Protein target profile

KP13_01784

Prolyl-tRNA synthetase

Genome: KpKP13 Gene: AHE46224.1 proS 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GS78

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Length 572

Pocket druggability 0.725

Direct ligand evidence 0 81 total records

Functional annotation 1 EC 9 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 0.72, P2Rank 0.92). 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 0.72. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.92. 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 (%): 45.575 Lower values reduce human off-target concern.
Human E-value: 6.860000000000001e-64
Gut microbiome similarity: 8.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 94.755 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: 95.43 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 0.725

Structure A0A0H3GS78

Pocket Pocket 1

P2Rank 0.924

Structure A0A0H3GS78

Pocket Pocket 1

ColabFold model

FPocket 0.415 · Pocket 20

P2Rank 0.876 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 405 / 4744 genomes with a hit

Prevalence 8.5%

Cross-references

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

Sequence

UniProt A0A0H3GS78

Chemistry

ChEMBL 1B3 ChEMBL CHEMBL2311925 ChEMBL CHEMBL2311926 ChEMBL CHEMBL2311924 ChEMBL 409 ChEMBL CHEMBL2316966 ChEMBL CHEMBL2311928 ChEMBL P5A ChEMBL CHEMBL2311927 ChEMBL CHEMBL2311919 ChEMBL X16 ChEMBL CHEMBL2311917 ChEMBL CHEMBL2316967 ChEMBL CHEMBL2311922 ChEMBL CHEMBL2311929 ChEMBL CHEMBL2316963 ChEMBL CHEMBL2316960 ChEMBL CHEMBL2311923 ChEMBL 1B2 ChEMBL CHEMBL2316962 ChEMBL CHEMBL5279127

Sequence

Primary amino-acid sequence viewer.

MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGVRVLKKVENIVREEMNNAGAIEVLMPVVQPSELWQESGRWEQYGPELLRIADRGDRPFVLGPTHEEVITDLIRNELNSYKQLPLNFYQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESLQETYDAMYAAYSKIFSRMGLDFRAVQADTGSIGGSASHEFQVLAQSGEDDVIFSDSSDYAANIEFAEAVAPKEPRAAATQEMTLVDTPNAKTIAELVEQFNLPIEKTVKTLLVKAVEDSASPLVALLVRGDHELNEVKAEKLPQVASPLTFATEEEIRALVNAGPGSLGPVNMPVPVIIDRTVAVMSDFAAGANIDGKHYFGINWDRDVATPEVADIRNVVAGDPSPDGKGTLLIKRGIEVGHIFQLGTKYSEAMKAAVQGEDGRNQILTMGCYGIGVTRVVAAAIEQNFDDRGIVWPDAIAPFQVAILPMNMHKSYRVQELAEKLYAELSAQGIEVLMDDRKERPGVMFADMELIGIPHTIVLGDRNLDNDDIEYKYRRNGEKQLIKTGDIVEYLVKAIKG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

6.1.1.15

Gene Ontology (GO)

GO:0004827 Catalysis of the reaction: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
GO:0002161 The hydrolysis of an incorrectly aminoacylated tRNA.
GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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: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:0006433 The process of coupling proline to prolyl-tRNA, catalyzed by prolyl-tRNA synthetase. The prolyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a methionine-accetping tRNA.
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.

