Protein target profile

KP13_00709

Tryptophanyl-tRNA synthetase

Genome: KpKP13 Gene: AHE42327.1 trpS 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GU65

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Length 334

Pocket druggability 0.401

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 7 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 0.40. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.85. 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 (%): 42.296 Lower values reduce human off-target concern.
Human E-value: 5.96e-87
Gut microbiome similarity: 31.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 95.21 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: 94.28 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 0.401

Structure A0A0H3GU65

Pocket Pocket 26

P2Rank 0.851

Structure A0A0H3GU65

Pocket Pocket 1

ColabFold model

FPocket 0.369 · Pocket 1

P2Rank 0.88 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1492 / 4744 genomes with a hit

Prevalence 31.5%

Cross-references

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

Sequence

UniProt A0A0H3GU65

Sequence

Primary amino-acid sequence viewer.

MTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDPQQLRKATLDTLALYLACGIDPQKSTIFVQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNQVPVGEDQKQHLELSRDIAQRFNAIYGDIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDLKEKAGVSNLLDILSAVTGKTIPELEQHFEGKMYGHLKGEVAEAVSGMLIDLQERYHRFRNDEAFLNQVMKDGAEKASARASQTLKAVYEAIGFVAKP

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

6.1.1.2

Gene Ontology (GO)

GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0006436 The process of coupling tryptophan to tryptophanyl-tRNA, catalyzed by tryptophanyl-tRNA synthetase. The tryptophanyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tryptophan-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
GO:0006418 The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, to be used in ribosome-mediated polypeptide synthesis.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004830 Catalysis of the reaction: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophanyl-tRNA(Trp).
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
142	163	PRINTS	PR01039	Tryptophanyl-tRNA synthetase signature
142	163	InterPro	IPR002306	Tryptophan-tRNA ligase
195	205	PRINTS	PR01039	Tryptophanyl-tRNA synthetase signature
195	205	InterPro	IPR002306	Tryptophan-tRNA ligase
16	32	PRINTS	PR01039	Tryptophanyl-tRNA synthetase signature
16	32	InterPro	IPR002306	Tryptophan-tRNA ligase
66	85	PRINTS	PR01039	Tryptophanyl-tRNA synthetase signature
66	85	InterPro	IPR002306	Tryptophan-tRNA ligase
3	285	Pfam	PF00579	tRNA synthetases class I (W and Y)
3	285	InterPro	IPR002305	Aminoacyl-tRNA synthetase, class Ic
186	298	FunFam	G3DSA:1.10.240.10:FF:000002	Tryptophan--tRNA ligase
6	212	FunFam	G3DSA:3.40.50.620:FF:000024	Tryptophan--tRNA ligase
5	284	CDD	cd00806	TrpRS_core
5	284	InterPro	IPR002306	Tryptophan-tRNA ligase
3	331	Hamap	MF_00140_B	Tryptophan--tRNA ligase [trpS].
3	331	InterPro	IPR024109	Tryptophan-tRNA ligase, bacterial-type
6	329	Gene3D	G3DSA:3.40.50.620	HUPs
6	329	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
12	21	ProSitePatterns	PS00178	Aminoacyl-transfer RNA synthetases class-I signature.
12	21	InterPro	IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site
3	330	NCBIfam	TIGR00233	tryptophan--tRNA ligase
3	330	InterPro	IPR002306	Tryptophan-tRNA ligase
3	330	PANTHER	PTHR43766	TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL
5	330	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
186	298	Gene3D	G3DSA:1.10.240.10	-

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 #26

0.401

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Surrounding area

Site 2 FPocket #2

0.262

Likely same site as P2Rank 1 5.4 Å 18 shared residues 67% 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

0.851

Likely same site as FPocket 2 5.4 Å 18 shared residues 67% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.055

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Surrounding area

Site 3 P2Rank #3

0.009

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Surrounding area

Residue sets

UniProt: Binding site:11-13

UniProt: Binding site:135-135

UniProt: Binding site:147-149

UniProt: Binding site:186-186

UniProt: Binding site:19-20

UniProt: Binding site:195-199

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.88

Likely same site as FPocket 1 5.7 Å 17 shared residues 94% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.049

