Protein target profile

KP13_05384

Catalase HPII

Genome: KpKP13 Gene: katE AHE45029.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GVY8

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Length 752

Pocket druggability 0.972

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 6 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 0.97, P2Rank 0.93). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.97. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.93. 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 (%): 41.016 Lower values reduce human off-target concern.
Human E-value: 1.41e-114
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 80.851 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: 97.05 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 0.972

Structure A0A0H3GVY8

Pocket Pocket 1

P2Rank 0.934

Structure A0A0H3GVY8

Pocket Pocket 1

ColabFold model

FPocket 0.953 · Pocket 1

P2Rank 0.969 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 140 / 4744 genomes with a hit

Prevalence 3.0%

Cross-references

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

Sequence

UniProt A0A0H3GVY8

Sequence

Primary amino-acid sequence viewer.

MSDKHPNPHQQQAPVHDSEEAQPGLDSLAPDDREWRPTPKPTAPGVEPTAPGSLKAPDTHNSKLDSLEAQRKGGEDFPLTTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLAALTKADFLSSADKITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTDEGIFDLVGNNTPVFFIQDAMKFPDFVHAVKPEPHWAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDFHRRDLWEAIEAGDYPEFELGLQLIPEENEFAFDFDLLDPTKLIPEALVPVQRVGRMVLNRNPDNFFAENEQAAFHPGHIVPGIDFSNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMDIDTNPANYEPNSINDNWPRETPPAAKRGGFESLAERVDGEKIRQRSPSFGEYYAQPRLFWLSQTPIEQQHIIDGFSFELSKVVRTWIRERVVDHLAHIDTKLAEAVGANLGIELSDDQRNITLPAPVNGVEKDPSLSLYADAEGDVKGRVVAVLLNERTSAQDLVQLLQALQAQGVHSKLLYSRMGEVIADDGSPLPIAGTFAGSPSLTVDAVVVPGGDLSALSQSGDARYYLLEAYKHLKPILLAGDARQLTSVLHVPTQGEEGVIVTDALDTPAADKLLALMTAHRVWSRSPKIAAIPA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1.11.1.6

Gene Ontology (GO)

GO:0004096 Catalysis of the reaction: 2 H2O2 = O2 + 2 H2O.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046872 Binding to a metal ion.
GO:0042744 The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

46 records

Show feature table

Start	End	DB	Term	Name
599	739	CDD	cd03132	GATase1_catalase
599	739	InterPro	IPR041399	Large catalase, C-terminal domain
410	418	ProSitePatterns	PS00437	Catalase proximal heme-ligand signature.
410	418	InterPro	IPR002226	Catalase haem-binding site
41	492	FunFam	G3DSA:2.40.180.10:FF:000003	Catalase
1	82	MobiDBLite	mobidb-lite	consensus disorder prediction
156	174	PRINTS	PR00067	Catalase signature
156	174	InterPro	IPR018028	Catalase, mono-functional, haem-containing
397	423	PRINTS	PR00067	Catalase signature
397	423	InterPro	IPR018028	Catalase, mono-functional, haem-containing
177	194	PRINTS	PR00067	Catalase signature
177	194	InterPro	IPR018028	Catalase, mono-functional, haem-containing
196	214	PRINTS	PR00067	Catalase signature
196	214	InterPro	IPR018028	Catalase, mono-functional, haem-containing
93	116	PRINTS	PR00067	Catalase signature
93	116	InterPro	IPR018028	Catalase, mono-functional, haem-containing
365	392	PRINTS	PR00067	Catalase signature
365	392	InterPro	IPR018028	Catalase, mono-functional, haem-containing
599	752	Gene3D	G3DSA:3.40.50.880	-
599	752	InterPro	IPR029062	Class I glutamine amidotransferase-like
495	598	Gene3D	G3DSA:1.20.1370.20	-
495	598	InterPro	IPR043156	Catalase, mono-functional, haem-containing, clade 2, helical domain
80	465	Pfam	PF00199	Catalase
80	465	InterPro	IPR011614	Catalase core domain
117	561	CDD	cd08155	catalase_clade_2
1	17	MobiDBLite	mobidb-lite	consensus disorder prediction
2	492	Gene3D	G3DSA:2.40.180.10	Catalase core domain
43	750	PIRSF	PIRSF038927	Catalase_clade2
43	750	InterPro	IPR024712	Catalase, mono-functional, haem-containing, clade 2
598	703	SUPERFAMILY	SSF52317	Class I glutamine amidotransferase-like
598	703	InterPro	IPR029062	Class I glutamine amidotransferase-like
116	132	ProSitePatterns	PS00438	Catalase proximal active site signature.
116	132	InterPro	IPR024708	Catalase active site
598	745	Pfam	PF18011	C-terminal domain found in long catalases
598	745	InterPro	IPR041399	Large catalase, C-terminal domain
76	567	ProSiteProfiles	PS51402	catalase family profile.
76	567	InterPro	IPR018028	Catalase, mono-functional, haem-containing
493	596	FunFam	G3DSA:1.20.1370.20:FF:000001	Catalase HPII
498	561	Pfam	PF06628	Catalase-related immune-responsive
498	561	InterPro	IPR010582	Catalase immune-responsive domain
46	582	SUPERFAMILY	SSF56634	Heme-dependent catalase-like
46	582	InterPro	IPR020835	Catalase superfamily
80	468	SMART	SM01060	Catalase_2
80	468	InterPro	IPR011614	Catalase core domain
45	747	PANTHER	PTHR42821	CATALASE
45	747	InterPro	IPR024712	Catalase, mono-functional, haem-containing, clade 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

