Protein target profile

KP13_01719

ATP-dependent DNA helicase recQ

Genome: KpKP13 Gene: AHE46977.1 recQ 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GKF3

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Length 608

Pocket druggability 0.635

Direct ligand evidence 0 78 total records

Functional annotation 1 EC 18 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 0.64. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.95. 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 (%): 55.102 Lower values reduce human off-target concern.
Human E-value: 7.66e-13
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 63.744 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: 89.38 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 0.635

Structure A0A0H3GKF3

Pocket Pocket 10

P2Rank 0.948

Structure A0A0H3GKF3

Pocket Pocket 1

ColabFold model

FPocket 0.843 · Pocket 10

P2Rank 0.862 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 140 / 4744 genomes with a hit

Prevalence 3.0%

Cross-references

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

Sequence

UniProt A0A0H3GKF3

Chemistry

ChEMBL CHEMBL1399702 ChEMBL CHEMBL1608159 ChEMBL 5AE ChEMBL CHEMBL1590552 ChEMBL MZR ChEMBL CHEMBL316966 ChEMBL CHEMBL1395737 ChEMBL CHEMBL1394945 ChEMBL CHEMBL1436882 ChEMBL CHEMBL1475917 ChEMBL CHEMBL1596388 ChEMBL CHEMBL1231330 ChEMBL CHEMBL1457622 ChEMBL CHEMBL1471192 ChEMBL CHEMBL18238 ChEMBL CHEMBL1560762 ChEMBL CHEMBL1442153 ChEMBL CHEMBL1446521 ChEMBL CHEMBL1554131 ChEMBL CHEMBL64239 ChEMBL CHEMBL1448630 ChEMBL CHEMBL1057 ChEMBL CHEMBL119171 ChEMBL CHEMBL1715183

Sequence

Primary amino-acid sequence viewer.

MAQAEVLNQESLAKQVLQETFGYQQFRPGQETIIETALEGRDCLVVMPTGGGKSLCYQVPALVMGGLTVVVSPLISLMKDQVDQLLANGVAAACLNSTQSREQQQEVMAGCRSGQVRLLYIAPERLMLDNFLEHLANWNLAMLAVDEAHCISQWGHDFRPEYAALGQLRQRMPQIPFMALTATADDTTRRDIVRLLGLNDPLIQVSSFDRPNIRYMLMEKFKPLDQLMRYVQDQRGKSGIIYCNSRSKVEDTAARLQSRGISAAAYHAGLENDVRAEVQEKFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGPLQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQYDGLMDARKALSTIYRVNQRFGMGYVVEVLRGANNQRIREMGHDKLPVYGIGREQSHEHWVSVIRQLIHLGLVTQNIAQHSALQLTEAARPVLRGEVPLQLAVPRIVALKPKAMQKSFGGNYDRKLFAKLRKLRKAIADEENIPPYVVFNDATLIEMAEQSPLTAGEMLSVNGVGTRKLERFGKPFMALIRAHVDGDDE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 18 GO

Enzyme Commission (EC)

5.6.2.4

Gene Ontology (GO)

GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.
GO:0004386 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0043138 Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis.
GO:0009432 An error-prone process for repairing damaged microbial DNA.
GO:0003676 Binding to a nucleic acid.
GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
GO:0006310 Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
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:0043590 The region of a bacterial cell to which the DNA is confined.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0030894 A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0009378 Unwinding a DNA helix of DNA containing four-way junctions, including Holliday junctions, driven by ATP hydrolysis.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

