Protein target profile

KP13_01741

3-ketoacyl-CoA thiolase

Genome: KpKP13 Gene: AHE46956.1 fadA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GH83

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Length 387

Pocket druggability 0.843

Direct ligand evidence 0 61 total records

Functional annotation 1 EC 8 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 0.84, P2Rank 0.81). 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 0.84. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.81. 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 (%): 45.223 Lower values reduce human off-target concern.
Human E-value: 5.85e-71
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 64.323 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: 97.13 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 0.843

Structure A0A0H3GH83

Pocket Pocket 10

P2Rank 0.808

Structure A0A0H3GH83

Pocket Pocket 1

ColabFold model

FPocket 0.932 · Pocket 2

P2Rank 0.822 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 142 / 4744 genomes with a hit

Prevalence 3.0%

Cross-references

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

Sequence

UniProt A0A0H3GH83

Sequence

Primary amino-acid sequence viewer.

MEQVVIVDAIRTPMGRSKGGAFRHVRAEDLSAHLMRSLLSRNPSLEASAIDDIYWGCVQQTLEQGFNIARNAALLAEIPHSVPANTVNRLCGSSMQALHDAARMIMTGDASVCLIGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARLHGISREMQDQFAARSHARAWAATQSGAFKAEIIPTGGHDADGVLKSFNYDEVIRPETTVETLSTLKPAFDPVTGTVTAGTSSALSDGAAAMLLMNESRARELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSTSDIDVFEMNEAFAAQILPCIKDLGLMEQIDEKINLNGGAIALGHPLGCSGARISTTLINQMERKDAQFGLATMCIGLGQGIATVFERV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

2.3.1.16

Gene Ontology (GO)

GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
GO:0016042 The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
GO:0003988 Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
GO:0006635 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
GO:0010124 The chemical reactions and pathways resulting in the breakdown of phenylacetate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
1	387	PIRSF	PIRSF000429	Ac-CoA_Ac_transf
1	387	InterPro	IPR002155	Thiolase
262	386	SUPERFAMILY	SSF53901	Thiolase-like
262	386	InterPro	IPR016039	Thiolase-like
4	267	Gene3D	G3DSA:3.40.47.10	-
4	267	InterPro	IPR016039	Thiolase-like
87	105	ProSitePatterns	PS00098	Thiolases acyl-enzyme intermediate signature.
87	105	InterPro	IPR020615	Thiolase, acyl-enzyme intermediate active site
127	381	Gene3D	G3DSA:3.40.47.10	-
127	381	InterPro	IPR016039	Thiolase-like
1	387	Hamap	MF_01620	3-ketoacyl-CoA thiolase [fadA].
1	387	InterPro	IPR012805	Acetyl-CoA C-acyltransferase FadA
3	387	NCBIfam	TIGR02445	acetyl-CoA C-acyltransferase FadA
3	387	InterPro	IPR012805	Acetyl-CoA C-acyltransferase FadA
5	386	CDD	cd00751	thiolase
5	386	InterPro	IPR002155	Thiolase
6	385	NCBIfam	TIGR01930	acetyl-CoA C-acyltransferase
6	385	InterPro	IPR002155	Thiolase
2	387	PANTHER	PTHR43853	3-KETOACYL-COA THIOLASE, PEROXISOMAL
261	386	Pfam	PF02803	Thiolase, C-terminal domain
261	386	InterPro	IPR020617	Thiolase, C-terminal
368	381	ProSitePatterns	PS00099	Thiolases active site.
368	381	InterPro	IPR020610	Thiolase, active site
1	386	FunFam	G3DSA:3.40.47.10:FF:000010	Acetyl-CoA acetyltransferase (Thiolase)
333	349	ProSitePatterns	PS00737	Thiolases signature 2.
333	349	InterPro	IPR020613	Thiolase, conserved site
1	259	SUPERFAMILY	SSF53901	Thiolase-like
1	259	InterPro	IPR016039	Thiolase-like
4	254	Pfam	PF00108	Thiolase, N-terminal domain
4	254	InterPro	IPR020616	Thiolase, N-terminal

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 #10

0.843

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Surrounding area

Site 2 FPocket #17

0.394

Likely same site as P2Rank 1 5.8 Å 10 shared residues 77% 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

0.808

Likely same site as FPocket 17 5.8 Å 10 shared residues 77% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.215

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Surrounding area

Site 3 P2Rank #3

0.011

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Surrounding area

Site 4 P2Rank #4

0.003

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Surrounding area

Residue sets

UniProt: Active site:343-343 Proton acceptor

UniProt: Active site:373-373 Proton acceptor

UniProt: Active site:91-91 Acyl-thioester intermediate

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.822

Likely same site as FPocket 2 3.6 Å 19 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.109

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Surrounding area

Site 3 P2Rank #3

0.014

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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_A0A0H3GH83	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01741	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.

