Protein target profile

KP13_03141

Uridine kinase

Genome: KpKP13 Gene: AHE43644.1 udk 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GVV7

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Length 213

Pocket druggability 0.556

Direct ligand evidence 0 64 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.56. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.87. 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 (%): 37.624 Lower values reduce human off-target concern.
Human E-value: 2.91e-42
Gut microbiome similarity: 7.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 68.159 Higher values support similarity to known essential genes.
DEG E-value: 6.6999999999999994e-105 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.52 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 0.556

Structure A0A0H3GVV7

Pocket Pocket 1

P2Rank 0.874

Structure A0A0H3GVV7

Pocket Pocket 1

ColabFold model

FPocket 0.696 · Pocket 1

P2Rank 0.872 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 370 / 4744 genomes with a hit

Prevalence 7.8%

Cross-references

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

Sequence

UniProt A0A0H3GVV7

Chemistry

ChEMBL CHEMBL1592234 ChEMBL CHEMBL4787313

Sequence

Primary amino-acid sequence viewer.

MTDMSHQCVIVGIAGASASGKSLIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPSSMDHSLLFQHLQMLKSGQPIELPVYSYVEHTRTPNTIHVEPKKVIILEGILLLTDARLRNELNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

2.7.1.48

Gene Ontology (GO)

GO:0016773 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to an alcohol group (acceptor).
GO:0004849 Catalysis of the reaction: ATP + uridine = ADP + UMP.
GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0043771 Catalysis of the reaction: ATP + cytidine = ADP + CMP.
GO:0044211 Any process which produces cytidine 5'-triphosphate (CTP) from derivatives of it, without de novo synthesis.
GO:0044206 Any process which produces UMP, uridine monophosphate, from derivatives of it (e.g. cytidine, uridine, cytosine) without de novo synthesis.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
10	208	CDD	cd02023	UMPK
10	208	InterPro	IPR000764	Uridine kinase-like
21	213	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
5	213	Hamap	MF_00551	Uridine kinase [udk].
5	213	InterPro	IPR026008	Uridine kinase
1	7	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
5	213	Gene3D	G3DSA:3.40.50.300	-
5	213	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
7	213	FunFam	G3DSA:3.40.50.300:FF:000252	Uridine kinase
10	199	Pfam	PF00485	Phosphoribulokinase / Uridine kinase family
10	199	InterPro	IPR006083	Phosphoribulokinase/uridine kinase
8	205	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
8	205	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
8	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
6	213	NCBIfam	TIGR00235	uridine kinase
6	213	InterPro	IPR000764	Uridine kinase-like
9	190	PANTHER	PTHR10285	URIDINE KINASE
157	168	PRINTS	PR00988	Uridine kinase signature
8	25	PRINTS	PR00988	Uridine kinase signature
87	102	PRINTS	PR00988	Uridine kinase signature
143	153	PRINTS	PR00988	Uridine kinase signature
179	192	PRINTS	PR00988	Uridine kinase signature
42	53	PRINTS	PR00988	Uridine kinase signature

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

0.556

Likely same site as P2Rank 1 3.9 Å 16 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #3

0.484

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Surrounding area

Site 3 FPocket #6

0.455

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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

0.874

Likely same site as FPocket 1 3.9 Å 16 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.032

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Surrounding area

Site 3 P2Rank #3

0.019

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Surrounding area

Residue sets

UniProt: Binding site:15-22

Binding pockets · FPocket

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

Site 1 FPocket #1

0.696

Likely same site as P2Rank 1 4.0 Å 16 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #5

0.257

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Surrounding area

Site 3 FPocket #3

0.255

Likely same site as P2Rank 2 1.6 Å 7 shared residues 88% 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

0.872

Likely same site as FPocket 1 4.0 Å 16 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.019

Likely same site as FPocket 3 1.6 Å 7 shared residues 88% of smaller site

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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_A0A0H3GVV7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03141	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 12 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0JR PDB via homolog 309.4 Da · LogP -0.42 · TPSA 111.6 Open detail RCSB PDB