45 records

Show feature table

Start	End	DB	Term	Name
95	459	Pfam	PF00587	tRNA synthetase class II core domain (G, H, P, S and T)
95	459	InterPro	IPR002314	Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
388	467	Gene3D	G3DSA:3.30.930.10	Bira Bifunctional Protein; Domain 2
388	467	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
1	572	PIRSF	PIRSF001535	ProRS_1
1	572	InterPro	IPR023717	Prolyl-tRNA synthetase, class IIa, type 1
1	571	Hamap	MF_01569	Proline--tRNA ligase [proS].
1	571	InterPro	IPR023717	Prolyl-tRNA synthetase, class IIa, type 1
242	387	Gene3D	G3DSA:3.90.960.10	-
242	387	InterPro	IPR036754	YbaK/aminoacyl-tRNA synthetase-associated domain superfamily
219	390	SUPERFAMILY	SSF55826	YbaK/ProRS associated domain
219	390	InterPro	IPR036754	YbaK/aminoacyl-tRNA synthetase-associated domain superfamily
342	460	FunFam	G3DSA:3.30.930.10:FF:000097	Proline--tRNA ligase
1	568	NCBIfam	TIGR00409	proline--tRNA ligase
1	568	InterPro	IPR004500	Prolyl-tRNA synthetase, class IIa, bacterial-type
473	567	CDD	cd00861	ProRS_anticodon_short
473	567	InterPro	IPR044140	Proline--tRNA ligase, anticodon binding domain
226	387	CDD	cd04334	ProRS-INS
2	568	PANTHER	PTHR42753	MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER
10	478	SUPERFAMILY	SSF55681	Class II aaRS and biotin synthetases
10	478	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
3	241	Gene3D	G3DSA:3.30.930.10	Bira Bifunctional Protein; Domain 2
3	241	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
257	376	Pfam	PF04073	Aminoacyl-tRNA editing domain
257	376	InterPro	IPR007214	YbaK/aminoacyl-tRNA synthetase-associated domain
134	142	PRINTS	PR01046	Prolyl-tRNA synthetase signature
134	142	InterPro	IPR002316	Proline-tRNA ligase, class IIa
68	86	PRINTS	PR01046	Prolyl-tRNA synthetase signature
68	86	InterPro	IPR002316	Proline-tRNA ligase, class IIa
144	155	PRINTS	PR01046	Prolyl-tRNA synthetase signature
144	155	InterPro	IPR002316	Proline-tRNA ligase, class IIa
104	115	PRINTS	PR01046	Prolyl-tRNA synthetase signature
104	115	InterPro	IPR002316	Proline-tRNA ligase, class IIa
244	386	FunFam	G3DSA:3.90.960.10:FF:000001	Proline--tRNA ligase
468	566	Gene3D	G3DSA:3.40.50.800	-
468	566	InterPro	IPR036621	Anticodon-binding domain superfamily
38	468	ProSiteProfiles	PS50862	Aminoacyl-transfer RNA synthetases class-II family profile.
38	468	InterPro	IPR006195	Aminoacyl-tRNA synthetase, class II
15	303	FunFam	G3DSA:3.30.930.10:FF:000043	Proline--tRNA ligase
462	571	SUPERFAMILY	SSF52954	Class II aaRS ABD-related
475	567	Pfam	PF03129	Anticodon binding domain
475	567	InterPro	IPR004154	Anticodon-binding
17	458	CDD	cd00779	ProRS_core_prok
17	458	InterPro	IPR033730	Prokaryote proline-tRNA ligase core domain
468	566	FunFam	G3DSA:3.40.50.800:FF:000006	Proline--tRNA ligase

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

0.725

Likely same site as P2Rank 1 3.8 Å 21 shared residues 88% of smaller site

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Surrounding area

Site 2 FPocket #2

0.548

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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

0.924

Likely same site as FPocket 1 3.8 Å 21 shared residues 88% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.142

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Surrounding area

Site 3 P2Rank #3

0.037

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Surrounding area

Site 4 P2Rank #4

0.03

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Surrounding area

Site 5 P2Rank #5

0.016

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #20

0.415

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Surrounding area

Site 2 FPocket #7

0.383

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Surrounding area

Site 3 FPocket #1

0.367

Likely same site as P2Rank 1 2.3 Å 25 shared residues 100% 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

0.876

Likely same site as FPocket 1 2.3 Å 25 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.143

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Surrounding area

Site 3 P2Rank #3

0.106

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Surrounding area

Site 4 P2Rank #4

0.036

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Surrounding area

Site 5 P2Rank #5

0.023

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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_A0A0H3GS78	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01784	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.

81 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 31 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 21 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5CA PDB via homolog 449.5 Da · LogP -3.34 · TPSA 217.8 Open detail RCSB PDB