48 records

Show feature table

Start	End	DB	Term	Name
529	608	ProSiteProfiles	PS50967	HRDC domain profile.
529	608	InterPro	IPR002121	HRDC domain
2	208	Gene3D	G3DSA:3.40.50.300	-
2	208	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
341	522	Gene3D	G3DSA:1.10.10.10	-
341	522	InterPro	IPR036388	Winged helix-like DNA-binding domain superfamily
223	371	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
223	371	InterPro	IPR001650	Helicase, C-terminal
8	201	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
8	201	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
28	187	Pfam	PF00270	DEAD/DEAH box helicase
28	187	InterPro	IPR011545	DEAD/DEAH box helicase domain
529	608	SMART	SM00341	hrdc7
1	209	FunFam	G3DSA:3.40.50.300:FF:000296	ATP-dependent DNA helicase RecQ
526	606	FunFam	G3DSA:1.10.150.80:FF:000002	ATP-dependent DNA helicase RecQ
530	605	SUPERFAMILY	SSF47819	HRDC-like
530	605	InterPro	IPR010997	HRDC-like superfamily
210	340	FunFam	G3DSA:3.40.50.300:FF:000156	ATP-dependent DNA helicase recQ
13	592	PANTHER	PTHR13710	DNA HELICASE RECQ FAMILY MEMBER
15	464	NCBIfam	TIGR00614	RecQ family ATP-dependent DNA helicase
15	464	InterPro	IPR004589	DNA helicase, ATP-dependent, RecQ type
210	340	CDD	cd18794	SF2_C_RecQ
34	202	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
34	202	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
523	608	Gene3D	G3DSA:1.10.150.80	HRDC domain
523	608	InterPro	IPR044876	HRDC domain superfamily
223	330	Pfam	PF00271	Helicase conserved C-terminal domain
223	330	InterPro	IPR001650	Helicase, C-terminal
533	599	Pfam	PF00570	HRDC domain
533	599	InterPro	IPR002121	HRDC domain
343	404	Pfam	PF16124	RecQ zinc-binding
343	404	InterPro	IPR032284	ATP-dependent DNA helicase RecQ, zinc-binding domain
406	514	Pfam	PF09382	RQC domain
406	514	InterPro	IPR018982	RQC domain
22	218	SMART	SM00487	ultradead3
22	218	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
411	514	SMART	SM00956	RQC_2
411	514	InterPro	IPR018982	RQC domain
14	209	CDD	cd17920	DEXHc_RecQ
13	601	NCBIfam	TIGR01389	DNA helicase RecQ
13	601	InterPro	IPR006293	DNA helicase, ATP-dependent, RecQ type, bacterial
209	340	Gene3D	G3DSA:3.40.50.300	-
209	340	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
341	522	FunFam	G3DSA:1.10.10.10:FF:000175	ATP-dependent DNA helicase RecQ
250	331	SMART	SM00490	helicmild6
250	331	InterPro	IPR001650	Helicase, C-terminal
208	455	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
208	455	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase

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 #10

0.635

Likely same site as P2Rank 2 0.7 Å 19 shared residues 95% 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

0.948

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Surrounding area

Site 2 P2Rank #2

0.323

Likely same site as FPocket 10 0.7 Å 19 shared residues 95% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.093

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Surrounding area

Site 4 P2Rank #4

0.088

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Surrounding area

Site 5 P2Rank #5

0.055

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #10

0.843

Likely same site as P2Rank 2 2.1 Å 15 shared residues 88% of smaller site

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Surrounding area

Site 2 FPocket #3

0.773

Likely same site as P2Rank 3 3.6 Å 14 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

0.862

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Surrounding area

Site 2 P2Rank #2

0.425

Likely same site as FPocket 10 2.1 Å 15 shared residues 88% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.09

Likely same site as FPocket 3 3.6 Å 14 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.056

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Surrounding area

Site 5 P2Rank #5

0.055

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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_A0A0H3GKF3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01719	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.

78 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 28 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 24 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

6SV PDB via homolog 226.3 Da · LogP 1.80 · TPSA 50.4 Open detail RCSB PDB

AGS PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

EU3 PDB via homolog Detail RCSB PDB

CHEMBL1399702 ChEMBL via homolog · pchembl 8.96 (~1.1 nM) Detail ChEMBL

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
6SV RCSB PDB	5LBA	O94762	226.3 Da LogP 1.80 TPSA 50.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NC(=O)NC[C@H]2CCCO2`
AGS RCSB PDB	1OYY	P15043	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP RCSB PDB	4D25	O01378	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)…`
EU3 RCSB PDB	2FBY	Q14191	152.0 Da LogP 0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Eu+3]`

