Protein target profile

KP13_05561

Phosphoglycerate transport system sensor protein pgtB

Genome: KpKP13 Gene: AHE44567.1 pgtB 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTK9

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Length 664

Pocket druggability 0.967

Direct ligand evidence 0 53 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 0.97, P2Rank 0.87). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. 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 0.87. 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: No hit
Gut microbiome similarity: 0.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 83.02 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 0.967

Structure A0A0H3GTK9

Pocket Pocket 59

P2Rank 0.87

Structure A0A0H3GTK9

Pocket Pocket 1

ColabFold model

FPocket 0.708 · Pocket 54

P2Rank 0.939 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 24 / 4744 genomes with a hit

Prevalence 0.5%

Cross-references

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

Sequence

UniProt A0A0H3GTK9

Sequence

Primary amino-acid sequence viewer.

MLQRLRQISISSSLRGAFLTGALLTLIVSSVSLYSWHEQSSQIRYSLDEYFPRIHAAFLIEGNLNLVVDQLNEFLLAPNTTVRLQLRNQIIQHLDKIERLSQGLSPAERQQLGVILQDSRALLAELDRVLYNMFLVREKVGELAARIDWLHDDFTTELNSLVQDFTWQQGTLLDQIEARQGDARQYLKRAREVQNEQQQVYTLARIENQIVDDLRDRLNELKSGNDDGMLVETHIRYLENLKKTADENIRALDDWPSTITLRQTIDELLEIGMVKNNMPDTMRDYVSAQKALVEASRSREATLGRFRTLLEAQLGSSHQQMQMFNQRMAQIVRVSGGLILVATLLALLLAWGLNHYFIRSRLVKRFSALNQAVVQIGLGRTEATIPVYGRDELGRIAGLLRHTLGQLNAQKQQLEQEIGERKAIEADLRATQDELIQTAKLAVVGQTMTTLAHEINQPLNALSMYLFTAGRAIEQGQAEQARMTLSKAEGLINRIDAIIRSLRQFTRRAELETPLHPVDLRQTFTVAWELLAMRHKPQQGTLVIPDDTVWIQGDEVRVHQVLVNVLSNALDACPHAAQITVSWQIQGGRLCVLIADNGPGWPAALLPSLLKPFTTSKTVGLGIGLSICVSLMTQMEGALRLASTFTRSACVVLEFNLTDVKDVE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

2.7.13.3

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0000155 Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response.
GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

41 records

Show feature table

Start	End	DB	Term	Name
419	506	Gene3D	G3DSA:1.10.287.130	-
1	403	PIRSF	PIRSF037119	HK_PgtB
1	403	InterPro	IPR017116	Signal transduction histidine kinase, PgtB
398	661	PIRSF	PIRSF037119	HK_PgtB
398	661	InterPro	IPR017116	Signal transduction histidine kinase, PgtB
439	507	SUPERFAMILY	SSF47384	Homodimeric domain of signal transducing histidine kinase
439	507	InterPro	IPR036097	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
553	659	SMART	SM00387	HKATPase_4
553	659	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
558	655	CDD	cd00075	HATPase
510	655	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
510	655	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
29	33	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
360	412	ProSiteProfiles	PS50885	HAMP domain profile.
360	412	InterPro	IPR003660	HAMP domain
1	16	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
15	37	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
441	507	CDD	cd00082	HisKA
441	507	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
553	657	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
553	657	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
317	418	Gene3D	G3DSA:6.10.340.10	-
360	412	SMART	SM00304	HAMP_11
445	508	Pfam	PF00512	His Kinase A (phospho-acceptor) domain
445	508	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
34	333	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
357	408	Pfam	PF00672	HAMP domain
357	408	InterPro	IPR003660	HAMP domain
331	353	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
17	28	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
397	434	Coils	Coil	Coil
107	647	PANTHER	PTHR43065	SENSOR HISTIDINE KINASE
1	33	Phobius	SIGNAL_PEPTIDE	Signal peptide region
443	511	SMART	SM00388	HisKA_10
443	511	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
515	662	Gene3D	G3DSA:3.30.565.10	-
515	662	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
334	357	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
358	664	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
450	659	ProSiteProfiles	PS50109	Histidine kinase domain profile.
450	659	InterPro	IPR005467	Histidine kinase domain

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 #59

0.967

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Surrounding area

Site 2 FPocket #32

0.305

Likely same site as P2Rank 3 2.2 Å 7 shared residues 100% 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

0.87

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Surrounding area

Site 2 P2Rank #2

0.073

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Surrounding area

Site 3 P2Rank #3

0.056

Likely same site as FPocket 32 2.2 Å 7 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.031

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Surrounding area

Site 5 P2Rank #5

0.014

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #54

0.708

Likely same site as P2Rank 1 3.7 Å 40 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #45

0.545

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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

0.939

Likely same site as FPocket 54 3.7 Å 40 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.019