86U PDB via homolog Detail RCSB PDB

86X PDB via homolog Detail RCSB PDB

873 PDB via homolog Detail RCSB PDB

87C 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
5CA RCSB PDB	1NJ1	O26708	449.5 Da LogP -3.34 TPSA 217.8	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
86U RCSB PDB	5XIH	S8G8I1	321.3 Da LogP 1.78 TPSA 64.0	✓ Ro5	✓ Clean	`c1c2c(cc(c1F)F)N=CN(C2=O)CCC[C@@H]3C(=O)CCCN3`
86X RCSB PDB	5XII	S8G8I1	337.8 Da LogP 2.29 TPSA 64.0	✓ Ro5	✓ Clean	`c1c2c(cc(c1Cl)F)N=CN(C2=O)CCC[C@@H]3C(=O)CCCN3`
873 RCSB PDB	5XIJ	S8G8I1	303.4 Da LogP 0.26 TPSA 87.4	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=O)N(C=N2)C[C@@H](C[C@@H]3[C@@H](C…`
87C RCSB PDB	5XIK	S8G8I1	305.4 Da LogP 0.19 TPSA 84.2	✓ Ro5	✓ Clean	`C1CCC2=C(C1)C(=O)N(C=N2)CC(=O)C[C@@H]3[C@@H](CC…`
87F RCSB PDB	5XIG	S8G8I1	285.3 Da LogP 1.50 TPSA 64.0	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=O)N(C=N2)CCC[C@@H]3C(=O)CCCN3`
9SF RCSB PDB	6A88	S8G8I1	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=O)N(C=N2)CC(=O)C[C@@H]3[C@H](CCCN…`
A5A RCSB PDB	1NJ6	O26708	417.4 Da LogP -3.25 TPSA 217.8	1 viol.	✓ Clean	`C[C@@H](C(=O)NS(=O)(=O)OC[C@@H]1[C@H]([C@H]([C@…`
ANP RCSB PDB	6UYH	A0A4V8H034	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
HFG RCSB PDB	6UYH	A0A4V8H034	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`c1c2c(cc(c1Cl)Br)N=CN(C2=O)CC(=O)C[C@@H]3[C@H](…`

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
1B3 ChEMBL	Q8ZDW5	9.15 ~0.7 nM	435.9 Da LogP 1.05 TPSA 161.3	✓ Ro5	✓ Clean	`C[C@H]([C@@H](C(=O)NS(=O)(=O)c1cccc(c1)c2ccc3c(…`
CHEMBL2311925 ChEMBL	Q8ZDW5	8.74 ~1.8 nM	377.4 Da LogP -0.15 TPSA 161.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)/C=C/c1cccc(-c…`
CHEMBL2311926 ChEMBL	Q8ZDW5	8.74 ~1.8 nM	425.5 Da LogP 1.29 TPSA 151.1	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)c1ccc2ccc(-c3n…`
CHEMBL2311924 ChEMBL	Q8ZDW5	8.70 ~2.0 nM	401.4 Da LogP 0.39 TPSA 161.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)c1ccc2ccc(-c3c…`
409 ChEMBL	Q8ZDW5	8.66 ~2.2 nM	401.4 Da LogP 0.39 TPSA 161.3	✓ Ro5	✓ Clean	`C[C@H]([C@@H](C(=O)NS(=O)(=O)c1cccc(c1)c2ccc3c(…`
CHEMBL2316966 ChEMBL	Q8ZDW5	8.57 ~2.7 nM	391.5 Da LogP 0.24 TPSA 161.3	✓ Ro5	✓ Clean	`CC[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)/C=C/c1cccc(-…`
CHEMBL2311928 ChEMBL	Q8ZDW5	8.41 ~3.9 nM	389.4 Da LogP 0.11 TPSA 138.6	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)c1cccc(-c2ccc3…`
P5A ChEMBL	P16659	8.37 ~4.3 nM	443.4 Da LogP -2.84 TPSA 203.8	1 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CHEMBL2311927 ChEMBL	Q8ZDW5	8.24 ~5.8 nM	430.5 Da LogP 0.05 TPSA 154.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)N1CCc2ccc(-c3n…`
CHEMBL2311919 ChEMBL	Q8ZDW5	8.09 ~8.1 nM	416.5 Da LogP -0.03 TPSA 187.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)c1cccc(-c2ccc3…`
X16 ChEMBL	Q8ZDW5	8.03 ~9.3 nM	415.5 Da LogP 0.70 TPSA 161.3	✓ Ro5	✓ Clean	`Cc1nc2cc(ccc2c(n1)N)c3cccc(c3)S(=O)(=O)NC(=O)[C…`
CHEMBL2311917 ChEMBL	Q8ZDW5	8.01 ~9.8 nM	447.4 Da LogP -3.89 TPSA 238.0	2 viol.	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C@H…`
CHEMBL2316967 ChEMBL	Q8ZDW5	7.65 ~22.4 nM	405.5 Da LogP 0.49 TPSA 161.3	✓ Ro5	✓ Clean	`CC(C)[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)/C=C/c1ccc…`
CHEMBL2311922 ChEMBL	Q8ZDW5	7.60 ~25.1 nM	434.9 Da LogP 1.65 TPSA 148.4	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)c1cccc(-c2ccc3…`
CHEMBL2311929 ChEMBL	Q8ZDW5	7.41 ~38.9 nM	408.9 Da LogP 1.40 TPSA 138.2	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)c1cccc(-c2ccc3…`
CHEMBL2316963 ChEMBL	Q8ZDW5	7.16 ~69.2 nM	386.8 Da LogP 1.68 TPSA 139.2	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NNc1cccc(-c2ccc3c(N)nc(C…`
CHEMBL2316960 ChEMBL	Q8ZDW5	7.08 ~83.2 nM	388.4 Da LogP 1.05 TPSA 138.2	✓ Ro5	✓ Clean	`Cc1n[nH]c2ccc(-c3cccc(S(=O)(=O)NC(=O)[C@@H](N)[…`
CHEMBL2311923 ChEMBL	Q8ZDW5	6.94 ~114.8 nM	400.5 Da LogP 1.00 TPSA 148.4	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NS(=O)(=O)c1cccc(-c2ccc3…`
1B2 ChEMBL	Q8ZDW5	6.88 ~131.8 nM	374.4 Da LogP 0.74 TPSA 138.2	✓ Ro5	✓ Clean	`C[C@H]([C@@H](C(=O)NS(=O)(=O)c1cccc(c1)c2ccc3c(…`
CHEMBL2316962 ChEMBL	Q8ZDW5	6.36 ~436.5 nM	385.9 Da LogP 1.86 TPSA 127.1	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)NCc1cccc(-c2ccc3c(N)nc(C…`
CHEMBL5279127 ChEMBL	P16659	6.31 ~489.8 nM	443.4 Da LogP -2.84 TPSA 203.8	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(=O)(=O)NC(=O)[C…`

