Protein target profile

VK055_2895

tRNA dimethylallyltransferase

Genome: KpATCC43816 Gene: miaA AIK81484.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GI16

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Length 301

Pocket druggability 0.939

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 4 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 89.0% 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. 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 (%): 40.196 Lower values reduce human off-target concern.
Human E-value: 2.44e-17
Gut microbiome similarity: 5.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.282 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: 95.62 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 0.939

Structure A0A0H3GI16

Pocket Pocket 2

P2Rank 0.915

Structure A0A0H3GI16

Pocket Pocket 1

ColabFold model

FPocket 0.924 · Pocket 2

P2Rank 0.878 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 235 / 4744 genomes with a hit

Prevalence 5.0%

Cross-references

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

Sequence

UniProt A0A0H3GI16

Pathways

KEGG R01122 BioCyc RXN0-6274

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Zeatin biosynthesis, no isoenzyme backup detected, more central than 89.0% of genes in this genome.

Relative network centrality 89.0% more central than 89.0% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MGPTASGKTALAIALRKVLPVELISVDSALIYRGMDIGTAKPDAAELSAAPHRLLDILDPAEAYSAADFRRDALAAMADIVAAGRIPLLVGGTMLYFKALLEGLSPLPSADPEVRARIEQQAAEQGWNALHQQLQEIDPVAAARIHPNDPQRLSRALEVFFISGKTLTELTQTSGDALPYQVHQFAIAPASRELLHQRIEQRFHQMLASGFEAEVRALFARGDLHTDMPSIRCVGYRQMWSYLNGEIPYDEMVYRGVCATRQLAKRQVTWLRGWEGVHWLDSEQPEQALNKVLQVVGASQN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

2.5.1.75

Gene Ontology (GO)

GO:0008033 The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0052381 Catalysis of the reaction: adenosine(37) in tRNA + dimethylallyl diphosphate = N(6)-dimethylallyladenosine(37) in tRNA + diphosphate.
GO:0006400 The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

13 records

Show feature table

Start	End	DB	Term	Name
31	273	Pfam	PF01715	IPP transferase
1	142	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
1	142	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
1	299	Gene3D	G3DSA:3.40.50.300	-
1	299	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
105	175	Gene3D	G3DSA:1.10.20.140	-
105	175	FunFam	G3DSA:1.10.20.140:FF:000001	tRNA dimethylallyltransferase
1	294	PANTHER	PTHR11088	TRNA DIMETHYLALLYLTRANSFERASE
1	294	InterPro	IPR039657	Dimethylallyltransferase
1	294	Hamap	MF_00185	tRNA dimethylallyltransferase [miaA].
1	294	InterPro	IPR018022	IPP transferase
1	285	NCBIfam	TIGR00174	tRNA (adenosine(37)-N6)-dimethylallyltransferase MiaA
1	285	InterPro	IPR018022	IPP transferase

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 #2

0.939

Likely same site as P2Rank 2 1.1 Å 25 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #3

0.226

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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

0.915

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Surrounding area

Site 2 P2Rank #2

0.797

Likely same site as FPocket 2 1.1 Å 25 shared residues 100% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:2-9

UniProt: Binding site:4-9

UniProt: Site:115-115 Interaction with substrate tRNA

UniProt: Site:93-93 Interaction with substrate tRNA

Binding pockets · FPocket

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

Site 1 FPocket #2

0.924

Likely same site as P2Rank 2 0.6 Å 26 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #3

0.229

Likely same site as P2Rank 3 3.1 Å 9 shared residues 100% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.878

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.839

Likely same site as FPocket 2 0.6 Å 26 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.012

Likely same site as FPocket 3 3.1 Å 9 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.012

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:2-9

UniProt: Binding site:4-9

UniProt: Site:115-115 Interaction with substrate tRNA

UniProt: Site:93-93 Interaction with substrate tRNA

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_A0A0H3GI16	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2895	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.