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
CHEMBL1399702 ChEMBL	P54132	8.96 ~1.1 nM	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@H](O)[C@@H]1O`
CHEMBL1608159 ChEMBL	P54132	8.96 ~1.1 nM	629.6 Da LogP -15.49 TPSA 290.4	2 viol.	✓ Clean	`Nc1nc(Cl)nc2c1ncn2[C@@H]1O[C@H](COP(=O)([O-])OP…`
5AE ChEMBL	P54132	8.80 ~1.6 nM	244.2 Da LogP -3.17 TPSA 143.7	✓ Ro5	✓ Clean	`C1=NC(=NC(=O)N1[C@H]2[C@@H]([C@@H]([C@H](O2)CO)…`
CHEMBL1590552 ChEMBL	P54132	8.55 ~2.8 nM	641.2 Da LogP -15.42 TPSA 290.4	2 viol.	✓ Clean	`CSc1nc(N)c2ncn([C@@H]3O[C@H](COP(=O)([O-])OP(=O…`
MZR ChEMBL	P54132	8.55 ~2.8 nM	259.2 Da LogP -2.70 TPSA 151.1	✓ Ro5	✓ Clean	`c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)CO)O)O)O)…`
CHEMBL316966 ChEMBL	P54132	8.46 ~3.5 nM	329.2 Da LogP -0.82 TPSA 154.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H]2COP(=O)(O)O[C@H]2[…`
CHEMBL1395737 ChEMBL	P54132	8.30 ~5.0 nM	399.4 Da LogP -0.61 TPSA 160.4	✓ Ro5	Alert	`CNC(=O)[C@H]1O[C@@H](n2cnc3c(NCc4ccc(N)cc4)ncnc…`
CHEMBL1394945 ChEMBL	P54132	8.05 ~8.9 nM	361.4 Da LogP 0.04 TPSA 125.6	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3c(N[C@H]4CC5CCC4C5)ncnc32…`
CHEMBL1436882 ChEMBL	P54132	8.00 ~10.0 nM	358.4 Da LogP -0.24 TPSA 151.6	✓ Ro5	✓ Clean	`Nc1nc(Nc2ccccc2)nc2c1ncn2[C@@H]1O[C@H](CO)[C@H]…`
CHEMBL1475917 ChEMBL	P54132	7.90 ~12.6 nM	419.4 Da LogP 0.64 TPSA 156.7	1 viol.	✓ Clean	`O=[N+]([O-])c1ccc(CSc2ncnc3c2ncn3[C@@H]2O[C@H](…`
CHEMBL1596388 ChEMBL	P54132	7.60 ~25.1 nM	781.5 Da LogP -6.62 TPSA 353.4	3 viol.	✓ Clean	`NC(=S)c1ccc[n+]([C@@H]2O[C@@H](COP(=O)([O-])OP(…`
CHEMBL1231330 ChEMBL	P54132	7.55 ~28.2 nM	149.1 Da LogP -2.16 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](C(=O)O)[C@H](O)C(=O)O`
CHEMBL1457622 ChEMBL	P54132	7.45 ~35.5 nM	448.1 Da LogP -9.87 TPSA 223.5	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)([O-])OP(=O)([O-])…`
CHEMBL1471192 ChEMBL	P46063	7.25 ~56.2 nM	451.6 Da LogP 1.73 TPSA 104.8	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)NCC(=O)N(CC(=O)NC2CCCCC2)CC2CCC…`
CHEMBL18238 ChEMBL	P54132	7.15 ~70.8 nM	371.4 Da LogP 0.36 TPSA 125.6	✓ Ro5	✓ Clean	`Cc1ccccc1CNc1ncnc2c1ncn2C1OC(CO)C(O)C1O`
CHEMBL1560762 ChEMBL	P46063	6.85 ~141.3 nM	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NCC1CCCO1`
CHEMBL1442153 ChEMBL	P54132	6.50 ~316.2 nM	294.3 Da LogP -2.23 TPSA 148.4	✓ Ro5	✓ Clean	`CNC(=O)[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[…`
CHEMBL1446521 ChEMBL	P46063	6.50 ~316.2 nM	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NCC3CCCO3)n2C)cc1`
CHEMBL1554131 ChEMBL	P54132	6.45 ~354.8 nM	281.3 Da LogP -1.52 TPSA 125.6	✓ Ro5	✓ Clean	`CNc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
CHEMBL64239 ChEMBL	P54132	6.40 ~398.1 nM	205.2 Da LogP 0.72 TPSA 78.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2C1CCCO1`
CHEMBL1448630 ChEMBL	P46063	6.05 ~891.3 nM	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NCC2CCCO2)cc1`
CHEMBL1057 ChEMBL	P46063	—	332.3 Da LogP 3.67 TPSA 76.0	✓ Ro5	✓ Clean	`O=C1OC2(c3ccc(O)cc3Oc3cc(O)ccc32)c2ccccc21`
CHEMBL119171 ChEMBL	Q14191	—	299.3 Da LogP -1.69 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(S)c2ncn(C3OC(CO)C(O)C3O)c2n1`
CHEMBL1715183 ChEMBL	Q14191	—	803.9 Da LogP 4.01 TPSA 236.7	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCNc1ccn(C2OC(COP(=O)(O)OCC3OC(…`

