Protein target profile

VK055_1764

galactose-1-phosphate uridylyltransferase

Genome: KpATCC43816 Gene: galT AIK80384.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GQ36

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Length 348

Pocket druggability 0.868

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 54 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

Central metabolic position More central than 92.4% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.88. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 60.345 Lower values reduce human off-target concern.
Human E-value: 2.39e-18
Gut microbiome similarity: 3.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 68.895 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 95.9 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 0.868

Structure A0A0H3GQ36

Pocket Pocket 3

P2Rank 0.88

Structure A0A0H3GQ36

Pocket Pocket 1

ColabFold model

FPocket 0.748 · Pocket 3

P2Rank 0.832 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 156 / 4744 genomes with a hit

Prevalence 3.3%

Cross-references

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

Sequence

UniProt A0A0H3GQ36

Pathways

KEGG R00502 BioCyc UTPHEXPURIDYLYLTRANS-RXN

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: more central than 92.4% of genes in this genome.

Relative network centrality 92.4% more central than 92.4% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSVFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTLPAHDPDCFLCPGNTRVTGDTNPNYTGTYVFTNDFAALMTDTPDAPESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGKSYPWVQVFENKGAAMGCSNPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAHVQRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDVHFRESGV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

2.7.7.12

Gene Ontology (GO)

GO:0008270 Binding to a zinc ion (Zn).
GO:0008108 Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
GO:0006012 The chemical reactions and pathways involving galactose, the aldohexose galacto-hexose. D-galactose is widely distributed in combined form in plants, animals and microorganisms as a constituent of oligo- and polysaccharides; it also occurs in galactolipids and as its glucoside in lactose and melibiose.
GO:0033499 The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate UDP-galactose.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
35	175	FunFam	G3DSA:3.30.428.10:FF:000002	Galactose-1-phosphate uridylyltransferase
11	338	CDD	cd00608	GalT
11	338	InterPro	IPR001937	Galactose-1-phosphate uridyl transferase, class I
179	345	SUPERFAMILY	SSF54197	HIT-like
179	345	InterPro	IPR036265	HIT-like superfamily
4	345	PANTHER	PTHR11943	GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE
4	345	InterPro	IPR001937	Galactose-1-phosphate uridyl transferase, class I
151	168	ProSitePatterns	PS00117	Galactose-1-phosphate uridyl transferase family 1 active site signature.
151	168	InterPro	IPR019779	Galactose-1-phosphate uridyl transferase, class I His-active site
35	175	Gene3D	G3DSA:3.30.428.10	-
35	175	InterPro	IPR036265	HIT-like superfamily
1	341	PIRSF	PIRSF000808	GalT
1	341	InterPro	IPR001937	Galactose-1-phosphate uridyl transferase, class I
4	177	SUPERFAMILY	SSF54197	HIT-like
4	177	InterPro	IPR036265	HIT-like superfamily
5	176	Pfam	PF01087	Galactose-1-phosphate uridyl transferase, N-terminal domain
5	176	InterPro	IPR005849	Galactose-1-phosphate uridyl transferase, N-terminal
176	347	Gene3D	G3DSA:3.30.428.10	-
176	347	InterPro	IPR036265	HIT-like superfamily
2	347	NCBIfam	TIGR00209	galactose-1-phosphate uridylyltransferase
2	347	InterPro	IPR001937	Galactose-1-phosphate uridyl transferase, class I
176	348	FunFam	G3DSA:3.30.428.10:FF:000001	Galactose-1-phosphate uridylyltransferase
183	345	Pfam	PF02744	Galactose-1-phosphate uridyl transferase, C-terminal domain
183	345	InterPro	IPR005850	Galactose-1-phosphate uridyl transferase, C-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 #3

0.868

Likely same site as P2Rank 3 2.1 Å 19 shared residues 79% 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

0.88

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Surrounding area

Site 2 P2Rank #2

0.506

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Surrounding area

Site 3 P2Rank #3

0.47

Likely same site as FPocket 3 2.1 Å 19 shared residues 79% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.058

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Surrounding area

Site 5 P2Rank #5

0.04

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Surrounding area

Residue sets

UniProt: Active site:166-166 Tele-UMP-histidine intermediate

UniProt: Binding site:115-115

UniProt: Binding site:153-153 in other chain

UniProt: Binding site:159-161 in other chain

UniProt: Binding site:164-164

UniProt: Binding site:168-168 in other chain

UniProt: Binding site:182-182

UniProt: Binding site:28-31

UniProt: Binding site:281-281

UniProt: Binding site:296-296

UniProt: Binding site:298-298

UniProt: Binding site:311-312

UniProt: Binding site:316-317

UniProt: Binding site:323-323 in other chain

UniProt: Binding site:52-52

UniProt: Binding site:55-55

UniProt: Binding site:61-61 in other chain

UniProt: Binding site:77-78 in other chain

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.832

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Surrounding area

Site 2 P2Rank #2

0.609

Likely same site as FPocket 3 1.7 Å 25 shared residues 93% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.462