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
ZINC1571579 ZINC	1.000	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C@@H]1O)Cn1cnc2ccccc2c1=O`
ZINC1571580 ZINC	1.000	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C@H]1O)Cn1cnc2ccccc2c1=O`
ZINC1571581 ZINC	1.000	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@H]1O)Cn1cnc2ccccc2c1=O`
ZINC1849658 ZINC	1.000	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C@@H]1O)Cn1cnc2cc(Br)c(Cl)cc2c…`
ZINC1849659 ZINC	1.000	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C@H]1O)Cn1cnc2cc(Br)c(Cl)cc2c1…`
ZINC1849660 ZINC	1.000	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@H]1O)Cn1cnc2cc(Br)c(Cl)cc2c1=O`
ZINC5641945 ZINC	1.000	301.3 Da LogP 0.47 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@@H]1O)Cn1cnc2ccccc2c1=O`
ZINC5784191 ZINC	1.000	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@@H]1O)Cn1cnc2cc(Br)c(Cl)cc2c1…`
ZINC1849460 ZINC	0.927	414.7 Da LogP 1.88 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1NCCC[C@H]1O)Cn1cnc2cc(Cl)c(Br)cc2c1=O`
ZINC14967098 ZINC	0.706	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033334 ZINC	0.706	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033425 ZINC	0.706	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC218033503 ZINC	0.706	403.4 Da LogP -3.64 TPSA 217.8	1 viol.	✓ Clean	`NCC(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc…`
ZINC1560411656 ZINC	0.698	413.7 Da LogP 2.43 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C@@H]1NCCC[C]1O)Cn1cnc2cc(Br)c(Cl)cc2c1=O`
ZINC526061700 ZINC	0.698	300.4 Da LogP 1.91 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(C[C@H]1CCCC[C@@H]1O)Cn1cnc2ccccc2c1=O`
ZINC240894758 ZINC	0.679	272.3 Da LogP 2.34 TPSA 55.1	✓ Ro5	✓ Clean	`O=c1c2ccccc2ncn1C[C@H](O)CC1CCCC1`
ZINC240894759 ZINC	0.679	272.3 Da LogP 2.34 TPSA 55.1	✓ Ro5	✓ Clean	`O=c1c2ccccc2ncn1C[C@@H](O)CC1CCCC1`
ZINC1560406176 ZINC	0.679	300.3 Da LogP 0.63 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(C[C]1NCCC[C@@H]1O)Cn1cnc2ccccc2c1=O`
ZINC1083817667 ZINC	0.649	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC(C)C[C@@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](n…`
ZINC936069043 ZINC	0.649	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C…`
ZINC936069053 ZINC	0.649	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC(C)C[C@@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C@H](n…`
ZINC12405780 ZINC	0.646	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@@H]…`
ZINC12502832 ZINC	0.646	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@@H]…`
ZINC79460727 ZINC	0.646	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`
ZINC79460732 ZINC	0.646	346.3 Da LogP -2.75 TPSA 188.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(N)(=O)=O)[C@H](…`
