Protein target profile

KP13_03557

DNA ligase

Genome: KpKP13 Gene: AHE43363.1 ligA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GVW8

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Length 671

Pocket druggability 0.815

Direct ligand evidence 0 60 total records

Functional annotation 1 EC 6 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 0.81, P2Rank 0.87). 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 0.81. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.87. 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 (%): 42.254 Lower values reduce human off-target concern.
Human E-value: 4.52e-08
Gut microbiome similarity: 4.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.239 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: 88.98 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 0.815

Structure A0A0H3GVW8

Pocket Pocket 26

P2Rank 0.874

Structure A0A0H3GVW8

Pocket Pocket 1

ColabFold model

FPocket 0.439 · Pocket 10

P2Rank 0.931 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 233 / 4744 genomes with a hit

Prevalence 4.9%

Cross-references

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

Sequence

UniProt A0A0H3GVW8

Chemistry

ChEMBL CHEMBL1807815

Sequence

Primary amino-acid sequence viewer.

MEPIEQQLTELRTTLRHHEYLYHVMDAPEVPDAEYDRLMRKLRELESQHPELITPDSPTQRVGAAPLTAFSQIRHEVPMLSLDNVFDEESFLAFNKRVQDRLKSTDHLTYCCELKLDGLAVSILYENGVLVQAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEVRGEVFLPQAGFEKINEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPASHSARLLQFKAWGLPVSDRVTLCHTPEEVLTYYRKVEEERPHLGFDIDGVVIKVDSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLKIGDKVVIRRAGDVIPQVVNVVLSERPADARDVVFPTHCPVCQSDVERVEGEAVARCTGGLICGAQRKESLKHFVSRRALDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAHFGTLEALEQASIEELQKVPDVGIVVATHTFNFFAEESNRDVIAQLLAEGVRWPAPVVVKAEEIDSPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAEMMRLLGE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

6.5.1.2

Gene Ontology (GO)

GO:0003911 Catalysis of the reaction: NAD+ + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + nicotinamide nucleotide + deoxyribonucleotide(n+m).
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: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:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