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Surrounding area

Site 4 P2Rank #4

0.051

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Surrounding area

Site 5 P2Rank #5

0.049

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Surrounding area

Residue sets

UniProt: Active site:166-166 Tele-UMP-histidine intermediate

UniProt: Binding site:115-115

UniProt: Binding site:153-153 in other chain

UniProt: Binding site:159-161 in other chain

UniProt: Binding site:164-164

UniProt: Binding site:168-168 in other chain

UniProt: Binding site:182-182

UniProt: Binding site:28-31

UniProt: Binding site:281-281

UniProt: Binding site:296-296

UniProt: Binding site:298-298

UniProt: Binding site:311-312

UniProt: Binding site:316-317

UniProt: Binding site:323-323 in other chain

UniProt: Binding site:52-52

UniProt: Binding site:55-55

UniProt: Binding site:61-61 in other chain

UniProt: Binding site:77-78 in other chain

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_A0A0H3GQ36	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1764	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ADQ PDB via homolog 589.3 Da · LogP -3.92 · TPSA 311.7 Open detail RCSB PDB

GDU PDB via homolog Detail RCSB PDB

H2U PDB via homolog Detail RCSB PDB

UPG PDB via homolog Detail RCSB PDB

ZINC12959005 ZINC proposed compound · Tanimoto 0.729 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
ADQ RCSB PDB	2H39	Q9FK51	589.3 Da LogP -3.92 TPSA 311.7	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
GDU RCSB PDB	1GUP	P09148	566.3 Da LogP -4.79 TPSA 297.0	3 viol.	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
H2U RCSB PDB	6GQD	P07902-2	326.2 Da LogP -2.52 TPSA 165.9	✓ Ro5	✓ Clean	`C1CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO…`
UPG RCSB PDB	1GUQ	P09148	566.3 Da LogP -4.79 TPSA 297.0	3 viol.	✓ Clean	`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).

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
ZINC12959005 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC12959016 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O…`
ZINC13548378 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726233 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC3861755 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875255 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875256 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)…`
ZINC3875257 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875258 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)…`
ZINC88466482 ZINC	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC35636069 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)OP(=O)(O)O)[…`
ZINC40655887 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)OP(=O)(O)O)[…`
ZINC40655889 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC44460318 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC4490939 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585026 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585028 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC8585030 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585032 ZINC	0.724	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC2069590148 ZINC	0.711	260.2 Da LogP -1.98 TPSA 108.3	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](N2CCC(=O)NC2=O)[C@H](O)[C@H]1O`
ZINC2069590149 ZINC	0.711	260.2 Da LogP -1.98 TPSA 108.3	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](N2CCC(=O)NC2=O)[C@H](O)[C@@H]1O`
ZINC2069590150 ZINC	0.711	260.2 Da LogP -1.98 TPSA 108.3	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](N2CCC(=O)NC2=O)[C@@H](O)[C@@H]…`
ZINC2069590151 ZINC	0.711	260.2 Da LogP -1.98 TPSA 108.3	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](N2CCC(=O)NC2=O)[C@@H](O)[C@H]1O`
ZINC102211562 ZINC	0.698	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC110347779 ZINC	0.698	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC110347782 ZINC	0.698	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC97976147 ZINC	0.698	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC4188096 ZINC	0.661	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188103 ZINC	0.661	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4188112 ZINC	0.661	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188116 ZINC	0.661	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC105358861 ZINC	0.659	246.2 Da LogP -2.63 TPSA 119.3	✓ Ro5	✓ Clean	`O=C1CCN([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)C(=O)…`
ZINC105358865 ZINC	0.659	246.2 Da LogP -2.63 TPSA 119.3	✓ Ro5	✓ Clean	`O=C1CCN([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)C(=O)N1`
ZINC1562565 ZINC	0.659	246.2 Da LogP -2.63 TPSA 119.3	✓ Ro5	✓ Clean	`O=C1CCN([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)C(=O)…`
ZINC2558628 ZINC	0.659	246.2 Da LogP -2.63 TPSA 119.3	✓ Ro5	✓ Clean	`O=C1CCN([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)C(=O)…`
ZINC12503831 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC12503833 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC13512000 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC1532538 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC2026984 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC2123545 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC2606131 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC36377965 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC3870257 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC3870258 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC3870259 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC3870260 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC9235501 ZINC	0.655	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H…`
ZINC3201878 ZINC	0.644	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC3830179 ZINC	0.644	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`

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.