ZINC168710640 ZINC	0.640	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC168710738 ZINC	0.640	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC1560404579 ZINC	0.615	412.7 Da LogP 2.92 TPSA 84.2	✓ Ro5	✓ Clean	`O=C(CC1=C(O)CCCN1)Cn1cnc2cc(Br)c(Cl)cc2c1=O`
ZINC1240209978 ZINC	0.596	272.3 Da LogP 2.63 TPSA 62.8	✓ Ro5	✓ Clean	`CS(=O)(=O)c1cccc(-c2ccc3n[nH]cc3c2)c1`
ZINC1574270 ZINC	0.589	421.4 Da LogP -0.26 TPSA 162.7	1 viol.	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@@H]2O[C@H](n3cnc4c(N)ncnc4…`
ZINC3861767 ZINC	0.589	421.4 Da LogP -0.26 TPSA 162.7	1 viol.	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@H]2O[C@@H](n3cnc4c(N)ncnc4…`
ZINC12921014 ZINC	0.587	332.4 Da LogP 2.20 TPSA 69.8	✓ Ro5	✓ Clean	`O=c1c2ccccc2ncn1CCCn1cnc2ccccc2c1=O`
ZINC3851415 ZINC	0.587	346.4 Da LogP 2.59 TPSA 69.8	✓ Ro5	✓ Clean	`O=c1c2ccccc2ncn1CCCCn1cnc2ccccc2c1=O`
ZINC406602 ZINC	0.586	301.4 Da LogP 1.68 TPSA 67.2	✓ Ro5	✓ Clean	`O=c1c2ccccc2ncn1C[C@H](O)CNC1CCCCC1`
ZINC5739636 ZINC	0.586	301.4 Da LogP 1.68 TPSA 67.2	✓ Ro5	✓ Clean	`O=c1c2ccccc2ncn1C[C@@H](O)CNC1CCCCC1`
ZINC58201920 ZINC	0.583	300.3 Da LogP -0.21 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(Cn1cnc2ccccc2c1=O)N[C@@H]1CCCNC1=O`
ZINC58201921 ZINC	0.583	300.3 Da LogP -0.21 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(Cn1cnc2ccccc2c1=O)N[C@H]1CCCNC1=O`
ZINC13547650 ZINC	0.574	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)…`
ZINC4823971 ZINC	0.574	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC4823975 ZINC	0.574	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC4823980 ZINC	0.574	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC4823984 ZINC	0.574	309.3 Da LogP -1.41 TPSA 145.6	✓ Ro5	✓ Clean	`CC(=O)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](…`
ZINC24951137 ZINC	0.560	417.4 Da LogP -2.41 TPSA 221.3	1 viol.	✓ Clean	`C[C@H](N)/C(O)=N/S(=O)(=O)OC[C@H]1O[C@@H](n2cnc…`
ZINC71825029 ZINC	0.559	301.4 Da LogP 1.49 TPSA 58.4	✓ Ro5	✓ Clean	`CC1CCN(C[C@H](O)Cn2cnc3ccccc3c2=O)CC1`
ZINC71825030 ZINC	0.559	301.4 Da LogP 1.49 TPSA 58.4	✓ Ro5	✓ Clean	`CC1CCN(C[C@@H](O)Cn2cnc3ccccc3c2=O)CC1`
ZINC14967079 ZINC	0.558	461.4 Da LogP -2.95 TPSA 258.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(=O)(=O)/N=C(\O)…`
ZINC63856830 ZINC	0.558	240.2 Da LogP 1.06 TPSA 55.1	✓ Ro5	✓ Clean	`O=c1c2cc(F)c(F)cc2ncn1CCCO`
ZINC6086732 ZINC	0.554	271.3 Da LogP 1.46 TPSA 64.0	✓ Ro5	✓ Clean	`O=C(Cn1cnc2ccccc2c1=O)NC1CCCC1`
ZINC7268731 ZINC	0.554	272.3 Da LogP -0.05 TPSA 84.3	✓ Ro5	✓ Clean	`O=C(Cn1cnc2ccccc2c1=O)N1CCNC1=O`
ZINC40351417 ZINC	0.551	208.2 Da LogP 0.21 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(O)Cn1cnc2c(c1=O)CCCC2`

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.