62 records

Show feature table

Start	End	DB	Term	Name
115	144	ProSitePatterns	PS01055	NAD-dependent DNA ligase signature 1.
115	144	InterPro	IPR018239	NAD-dependent DNA ligase, active site
317	390	FunFam	G3DSA:2.40.50.140:FF:000012	DNA ligase
1	64	Gene3D	G3DSA:1.10.287.610	Helix hairpin bin
480	499	SMART	SM00278	HhH1_4
480	499	InterPro	IPR003583	Helix-hairpin-helix DNA-binding motif, class 1
512	531	SMART	SM00278	HhH1_4
512	531	InterPro	IPR003583	Helix-hairpin-helix DNA-binding motif, class 1
446	465	SMART	SM00278	HhH1_4
446	465	InterPro	IPR003583	Helix-hairpin-helix DNA-binding motif, class 1
544	563	SMART	SM00278	HhH1_4
544	563	InterPro	IPR003583	Helix-hairpin-helix DNA-binding motif, class 1
407	434	Pfam	PF03119	NAD-dependent DNA ligase C4 zinc finger domain
407	434	InterPro	IPR004149	Zinc-finger, NAD-dependent DNA ligase C4-type
1	64	FunFam	G3DSA:1.10.287.610:FF:000002	DNA ligase
596	668	Pfam	PF00533	BRCA1 C Terminus (BRCT) domain
596	668	InterPro	IPR001357	BRCT domain
446	502	Pfam	PF14520	Helix-hairpin-helix domain
322	398	Pfam	PF03120	NAD-dependent DNA ligase OB-fold domain
322	398	InterPro	IPR004150	NAD-dependent DNA ligase, OB-fold
1	671	PIRSF	PIRSF001604	LigA
1	671	InterPro	IPR001679	NAD-dependent DNA ligase
2	669	Hamap	MF_01588	DNA ligase [ligA].
2	669	InterPro	IPR001679	NAD-dependent DNA ligase
598	668	CDD	cd17748	BRCT_DNA_ligase_like
17	652	PANTHER	PTHR23389	CHROMOSOME TRANSMISSION FIDELITY FACTOR 18
588	670	Gene3D	G3DSA:3.40.50.10190	BRCT domain
588	670	InterPro	IPR036420	BRCT domain superfamily
391	429	Gene3D	G3DSA:6.20.10.30	-
403	583	SUPERFAMILY	SSF47781	RuvA domain 2-like
403	583	InterPro	IPR010994	RuvA domain 2-like
596	669	SUPERFAMILY	SSF52113	BRCT domain
596	669	InterPro	IPR036420	BRCT domain superfamily
331	346	ProSitePatterns	PS01056	NAD-dependent DNA ligase signature 2.
331	346	InterPro	IPR033136	NAD-dependent DNA ligase, conserved site
318	399	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
318	399	InterPro	IPR012340	Nucleic acid-binding, OB-fold
430	505	Gene3D	G3DSA:1.10.150.20	-
506	584	Gene3D	G3DSA:1.10.150.20	-
593	671	ProSiteProfiles	PS50172	BRCT domain profile.
593	671	InterPro	IPR001357	BRCT domain
595	670	SMART	SM00292	BRCT_7
595	670	InterPro	IPR001357	BRCT domain
3	448	SMART	SM00532	ligaN3
3	448	InterPro	IPR013840	NAD-dependent DNA ligase, N-terminal
391	429	FunFam	G3DSA:6.20.10.30:FF:000001	DNA ligase
4	318	Pfam	PF01653	NAD-dependent DNA ligase adenylation domain
4	318	InterPro	IPR013839	NAD-dependent DNA ligase, adenylation
317	390	Gene3D	G3DSA:2.40.50.140	-
317	390	InterPro	IPR012340	Nucleic acid-binding, OB-fold
2	316	SUPERFAMILY	SSF56091	DNA ligase/mRNA capping enzyme, catalytic domain
588	670	FunFam	G3DSA:3.40.50.10190:FF:000004	DNA ligase
430	504	FunFam	G3DSA:1.10.150.20:FF:000007	DNA ligase
65	315	Gene3D	G3DSA:3.30.470.30	DNA ligase/mRNA capping enzyme
510	573	Pfam	PF12826	Helix-hairpin-helix motif
510	573	InterPro	IPR041663	DisA/LigA, helix-hairpin-helix motif
505	583	FunFam	G3DSA:1.10.150.20:FF:000006	DNA ligase
11	665	NCBIfam	TIGR00575	DNA ligase (NAD(+)) LigA
11	665	InterPro	IPR001679	NAD-dependent DNA ligase
65	315	FunFam	G3DSA:3.30.470.30:FF:000001	DNA ligase
6	317	CDD	cd00114	LIGANc
6	317	InterPro	IPR013839	NAD-dependent DNA ligase, adenylation

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

0.815

Likely same site as P2Rank 1 1.8 Å 23 shared residues 79% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.874

Likely same site as FPocket 26 1.8 Å 23 shared residues 79% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.471

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Surrounding area

Site 3 P2Rank #3

0.053

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Surrounding area

Site 4 P2Rank #4

0.035

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Surrounding area

Site 5 P2Rank #5

0.022

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Surrounding area

Residue sets

UniProt: Active site:115-115 N6-AMP-lysine intermediate

UniProt: Binding site:113-113

UniProt: Binding site:136-136

UniProt: Binding site:173-173

UniProt: Binding site:290-290

UniProt: Binding site:314-314

UniProt: Binding site:32-36

UniProt: Binding site:408-408

UniProt: Binding site:411-411

UniProt: Binding site:432-432

UniProt: Binding site:81-82

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.931

Likely same site as FPocket 10 4.8 Å 32 shared residues 82% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.297

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Surrounding area

Site 3 P2Rank #3

0.13

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Surrounding area

Site 4 P2Rank #4

0.063

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Surrounding area

Site 5 P2Rank #5

0.039

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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_A0A0H3GVW8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03557	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.

60 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0XS PDB via homolog 335.1 Da · LogP 2.09 · TPSA 94.9 Open detail RCSB PDB