ACP PDB via homolog Detail RCSB PDB

CTN PDB via homolog Detail RCSB PDB

DTT PDB via homolog Detail RCSB PDB

G6P 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
0JR RCSB PDB	4GI7	B5XYG3	309.4 Da LogP -0.42 TPSA 111.6	✓ Ro5	✓ Clean	`CC(C)(CO)[C@H](C(=O)NCCC(=O)NCc1cccnc1)O`
ACP RCSB PDB	3W34	Q5SKR5	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CTN RCSB PDB	3W34	Q5SKR5	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
DTT RCSB PDB	6KEV	Q31PL2	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
G6P RCSB PDB	6KEV	Q31PL2	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)OP…`
KEA RCSB PDB	6N54	Q9BZX2	348.2 Da LogP -1.13 TPSA 205.9	✓ Ro5	Alert	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
OS RCSB PDB	6HZL	A0A0H3K6J7	190.2 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Os+3]`
P6D RCSB PDB	6PWZ	Q9BZX2	—	—	—	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
PN4 RCSB PDB	4F7W	B5XYG3	288.4 Da LogP 0.18 TPSA 98.7	✓ Ro5	✓ Clean	`CCCCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO)O`
SH2 RCSB PDB	4NE2	B5XYG3	366.4 Da LogP -0.04 TPSA 117.1	✓ Ro5	✓ Clean	`CC(C)(CO)[C@H](C(=O)NCCC(=O)NCCc1ccc2c(c1)OCO2)O`
UZ0 RCSB PDB	6N55	Q9BZX2	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
UZR RCSB PDB	6N53	Q9BZX2	350.2 Da LogP -2.18 TPSA 201.4	✓ Ro5	Alert	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`

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
CHEMBL1592234 ChEMBL	Q9BZX2	6.00 ~1.0 µM	497.6 Da LogP 5.89 TPSA 101.4	1 viol.	✓ Clean	`Cc1ccc(-c2nc3c(c(SCC(=O)Nc4cccc(C(=O)O)c4)n2)Cc…`
CHEMBL4787313 ChEMBL	Q9BZX2	—	715.3 Da LogP 0.35 TPSA 129.5	1 viol.	✓ Clean	`COc1c(OCCOCCOCCNC(=O)CCCC[C@@H]2SC[C@@H]3NC(=O)…`

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
ZINC1078621 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC12336757 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC12336758 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC146563393 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1[C@@H](O)[C@@H](CO)O[C@H]1n1cc…`
ZINC16969357 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC17261182 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1[C@H](O)[C@@H](CO)O[C@@H]1n1cc…`
ZINC230402123 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1[C@@H](n2ccc(=O)[nH]c2=O)O[C@H…`
ZINC230402126 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1[C@@H](n2ccc(=O)[nH]c2=O)O[C@…`
ZINC230402130 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1[C@H](O)[C@@H](CO)O[C@@H]1n1c…`
ZINC2583632 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC3795098 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC3830623 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC3830624 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3978018 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)n1`
ZINC4521169 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1[C@H](O)[C@H](CO)O[C@@H]1n1cc…`
ZINC4521170 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1[C@H](O)[C@H](CO)O[C@H]1n1ccc…`
ZINC4521171 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1[C@H](O)[C@H](CO)O[C@@H]1n1ccc…`
ZINC4521172 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1[C@H](O)[C@H](CO)O[C@H]1n1ccc(…`
ZINC6091560 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1n1cc…`
ZINC6091575 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC6234828 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC6524892 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC83301154 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1[C@@H](n2ccc(=O)[nH]c2=O)O[C@…`
ZINC895248 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC90697708 ZINC	1.000	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1[C@@H](O)[C@@H](CO)O[C@H]1n1c…`
ZINC34268101 ZINC	0.848	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1[C@H](CO)O[C@H](n2ccc(=O)[nH]…`
ZINC34268103 ZINC	0.848	269.2 Da LogP -1.53 TPSA 153.3	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1[C@H](O)[C@@H](n2ccc(=O)[nH]c2…`
ZINC12360002 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC34085615 ZINC	0.829	242.2 Da LogP -2.60 TPSA 136.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2N)c(=O)n1`
ZINC13546396 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2F)c(=O)n1`
ZINC16952044 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2F)c(=O)n1`
ZINC17174505 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2F)c(=O…`
ZINC17174506 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2F)c(=O)…`
ZINC2522524 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2F)c(=O)n1`
ZINC3817231 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2F)c(=O)n1`
ZINC57331 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2F)c(=O)…`
ZINC5758597 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2F)c(=O)n1`
ZINC5758598 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2F)c(=O)…`
ZINC59201305 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2F)c(=O)n1`
ZINC85475812 ZINC	0.786	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](F)[C@H]2O)c(=O)n1`

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.