61 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

168 PDB via homolog 388.5 Da · LogP 0.15 · TPSA 131.0 Open detail RCSB PDB

5UG PDB via homolog Detail RCSB PDB

CAA PDB via homolog Detail RCSB PDB

COZ PDB via homolog Detail RCSB PDB

DNO 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
168 RCSB PDB	1OU6	P07097	388.5 Da LogP 0.15 TPSA 131.0	✓ Ro5	✓ Clean	`CC(=O)OCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COC(=O)C(C…`
5UG RCSB PDB	5F38	P76461	438.3 Da LogP -0.85 TPSA 191.7	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)OP(=O)(O)O)[C@@H](C(=O)NCCC(=O)…`
CAA RCSB PDB	1M1O	P07097	851.6 Da LogP -1.36 TPSA 380.7	3 viol.	✓ Clean	`CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
COZ RCSB PDB	5F38	P76461	767.5 Da LogP -1.67 TPSA 346.6	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…`
DNO RCSB PDB	2WKU	P07097	180.2 Da LogP -3.38 TPSA 118.2	✓ Ro5	✓ Clean	`C([C@H]([C@H]([C@@H]([C@@H](C=O)O)O)O)O)O`
DTT RCSB PDB	4C2K	P42765	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
NH4 RCSB PDB	6ARE	Q4WCL5	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
O8Y RCSB PDB	6PCC	Q88N39	100.2 Da LogP 1.77 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC=O`
OPI RCSB PDB	2VU1	P07097	346.4 Da LogP -0.42 TPSA 125.0	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCC(C)(C)[C@H](C(=O)NCCC(=O)NCCO)O`
OYA RCSB PDB	6PCD	Q88N39	128.2 Da LogP 2.55 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCCCC=O`
PN5 RCSB PDB	2VU2	P07097	362.5 Da LogP 0.52 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCC(C)(C)[C@H](C(=O)NCCC(=O)NCCS)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
ZINC100056793 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC100056796 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC12953159 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC12953162 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC12953168 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC13522675 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC13522684 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC4353166 ZINC	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353167 ZINC	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353168 ZINC	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353169 ZINC	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353180 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353181 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353182 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)…`
ZINC95884213 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC9915770 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC9915771 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC1693894 ZINC	0.938	212.4 Da LogP 4.89 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC=O`
ZINC43061660 ZINC	0.789	210.4 Da LogP 4.66 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC=O`
ZINC43061664 ZINC	0.789	210.4 Da LogP 4.66 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCC=O`
ZINC13546064 ZINC	0.700	210.4 Da LogP 4.66 TPSA 17.1	✓ Ro5	✓ Clean	`CCCC/C=C\CCCCCCCC=O`
ZINC1850393 ZINC	0.700	210.4 Da LogP 4.66 TPSA 17.1	✓ Ro5	✓ Clean	`CCCC/C=C/CCCCCCCC=O`
ZINC57988531 ZINC	0.600	360.3 Da LogP -6.60 TPSA 228.6	2 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O[C@@H](O)[C@H](O)[C…`
ZINC57988534 ZINC	0.600	360.3 Da LogP -6.60 TPSA 228.6	2 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O[C@@H](O)[C@H](O)[C@…`
ZINC12501123 ZINC	0.595	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC4228234 ZINC	0.595	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC79671662 ZINC	0.595	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC79671663 ZINC	0.595	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC3869683 ZINC	0.587	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@H](O)C(=O)NCCC(=O)NCCS`
ZINC3869684 ZINC	0.587	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@@H](O)C(=O)NCCC(=O)NCCS`
ZINC2382315554 ZINC	0.556	311.3 Da LogP -5.37 TPSA 201.8	1 viol.	✓ Clean	`N[C@@H](C=O)[C@@H](O)[C@H](O)[C@@H](O)C[C@H](O)…`
ZINC100055463 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC100064885 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC17780060 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC17952732 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC18042331 ZINC	0.550	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H]…`
ZINC18120313 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC3979006 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC4403103 ZINC	0.550	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403105 ZINC	0.550	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403107 ZINC	0.550	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@…`
ZINC9212412 ZINC	0.550	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@@H](O)CO`
ZINC12360703 ZINC	0.549	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.549	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC31977053 ZINC	0.549	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.549	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.549	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.549	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.549	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.549	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`

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.