Protein target profile

VK055_2437

membrane-bound PQQ-dependent dehydrogenase, glucose/quinate/shikimate family protein

Genome: KpATCC43816 Gene: AIK81034.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GMQ0

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Length 784

Pocket druggability 1

Direct ligand evidence 0 52 total records

Functional annotation 0 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

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.98. 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: No hit
Gut microbiome similarity: 1.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 90.434 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 94.9 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 1

Structure A0A0H3GMQ0

Pocket Pocket 1

P2Rank 0.977

Structure A0A0H3GMQ0

Pocket Pocket 1

ColabFold model

FPocket 1 · Pocket 1

P2Rank 0.985 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 89 / 4744 genomes with a hit

Prevalence 1.9%

Cross-references

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

Sequence

UniProt A0A0H3GMQ0

Sequence

Primary amino-acid sequence viewer.

MTLTALFAAFCGLYLLIGGAWLVVLGGSWYYPIAGLVMLGVTVMLFRGKRAALWLYAALLLATMIWGVWEVGFDFWALTPRSDILVFFGIWLILPFVWRRLPVPSAGAVGALVVALLISGGMLTWAGFNDPQEVNGTLSADATPAAPISTVADGDWPAYGRNQEGQRFSPLKQINADNVKNLKEAWVFRTGDLKQPNDPGEITNEVTPIKVGDTLFLCTAHQRLFALDAATGKEKWHFDPQLNADPSFQHVTCRGVSYHEAKADNAPADVVADCPRRIILPVNDGRLFAVNADNGKLCETFANKGILNLQTNMPVTTPGMYEPTSPPIITDKTIVIAGAVTDNFSTREPSGVIRGFDVNTGKLLWAFDPGAKDPNAIPSDEHHFTLNSPNSWAPAAYDAKLDLVYLPMGVTTPDIWGGNRTPEQERYASSIVALNATTGKLAWSYQTVHHDLWDMDMPSQPTLADIEVNGKTVPVIYAPAKTGNIFVLDRRNGELVVPAPEKPVPQGAAKGDYVTKTQPFSDLSFRPKKDLTGADMWGATMFDQLVCRVIFHQLRYEGIFTPPSEQGTLVFPGNLGMFEWGGISVDPNRQVAIANPMALPFVSKLIPRGPGNPMEPPKDAKGSGTESGVQPQYGVPYGVTLNPFLSPFGLPCKQPAWGYISALDLKTNEVVWKKRIGTPQDSLPFPMPVKLPFTMGMPMLGGPISTAGNVLFIGATADNYLRAYNMSNGEKLWEARLPAGGQATPMTYEVNGKQYVVISAGGHGSFGTKMGDYIVAYALPNDAK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0016614 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
GO:0048038 Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.
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:0008876 Catalysis of the reaction: D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

56 records

Show feature table

Start	End	DB	Term	Name
129	784	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
53	69	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
75	94	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
149	777	PANTHER	PTHR32303	QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C)
3	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
3	780	NCBIfam	TIGR03074	membrane-bound PQQ-dependent dehydrogenase, glucose/quinate/shikimate family
3	780	InterPro	IPR017511	PQQ-dependent membrane bound dehydrogenase
95	105	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
47	52	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
29	46	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
106	128	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
608	627	MobiDBLite	mobidb-lite	consensus disorder prediction
270	302	SMART	SM00564	ire1_9
270	302	InterPro	IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
389	446	SMART	SM00564	ire1_9
389	446	InterPro	IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
208	239	SMART	SM00564	ire1_9
208	239	InterPro	IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
467	500	SMART	SM00564	ire1_9
467	500	InterPro	IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
327	368	SMART	SM00564	ire1_9
327	368	InterPro	IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
703	736	SMART	SM00564	ire1_9
703	736	InterPro	IPR018391	Pyrrolo-quinoline quinone beta-propeller repeat
28	45	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
84	101	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
52	69	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
156	779	CDD	cd10280	PQQ_mGDH
156	779	InterPro	IPR017511	PQQ-dependent membrane bound dehydrogenase
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
392	413	ProSitePatterns	PS00364	Bacterial quinoprotein dehydrogenases signature 2.
392	413	InterPro	IPR001479	Quinoprotein dehydrogenase, conserved site
149	781	SUPERFAMILY	SSF50998	Quinoprotein alcohol dehydrogenase-like
149	781	InterPro	IPR011047	Quinoprotein alcohol dehydrogenase-like superfamily
143	784	Gene3D	G3DSA:2.140.10.10	-
155	183	ProSitePatterns	PS00363	Bacterial quinoprotein dehydrogenases signature 1.
155	183	InterPro	IPR001479	Quinoprotein dehydrogenase, conserved site
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
16	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
5	24	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
106	128	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
70	74	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
277	308	Pfam	PF01011	PQQ enzyme repeat
277	308	InterPro	IPR002372	Pyrrolo-quinoline quinone repeat
652	684	Pfam	PF01011	PQQ enzyme repeat
652	684	InterPro	IPR002372	Pyrrolo-quinoline quinone repeat
344	376	Pfam	PF01011	PQQ enzyme repeat
344	376	InterPro	IPR002372	Pyrrolo-quinoline quinone repeat
213	248	Pfam	PF01011	PQQ enzyme repeat
213	248	InterPro	IPR002372	Pyrrolo-quinoline quinone repeat
709	745	Pfam	PF01011	PQQ enzyme repeat
709	745	InterPro	IPR002372	Pyrrolo-quinoline quinone repeat
430	456	Pfam	PF01011	PQQ enzyme repeat
430	456	InterPro	IPR002372	Pyrrolo-quinoline quinone repeat
141	782	FunFam	G3DSA:2.140.10.10:FF:000001	Quinoprotein glucose dehydrogenase
20	28	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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