0XT PDB via homolog Detail RCSB PDB

1X7 PDB via homolog Detail RCSB PDB

1X8 PDB via homolog Detail RCSB PDB

DKR 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
0XS RCSB PDB	4GLX	P15042	335.1 Da LogP 2.09 TPSA 94.9	✓ Ro5	✓ Clean	`c1c2cc(c(nc2nc(c1C(=O)N)N)C(F)(F)F)Br`
0XT RCSB PDB	4GLW	C1CKI0	206.2 Da LogP -0.10 TPSA 112.8	✓ Ro5	✓ Clean	`Cc1c(nc2c(n1)c(nc(n2)N)N)OC`
1X7 RCSB PDB	4LH6	Q837V6	272.1 Da LogP 1.74 TPSA 82.0	✓ Ro5	✓ Clean	`c1c2c(c(cnc2N)C(=O)N)sc1Br`
1X8 RCSB PDB	4LH7	Q837V6	236.3 Da LogP 0.08 TPSA 125.1	✓ Ro5	✓ Clean	`c1c2c(c(cnc2N)C(=O)N)sc1C(=O)N`
DKR RCSB PDB	6KKV	P9WNV1	214.3 Da LogP 2.25 TPSA 44.9	✓ Ro5	✓ Clean	`Cc1ccc(cc1)CNC(=O)c2ccc[nH]2`
EWO RCSB PDB	6LW8	P9WNV1	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`c1cc(ccc1[C@@H]2c3c([nH]cn3)CCN2)F`
IVH RCSB PDB	3PN1	P43813	355.4 Da LogP -0.09 TPSA 139.5	✓ Ro5	✓ Clean	`CCCCSc1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H…`
IWH RCSB PDB	3PN1	P43813	256.3 Da LogP 1.61 TPSA 65.1	✓ Ro5	✓ Clean	`Cc1ccc(c(c1)C)CN2C=C(C=CC2=O)C(=O)N`
NMN RCSB PDB	6KDU	P9WNV1	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(…`

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
CHEMBL1807815 ChEMBL	Q9AIU7	6.37 ~426.6 nM	351.4 Da LogP -0.66 TPSA 148.8	✓ Ro5	✓ Clean	`Nc1nc(OC2CCCC2)nc2c1ncn2[C@@H]1O[C@H](CO)[C@@H]…`