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
ZINC316109 ZINC	1.000	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NC[C@H]2CCCO2)cc1`
ZINC316110 ZINC	1.000	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NC[C@@H]2CCCO2)cc1`
ZINC3286414 ZINC	1.000	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)cc1`
ZINC3286415 ZINC	1.000	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)cc1`
ZINC3860453 ZINC	1.000	332.3 Da LogP 3.67 TPSA 76.0	✓ Ro5	✓ Clean	`O=C1OC2(c3ccc(O)cc3Oc3cc(O)ccc32)c2ccccc21`
ZINC46867 ZINC	1.000	226.3 Da LogP 1.80 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(NC[C@H]1CCCO1)NC1CCCCC1`
ZINC46868 ZINC	1.000	226.3 Da LogP 1.80 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(NC[C@@H]1CCCO1)NC1CCCCC1`
ZINC798668 ZINC	1.000	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@H]1CCCO1`
ZINC798669 ZINC	1.000	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@@H]1CCC…`
ZINC804908 ZINC	0.979	382.5 Da LogP 1.58 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCC2)cc1)NC[C@H]1CCCO1`
ZINC804909 ZINC	0.979	382.5 Da LogP 1.58 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCC2)cc1)NC[C@@H]1CCCO1`
ZINC30984714 ZINC	0.968	212.3 Da LogP 1.41 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(NC[C@@H]1CCCO1)NC1CCCC1`
ZINC30984716 ZINC	0.968	212.3 Da LogP 1.41 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(NC[C@H]1CCCO1)NC1CCCC1`
ZINC3485814 ZINC	0.870	366.9 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(Cl)cc1`
ZINC3485816 ZINC	0.870	366.9 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(Cl)cc1`
ZINC6914139 ZINC	0.870	350.4 Da LogP 2.01 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(F)cc1`
ZINC6914143 ZINC	0.870	350.4 Da LogP 2.01 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(F)cc1`
ZINC12360002 ZINC	0.855	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	0.855	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	0.855	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	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC3402375 ZINC	0.855	388.5 Da LogP 3.17 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(C(C)(C)C)c…`
ZINC3402380 ZINC	0.855	388.5 Da LogP 3.17 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(C(C)(C)C)…`
ZINC4806433 ZINC	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC43199396 ZINC	0.842	331.3 Da LogP 3.54 TPSA 81.8	✓ Ro5	✓ Clean	`Nc1ccc2c(c1)Oc1cc(O)ccc1[C@]21OC(=O)c2ccccc21`
ZINC43199397 ZINC	0.842	331.3 Da LogP 3.54 TPSA 81.8	✓ Ro5	✓ Clean	`Nc1ccc2c(c1)Oc1cc(O)ccc1[C@@]21OC(=O)c2ccccc21`
ZINC880963 ZINC	0.839	362.5 Da LogP 1.88 TPSA 78.3	✓ Ro5	✓ Clean	`COc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)cc1`
ZINC880965 ZINC	0.839	362.5 Da LogP 1.88 TPSA 78.3	✓ Ro5	✓ Clean	`COc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)cc1`
ZINC26662657 ZINC	0.833	254.2 Da LogP -0.59 TPSA 93.3	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@@H](F)[C@@H]1O`
ZINC2207000 ZINC	0.810	403.5 Da LogP 2.22 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(=O)Nc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)c…`
ZINC2207001 ZINC	0.810	403.5 Da LogP 2.22 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(=O)Nc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)…`
ZINC62065644 ZINC	0.800	228.3 Da LogP 0.64 TPSA 59.6	✓ Ro5	✓ Clean	`O=C(NC[C@H]1CCCO1)NC1CCOCC1`
ZINC62065645 ZINC	0.800	228.3 Da LogP 0.64 TPSA 59.6	✓ Ro5	✓ Clean	`O=C(NC[C@@H]1CCCO1)NC1CCOCC1`
ZINC212148859 ZINC	0.791	254.2 Da LogP -0.59 TPSA 93.3	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@H](O)[C@@H]1F`
ZINC13518964 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1571045 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC2046931 ZINC	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](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.