55 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

6IA PDB via homolog 417.4 Da · LogP 0.01 · TPSA 172.1 Open detail RCSB PDB

DMA PDB via homolog Detail RCSB PDB

DPO PDB via homolog Detail RCSB PDB

DST PDB via homolog Detail RCSB PDB

PPV 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
6IA RCSB PDB	3EPL	P07884	417.4 Da LogP 0.01 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)CCNc1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C…`
DMA RCSB PDB	3EPL	P07884	246.1 Da LogP 1.18 TPSA 113.3	✓ Ro5	✓ Clean	`CC(=CCO[P@@](=O)(O)OP(=O)(O)O)C`
DPO RCSB PDB	3CRQ	Q9HUL9	173.9 Da LogP -3.34 TPSA 135.6	✓ Ro5	✓ Clean	`[O-]P(=O)([O-])OP(=O)([O-])[O-]`
DST RCSB PDB	2ZXU	P16384	262.2 Da LogP 1.90 TPSA 104.1	✓ Ro5	✓ Clean	`CC(=CCS[P@@](=O)(O)OP(=O)(O)O)C`
PPV RCSB PDB	3EPH	P07884	178.0 Da LogP -0.81 TPSA 124.3	✓ Ro5	✓ Clean	`OP(=O)(O)OP(=O)(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
ZINC13516496 ZINC	0.750	361.3 Da LogP -1.40 TPSA 172.1	✓ Ro5	✓ Clean	`CNc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC5439578 ZINC	0.734	415.3 Da LogP -0.07 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)=CCNc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O…`
ZINC5439579 ZINC	0.734	415.3 Da LogP -0.07 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)=CCNc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)…`
ZINC5439581 ZINC	0.734	415.3 Da LogP -0.07 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)=CCNc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O…`
ZINC5439583 ZINC	0.734	415.3 Da LogP -0.07 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)=CCNc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)…`
ZINC1852448 ZINC	0.697	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(NCc4ccccc4)ncn…`
ZINC2097407 ZINC	0.697	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](n2cnc3c(NCc4ccccc4)ncn…`
ZINC3212712 ZINC	0.697	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](n2cnc3c(NCc4ccccc4)nc…`
ZINC5412148 ZINC	0.697	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(NCc4ccccc4)ncn…`
ZINC5412151 ZINC	0.697	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](n2cnc3c(NCc4ccccc4)nc…`
ZINC5412155 ZINC	0.697	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(NCc4ccccc4)ncn…`
ZINC5412158 ZINC	0.697	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](n2cnc3c(NCc4ccccc4)nc…`
ZINC5432461 ZINC	0.676	427.3 Da LogP -0.24 TPSA 185.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(NCc4ccco4)ncnc…`
ZINC5432462 ZINC	0.676	427.3 Da LogP -0.24 TPSA 185.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](n2cnc3c(NCc4ccco4)ncn…`
ZINC5432464 ZINC	0.676	427.3 Da LogP -0.24 TPSA 185.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(NCc4ccco4)ncnc…`
ZINC5432465 ZINC	0.676	427.3 Da LogP -0.24 TPSA 185.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](n2cnc3c(NCc4ccco4)ncn…`
ZINC4096207 ZINC	0.672	463.3 Da LogP -2.11 TPSA 246.7	2 viol.	✓ Clean	`O=C(O)C[C@H](Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O…`
ZINC13531931 ZINC	0.656	348.2 Da LogP -1.74 TPSA 180.3	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](n2cnc3c(O)ncnc32)[C@@H…`
ZINC13531934 ZINC	0.656	348.2 Da LogP -1.74 TPSA 180.3	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](n2cnc3c(O)ncnc32)[C@@H…`
ZINC16990100 ZINC	0.656	364.3 Da LogP -1.16 TPSA 160.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(S)ncnc32)[C@H]…`
ZINC13518964 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC13526959 ZINC	0.645	366.7 Da LogP -0.79 TPSA 160.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](n2cnc3c(Cl)ncnc32)[C@H…`
ZINC1532515 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.645	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC1319874 ZINC	0.631	353.4 Da LogP -1.13 TPSA 145.8	✓ Ro5	✓ Clean	`C[C@H](CO)CCNc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@…`
ZINC13782061 ZINC	0.631	353.4 Da LogP -1.13 TPSA 145.8	✓ Ro5	✓ Clean	`C[C@@H](CO)CCNc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@…`
ZINC34718738 ZINC	0.591	444.3 Da LogP -1.04 TPSA 206.6	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@H](n2cnc3c(S)…`
ZINC34718739 ZINC	0.591	444.3 Da LogP -1.04 TPSA 206.6	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@@H](n2cnc3c(S…`
ZINC34718740 ZINC	0.591	444.3 Da LogP -1.04 TPSA 206.6	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@H](n2cnc3c(S)…`
ZINC34718741 ZINC	0.591	444.3 Da LogP -1.04 TPSA 206.6	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@@H](n2cnc3c(S…`
ZINC4096224 ZINC	0.585	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12360002 ZINC	0.582	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	0.582	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	0.582	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	0.582	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	0.582	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	0.582	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586020 ZINC	0.582	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	0.582	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	0.582	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`

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.