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
ZINC12503278 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@@H…`
ZINC1404028 ZINC	1.000	214.3 Da LogP 2.25 TPSA 44.9	✓ Ro5	✓ Clean	`Cc1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC1532667 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@H]2O[C@@H](COP(=O)(O)O)[C@H]…`
ZINC2545161 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@@H](COP(=O)(O)O)[C@H…`
ZINC3870109 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@@H](COP(=O)(O)O)[C@@…`
ZINC40465856 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@H]…`
ZINC40762833 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC4228273 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@@H…`
ZINC5886621 ZINC	1.000	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`Fc1ccc([C@H]2NCCc3[nH]cnc32)cc1`
ZINC5886640 ZINC	1.000	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`Fc1ccc([C@@H]2NCCc3[nH]cnc32)cc1`
ZINC77311638 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@H]…`
ZINC1730854 ZINC	0.867	320.4 Da LogP 1.60 TPSA 81.4	✓ Ro5	✓ Clean	`c1nc2c([nH]1)CCN[C@H]2c1ccc([C@@H]2NCCc3[nH]cnc…`
ZINC1730855 ZINC	0.867	320.4 Da LogP 1.60 TPSA 81.4	✓ Ro5	✓ Clean	`c1nc2c([nH]1)CCN[C@H]2c1ccc([C@H]2NCCc3[nH]cnc3…`
ZINC1730857 ZINC	0.867	320.4 Da LogP 1.60 TPSA 81.4	✓ Ro5	✓ Clean	`c1nc2c([nH]1)CCN[C@@H]2c1ccc([C@H]2NCCc3[nH]cnc…`
ZINC4095572 ZINC	0.809	336.2 Da LogP -1.60 TPSA 157.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@@H…`
ZINC77311659 ZINC	0.809	336.2 Da LogP -1.60 TPSA 157.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@H]…`
ZINC77311660 ZINC	0.809	336.2 Da LogP -1.60 TPSA 157.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@H]…`
ZINC77311661 ZINC	0.809	336.2 Da LogP -1.60 TPSA 157.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@@H…`
ZINC25756940 ZINC	0.760	331.3 Da LogP 0.35 TPSA 123.0	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H](COP(=O)(O)O)O[C@@H]([n+]2cccc(C(…`
ZINC1404025 ZINC	0.750	218.2 Da LogP 2.08 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NCc1ccc(F)cc1)c1ccc[nH]1`
ZINC4637217 ZINC	0.743	213.3 Da LogP 1.95 TPSA 40.7	✓ Ro5	✓ Clean	`Cc1ccc([C@@H]2NCCc3[nH]cnc32)cc1`
ZINC4637218 ZINC	0.743	213.3 Da LogP 1.95 TPSA 40.7	✓ Ro5	✓ Clean	`Cc1ccc([C@H]2NCCc3[nH]cnc32)cc1`
ZINC13815023 ZINC	0.722	297.3 Da LogP -1.97 TPSA 148.8	✓ Ro5	✓ Clean	`COc1nc(N)c2ncn([C@@H]3O[C@H](CO)[C@@H](O)[C@H]3…`
ZINC49053484 ZINC	0.722	297.3 Da LogP -1.97 TPSA 148.8	✓ Ro5	✓ Clean	`COc1nc(N)c2ncn([C@H]3O[C@@H](CO)[C@H](O)[C@@H]3…`
ZINC1404011 ZINC	0.718	230.3 Da LogP 1.95 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC32744798 ZINC	0.718	243.3 Da LogP 2.01 TPSA 48.1	✓ Ro5	Alert	`CN(C)c1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC32901157 ZINC	0.718	257.3 Da LogP 1.90 TPSA 74.0	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC6847206 ZINC	0.718	257.3 Da LogP 2.01 TPSA 48.1	✓ Ro5	✓ Clean	`CN(C)Cc1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC5928269 ZINC	0.711	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`Fc1cccc([C@H]2NCCc3[nH]cnc32)c1`
ZINC5928273 ZINC	0.711	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`Fc1cccc([C@@H]2NCCc3[nH]cnc32)c1`
ZINC1776011316 ZINC	0.700	333.3 Da LogP -1.74 TPSA 154.2	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CCP(=O)(O)O)[C@@H…`
ZINC32743681 ZINC	0.700	258.3 Da LogP 1.73 TPSA 71.2	✓ Ro5	✓ Clean	`COC(=O)c1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC4637222 ZINC	0.684	229.3 Da LogP 1.65 TPSA 49.9	✓ Ro5	✓ Clean	`COc1ccc([C@@H]2NCCc3[nH]cnc32)cc1`
ZINC4637223 ZINC	0.684	229.3 Da LogP 1.65 TPSA 49.9	✓ Ro5	✓ Clean	`COc1ccc([C@H]2NCCc3[nH]cnc32)cc1`
ZINC95992137 ZINC	0.683	292.4 Da LogP 1.74 TPSA 79.0	✓ Ro5	✓ Clean	`CCS(=O)(=O)c1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC14613564 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO)[C@@H](O)[C@@H…`
ZINC34633968 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@H]2O[C@H](CO)[C@@H](O)[C@H]2…`
ZINC4096036 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO)[C@@H](O)[C@H]…`
ZINC65748069 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO)[C@H](O)[C@H]2…`
ZINC65748073 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO)[C@H](O)[C@@H]…`
ZINC901659 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@H]2O[C@@H](CO)[C@H](O)[C@@H]…`
ZINC12981859 ZINC	0.675	242.3 Da LogP 1.61 TPSA 62.0	✓ Ro5	✓ Clean	`Cc1ccc(CNC(=O)c2ccc[nH]c2=O)cc1`
ZINC17300049 ZINC	0.660	297.3 Da LogP -2.69 TPSA 177.6	2 viol.	✓ Clean	`NNc1nc(N)c2ncn([C@@H]3O[C@H](CO)[C@@H](O)[C@@H]…`
ZINC1857790181 ZINC	0.660	299.3 Da LogP -1.69 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(S)nc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H…`
ZINC22048035 ZINC	0.660	282.3 Da LogP -2.40 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1nc(N)c2ncn([C@@H]3O[C@H](CO)[C@H](O)[C@@H]3O…`
ZINC22060240 ZINC	0.660	297.3 Da LogP -2.69 TPSA 177.6	2 viol.	✓ Clean	`NNc1nc(N)c2ncn([C@@H]3O[C@H](CO)[C@H](O)[C@@H]3…`
ZINC27332328 ZINC	0.660	282.3 Da LogP -2.40 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1nc(N)c2ncn([C@H]3O[C@@H](CO)[C@H](O)[C@@H]3O…`
ZINC4095498 ZINC	0.660	282.3 Da LogP -2.40 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1nc(N)c2ncn([C@@H]3O[C@H](CO)[C@@H](O)[C@H]3O…`
ZINC4353413 ZINC	0.660	282.3 Da LogP -2.40 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1nc(N)c2ncn([C@H]3O[C@@H](CO)[C@@H](O)[C@H]3O…`
ZINC4353414 ZINC	0.660	282.3 Da LogP -2.40 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1nc(N)c2ncn([C@@H]3O[C@@H](CO)[C@@H](O)[C@H]3…`

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.