓ Clean	`CC(=O)c1ccc(NC(=O)c2ccccc2)cc1`
ZINC1672966 ZINC	0.611	210.2 Da LogP 2.75 TPSA 34.1	✓ Ro5	Alert	`O=C(C(=O)c1ccccc1)c1ccccc1`
ZINC1401590 ZINC	0.600	244.3 Da LogP 3.06 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc([S@](=O)c2ccccc2)cc1`
ZINC143035 ZINC	0.600	260.3 Da LogP 2.72 TPSA 51.2	✓ Ro5	✓ Clean	`CC(=O)c1ccc(S(=O)(=O)c2ccccc2)cc1`
ZINC34354396 ZINC	0.600	224.3 Da LogP 4.04 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc([C@@H](C)c2ccccc2)cc1`
ZINC34354398 ZINC	0.600	224.3 Da LogP 4.04 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc([C@H](C)c2ccccc2)cc1`
ZINC4073660 ZINC	0.600	244.3 Da LogP 3.06 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc([S@@](=O)c2ccccc2)cc1`
ZINC56557 ZINC	0.600	238.3 Da LogP 3.76 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(-c2ccc(C(C)=O)cc2)cc1`
ZINC1720279 ZINC	0.591	212.3 Da LogP 3.52 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@@H](c1ccccc1)[C@H](O)c1ccccc1`
ZINC1720280 ZINC	0.591	212.3 Da LogP 3.52 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@H](c1ccccc1)[C@H](O)c1ccccc1`
ZINC1720281 ZINC	0.591	212.3 Da LogP 3.52 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@@H](c1ccccc1)[C@@H](O)c1ccccc1`
ZINC1720282 ZINC	0.591	212.3 Da LogP 3.52 TPSA 20.2	✓ Ro5	✓ Clean	`C[C@H](c1ccccc1)[C@@H](O)c1ccccc1`
ZINC141045875 ZINC	0.583	250.3 Da LogP -0.10 TPSA 63.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCC=O`
ZINC15148066 ZINC	0.583	222.4 Da LogP 3.78 TPSA 20.2	✓ Ro5	✓ Clean	`C=C1CC[C@H]2C(C)(C)CCC[C@@]2(C)[C@H]1CO`
ZINC336592 ZINC	0.583	224.3 Da LogP 3.12 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccccc1C(=O)c1ccccc1`
ZINC12359951 ZINC	0.579	214.3 Da LogP 2.45 TPSA 40.5	✓ Ro5	✓ Clean	`O[C@@H](c1ccccc1)[C@H](O)c1ccccc1`
ZINC12501520 ZINC	0.579	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1577122 ZINC	0.579	208.3 Da LogP 4.64 TPSA 0.0	✓ Ro5	✓ Clean	`C/C(=C(/C)c1ccccc1)c1ccccc1`
ZINC1590838 ZINC	0.579	342.4 Da LogP 3.82 TPSA 68.3	✓ Ro5	Alert	`O=C(C(=O)c1ccc(C(=O)C(=O)c2ccccc2)cc1)c1ccccc1`
ZINC16133932 ZINC	0.579	474.5 Da LogP 4.88 TPSA 102.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc(C(=O)C(=O)c2ccc(C(=O)C(=O)c3cccc…`
ZINC1720954 ZINC	0.579	210.3 Da LogP 4.59 TPSA 0.0	✓ Ro5	✓ Clean	`C[C@@H](c1ccccc1)[C@@H](C)c1ccccc1`
ZINC1720957 ZINC	0.579	210.3 Da LogP 4.59 TPSA 0.0	✓ Ro5	✓ Clean	`C[C@H](c1ccccc1)[C@H](C)c1ccccc1`
ZINC3123872 ZINC	0.579	208.3 Da LogP 4.64 TPSA 0.0	✓ Ro5	✓ Clean	`C/C(=C(\C)c1ccccc1)c1ccccc1`
ZINC3874716 ZINC	0.579	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC388745 ZINC	0.579	214.3 Da LogP 2.45 TPSA 40.5	✓ Ro5	✓ Clean	`O[C@@H](c1ccccc1)[C@@H](O)c1ccccc1`
ZINC4283769 ZINC	0.579	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	0.579	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	0.579	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	0.579	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC68564262 ZINC	0.579	210.3 Da LogP 4.59 TPSA 0.0	✓ Ro5	✓ Clean	`C[C@H](c1ccccc1)[C@@H](C)c1ccccc1`

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.