1.0

Likely same site as P2Rank 1 2.1 Å 45 shared residues 92% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #11

0.871

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Surrounding area

Site 3 FPocket #19

0.5

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Surrounding area

Site 4 FPocket #5

0.436

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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

0.977

Likely same site as FPocket 1 2.1 Å 45 shared residues 92% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.569

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Surrounding area

Site 3 P2Rank #3

0.179

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Surrounding area

Site 4 P2Rank #4

0.162

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Surrounding area

Site 5 P2Rank #5

0.068

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #1

1.0

Likely same site as P2Rank 1 1.3 Å 46 shared residues 92% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #4

0.885

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Surrounding area

Site 3 FPocket #20

0.256

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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

0.985

Likely same site as FPocket 1 1.3 Å 46 shared residues 92% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.566

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Surrounding area

Site 3 P2Rank #3

0.202

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Surrounding area

Site 4 P2Rank #4

0.186

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Surrounding area

Site 5 P2Rank #5

0.175

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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_A0A0H3GMQ0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2437	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

15P PDB via homolog 1529.8 Da · LogP 0.17 · TPSA 334.1 Open detail RCSB PDB

TFB PDB via homolog Detail RCSB PDB

ZINC1580161 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC16052118 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC16052257 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
15P RCSB PDB	4MAE	I0JWN7	1529.8 Da LogP 0.17 TPSA 334.1	2 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO…`
TFB RCSB PDB	1KB0	Q46444	116.1 Da LogP 0.25 TPSA 46.5	✓ Ro5	✓ Clean	`C1C[C@H](OC1)C(=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
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`
ZINC6741121 ZINC	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCCCCCC1`
ZINC6741122 ZINC	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@H]1CCCO1)N1CCCCCCC1`
ZINC108323602 ZINC	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCCC[C@H]1NC(=O)[C@H]1CCCO1`
ZINC157702634 ZINC	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCCCC[C@H]1C(=O)O)[C@H]1CCCO1`
ZINC94744170 ZINC	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCCCC[C@@H]1C(=O)O)[C@@H]1CCCO1`
ZINC94744171 ZINC	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCCCC[C@H]1C(=O)O)[C@@H]1CCCO1`
ZINC13968104 ZINC	0.556	282.3 Da LogP 0.02 TPSA 59.1	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCN(C(=O)[C@H]2CCCO2)CC1`
ZINC5898254 ZINC	0.556	282.3 Da LogP 0.02 TPSA 59.1	✓ Ro5	✓ Clean	`O=C([C@H]1CCCO1)N1CCN(C(=O)[C@H]2CCCO2)CC1`
ZINC5898478 ZINC	0.556	282.3 Da LogP 0.02 TPSA 59.1	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCN(C(=O)[C@@H]2CCCO2)CC1`
ZINC473792 ZINC	0.552	225.3 Da LogP 2.39 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)[C@H]1CCCO1`
ZINC473793 ZINC	0.552	225.3 Da LogP 2.39 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCCC1)[C@@H]1CCCO1`
ZINC476365 ZINC	0.552	211.3 Da LogP 2.00 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)[C@H]1CCCO1`
ZINC476366 ZINC	0.552	211.3 Da LogP 2.00 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)[C@@H]1CCCO1`
ZINC34764844 ZINC	0.550	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC11891528 ZINC	0.548	227.3 Da LogP 0.49 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)[C@@H]2CCCO2)CC1`
ZINC11891532 ZINC	0.548	227.3 Da LogP 0.49 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)[C@H]2CCCO2)CC1`
ZINC1644613 ZINC	0.545	206.3 Da LogP 0.83 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCO`
ZINC2383745924 ZINC	0.542	398.5 Da LogP -0.01 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCC(CO)COCCOCCOCCOC`
ZINC17722834 ZINC	0.536	256.3 Da LogP -0.42 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)[C@H]1CCCO1)[C@@H]1CCCO1`
ZINC376062 ZINC	0.536	310.4 Da LogP 0.89 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(NC1CCC(NC(=O)[C@H]2CCCO2)CC1)[C@H]1CCCO1`

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.