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Surrounding area

Site 3 P2Rank #3

0.015

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Surrounding area

Site 4 P2Rank #4

0.004

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Surrounding area

Site 5 P2Rank #5

0.001

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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_A0A0H3GU65	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00709	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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5BX PDB via homolog 257.3 Da · LogP 1.77 · TPSA 66.5 Open detail RCSB PDB

9E0 PDB via homolog Detail RCSB PDB

ANL PDB via homolog Detail RCSB PDB

AQP PDB via homolog Detail RCSB PDB

LTN 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
5BX RCSB PDB	5DK4	P00953	257.3 Da LogP 1.77 TPSA 66.5	✓ Ro5	✓ Clean	`C[C@H](c1c[nH]c2c1cccc2)[C@H]3C(=O)N=C(O3)NC`
9E0 RCSB PDB	7CMS	P00953	233.3 Da LogP 2.83 TPSA 53.1	✓ Ro5	✓ Clean	`C[C@H]1c2c[nH]c3c2c(ccc3)S[C@H]1C(=O)O`
ANL RCSB PDB	2OV4	P00953	93.1 Da LogP 1.27 TPSA 26.0	✓ Ro5	✓ Clean	`c1ccc(cc1)N`
AQP RCSB PDB	2OV4	P00953	587.2 Da LogP -1.51 TPSA 325.7	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
LTN RCSB PDB	1MAU	P00953	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)C[C@@H](C(=O)N)N`
NH4 RCSB PDB	1I6K	P00953	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
TYM RCSB PDB	1I6K	P00953	533.4 Da LogP -0.26 TPSA 233.9	3 viol.	✓ Clean	`c1ccc2c(c1)c(c[nH]2)C[C@@H](C(=O)O[P@](=O)(O)OC…`
WSA RCSB PDB	2YY5	P75510	532.5 Da LogP -1.54 TPSA 233.6	3 viol.	✓ Clean	`c1ccc2c(c1)c(c[nH]2)C[C@@H](C(=O)NS(=O)(=O)OC[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
ZINC13508004 ZINC	1.000	257.3 Da LogP 1.77 TPSA 66.5	✓ Ro5	✓ Clean	`CNC1=NC(=O)[C@@H]([C@@H](C)c2c[nH]c3ccccc23)O1`
ZINC13508006 ZINC	1.000	257.3 Da LogP 1.77 TPSA 66.5	✓ Ro5	✓ Clean	`CNC1=NC(=O)[C@H]([C@@H](C)c2c[nH]c3ccccc23)O1`
ZINC3964188 ZINC	1.000	257.3 Da LogP 1.77 TPSA 66.5	✓ Ro5	✓ Clean	`CNC1=NC(=O)[C@H]([C@H](C)c2c[nH]c3ccccc23)O1`
ZINC83315 ZINC	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC83317 ZINC	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC9049 ZINC	1.000	257.3 Da LogP 1.77 TPSA 66.5	✓ Ro5	✓ Clean	`CNC1=NC(=O)[C@@H]([C@H](C)c2c[nH]c3ccccc23)O1`
ZINC12360002 ZINC	0.980	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	0.980	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	0.980	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	0.980	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	0.980	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	0.980	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	0.980	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	0.980	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	0.980	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	0.980	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	0.980	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964 ZINC	0.830	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.830	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	0.830	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	0.830	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	0.830	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	0.830	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	0.830	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	0.830	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	0.830	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	0.830	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	0.830	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	0.830	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	0.830	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC34718738 ZINC	0.786	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	0.786	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	0.786	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	0.786	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	0.782	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC4899521 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC57505 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC12503850 ZINC	0.776	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.776	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.776	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.776	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833 ZINC	0.764	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.764	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.764	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.764	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC2566035 ZINC	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC6864822 ZINC	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC31475423 ZINC	0.750	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC31539924 ZINC	0.747	494.4 Da LogP -0.74 TPSA 218.2	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OC(=O…`
ZINC13434883 ZINC	0.746	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@@](=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.