0.972

Likely same site as P2Rank 1 0.6 Å 22 shared residues 85% 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

0.934

Likely same site as FPocket 1 0.6 Å 22 shared residues 85% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.445

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Surrounding area

Site 3 P2Rank #3

0.408

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Surrounding area

Site 4 P2Rank #4

0.134

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Surrounding area

Site 5 P2Rank #5

0.103

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Surrounding area

Residue sets

UniProt: Active site:127-127

UniProt: Active site:200-200

UniProt: Binding site:124-124

UniProt: Binding site:164-164

UniProt: Binding site:213-213

UniProt: Binding site:410-410

UniProt: Binding site:414-414 axial binding residue

UniProt: Binding site:421-421

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.969

Likely same site as FPocket 1 1.0 Å 26 shared residues 87% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.476

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Surrounding area

Site 3 P2Rank #3

0.355

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Surrounding area

Site 4 P2Rank #4

0.329

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Surrounding area

Site 5 P2Rank #5

0.136

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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_A0A0H3GVY8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05384	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

3TR PDB via homolog 84.1 Da · LogP -0.61 · TPSA 67.6 Open detail RCSB PDB

AE3 PDB via homolog Detail RCSB PDB

H2S PDB via homolog Detail RCSB PDB

HDD PDB via homolog Detail RCSB PDB

HDE 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
3TR RCSB PDB	4B7A	M4GGR5	84.1 Da LogP -0.61 TPSA 67.6	✓ Ro5	✓ Clean	`c1[nH]nc(n1)N`
AE3 RCSB PDB	3ZJ5	Q9C169	134.2 Da LogP 0.03 TPSA 38.7	✓ Ro5	✓ Clean	`CCOCCOCCO`
H2S RCSB PDB	3P9Q	P21179	34.1 Da LogP 0.11 TPSA 0.0	✓ Ro5	✓ Clean	`S`
HDD RCSB PDB	4AUE	M4GGR5	632.5 Da LogP 3.21 TPSA 101.9	1 viol.	✓ Clean	`Cc1c2n3c(c1CCC(=O)O)C=C4[C@]5(CCC(=O)O5)[C@@](C…`
HDE RCSB PDB	3P9Q	P21179	638.5 Da LogP 4.58 TPSA 101.9	1 viol.	✓ Clean	`CCc1c(c2n3c1Cc4c(c(c5n4[Fe]36n7c(c(c(c7C=C8N6C(…`
O RCSB PDB	6NSW	Q9C169	18.0 Da LogP -0.82 TPSA 31.5	✓ Ro5	✓ Clean	`O`
PEO RCSB PDB	1GGF	P21179	34.0 Da LogP 0.02 TPSA 40.5	✓ Ro5	✓ Clean	`OO`
TAR RCSB PDB	3ZJ5	Q9C169	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@@H](C(=O)O)O)(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
ZINC12501520 ZINC	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716 ZINC	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC115086873 ZINC	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264 ZINC	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823 ZINC	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1542984442 ZINC	0.688	413.5 Da LogP -0.93 TPSA 120.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1565503710 ZINC	0.688	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792028 ZINC	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057 ZINC	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC230494776 ZINC	0.688	325.4 Da LogP -0.96 TPSA 101.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38917157 ZINC	0.688	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5650743 ZINC	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182 ZINC	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC83253921 ZINC	0.688	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC90741446 ZINC	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447 ZINC	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`
ZINC144169243 ZINC	0.647	281.3 Da LogP -1.37 TPSA 89.4	✓ Ro5	✓ Clean	`OCCOCCOCCNCCOCCOCCO`
ZINC205758716 ZINC	0.647	457.6 Da LogP -1.31 TPSA 126.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCNCCOCCOCCOCCOCCO`
ZINC575441396 ZINC	0.647	369.5 Da LogP -1.34 TPSA 107.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCNCCOCCOCCOCCO`
ZINC1644613 ZINC	0.611	206.3 Da LogP 0.83 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCO`
ZINC258839852 ZINC	0.611	276.3 Da LogP 0.61 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCC(F)(F)F`
ZINC167715346 ZINC	0.600	266.3 Da LogP -0.18 TPSA 77.4	✓ Ro5	✓ Clean	`OCCCOCCOCCOCCOCCCO`
ZINC34160867 ZINC	0.600	222.3 Da LogP -0.20 TPSA 68.2	✓ Ro5	✓ Clean	`OCCCOCCOCCOCCCO`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC1580159 ZINC	0.588	210.3 Da LogP -0.26 TPSA 58.9	✓ Ro5	✓ Clean	`OCCOCCSCCOCCO`
ZINC39267847 ZINC	0.579	208.2 Da LogP -0.89 TPSA 85.2	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCO`
ZINC4974293 ZINC	0.579	280.4 Da LogP 1.08 TPSA 55.4	✓ Ro5	✓ Clean	`CCOCCOCCOCOCCOCCOCC`
ZINC725239375 ZINC	0.579	310.3 Da LogP -0.46 TPSA 103.7	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCO`

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.