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Surrounding area

Site 3 P2Rank #3

0.018

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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_A0A0H3GTK9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05561	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

EMC PDB via homolog 229.7 Da · LogP 0.97 · TPSA 0.0 Open detail RCSB PDB

EMT PDB via homolog Detail RCSB PDB

PG0 PDB via homolog Detail RCSB PDB

ZINC1580161 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC16052118 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
EMC RCSB PDB	3A0W	Q9X180	229.7 Da LogP 0.97 TPSA 0.0	✓ Ro5	✓ Clean	`CC[Hg+]`
EMT RCSB PDB	3A0W	Q9X180	382.8 Da LogP 2.91 TPSA 37.3	✓ Ro5	✓ Clean	`CC[Hg]Sc1ccccc1C(=O)O`
PG0 RCSB PDB	5UKV	P71815	120.1 Da LogP -0.36 TPSA 38.7	✓ Ro5	✓ Clean	`COCCOCCO`

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
ZINC1580161 ZINC	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059 ZINC	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860 ZINC	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC575419714 ZINC	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC115163232 ZINC	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC258837490 ZINC	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC12501520 ZINC	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1692489 ZINC	0.688	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC3874716 ZINC	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC4530388 ZINC	0.688	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5178829 ZINC	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5701172 ZINC	0.688	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	0.688	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC575432150 ZINC	0.667	344.4 Da LogP -0.89 TPSA 100.5	✓ Ro5	✓ Clean	`COCCOCCOCCS(=O)(=O)CCOCCOCCO`
ZINC1857524240 ZINC	0.652	207.3 Da LogP -0.75 TPSA 60.0	✓ Ro5	✓ Clean	`COCCNCCOCCOCCO`
ZINC5650743 ZINC	0.600	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.600	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC116078641 ZINC	0.583	222.2 Da LogP -0.80 TPSA 74.2	✓ Ro5	✓ Clean	`COC(=O)COCCOCCOCCO`
ZINC1857790631 ZINC	0.583	280.3 Da LogP -0.39 TPSA 83.5	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCOCCO`
ZINC196151418 ZINC	0.583	266.3 Da LogP -0.78 TPSA 83.5	✓ Ro5	✓ Clean	`COC(=O)COCCOCCOCCOCCO`
ZINC202958272 ZINC	0.583	236.3 Da LogP -0.41 TPSA 74.2	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCO`
ZINC34111591 ZINC	0.583	207.3 Da LogP -1.06 TPSA 62.2	✓ Ro5	✓ Clean	`COCCOCCN(CCO)CCO`
ZINC642881862 ZINC	0.583	324.4 Da LogP -0.38 TPSA 92.7	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCOCCOCCO`
ZINC34764844 ZINC	0.550	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC5369059 ZINC	0.548	274.3 Da LogP 3.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Sc1ccccc1C(=O)O`
ZINC1644613 ZINC	0.545	206.3 Da LogP 0.83 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCO`
ZINC1672344 ZINC	0.545	230.3 Da LogP 3.54 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Sc1ccccc1`
ZINC2675142 ZINC	0.545	334.4 Da LogP 3.97 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1SCCSc1ccccc1C(=O)O`
ZINC2383745924 ZINC	0.542	398.5 Da LogP -0.01 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCC(CO)COCCOCCOCCOC`
ZINC5059317 ZINC	0.541	240.3 Da LogP 2.34 TPSA 74.6	✓ Ro5	✓ Clean	`CC[C@H](Sc1ccccc1C(=O)O)C(=O)O`
ZINC5059320 ZINC	0.541	240.3 Da LogP 2.34 TPSA 74.6	✓ Ro5	✓ Clean	`CC[C@@H](Sc1ccccc1C(=O)O)C(=O)O`
ZINC7262012 ZINC	0.541	210.3 Da LogP 3.28 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCSc1ccccc1C(=O)O`
ZINC3122032 ZINC	0.529	256.2 Da LogP 1.01 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1SC(C(=O)O)C(=O)O`
ZINC2584162 ZINC	0.528	210.3 Da LogP 3.13 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CSc1ccccc1C(=O)O`
ZINC3375023 ZINC	0.528	210.3 Da LogP 2.07 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CSc1ccccc1C(=O)O`
ZINC19263534 ZINC	0.526	224.3 Da LogP 3.67 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCSc1ccccc1C(=O)O`
ZINC115086873 ZINC	0.524	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC140264883 ZINC	0.524	223.3 Da LogP -0.43 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCON`
ZINC146143823 ZINC	0.524	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC5024003 ZINC	0.524	251.3 Da LogP -0.34 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCN`
ZINC83253927 ZINC	0.524	400.5 Da LogP 0.68 TPSA 73.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC83253930 ZINC	0.524	224.3 Da LogP 0.61 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCS`
ZINC90741447 ZINC	0.524	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`

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.