KpATCC43816 Protein target profile

DNA ligase

Accession: VK055_3473

Gene: ligB AIK82029.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3H4K3

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Length 558

Pocket druggability (P2Rank · AlphaFold DB model) 0.752

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 4 GO

Target summary

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

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.75. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 1.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 30.526 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 90.96 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.752

Structure A0A0H3H4K3

Pocket Pocket 1

Druggability (FPocket) 0.836

Structure A0A0H3H4K3

Pocket Pocket 1

ColabFold model

P2Rank 0.748 · Pocket 1

FPocket 0.862 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 61 / 4744 genomes with a hit

Prevalence 1.3%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction, no human homolog detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MRKGGWWLALGMFSASALATCPDWPPARGRQETSRLHQQIVAWKEAYWRQGASGVSDDVYDQLTLRLAQWRQCFPGATPEDDDLPPPTGDARHPVAHTGVRKLADEDSVARWMKNKSDLWIQPKVDGVAVTLVYRQGRLVQAISRGDGLRGEAWTARARQIPALAKVMTGELADSVLQGELFLRRDGHVQQQAGGMNARAKVAGLMMRADAAAALSQLDVFIWAWPDGPSDMRRRQKLLAQAGFKYSGQYTHPVSRIEQVAQWRQRWYRSPLPFVSDGVIVREGREPPGRVWSPGKGEWLAAWKYPPASRVMQVRAIRFSTGRSGRLNVVAELEPQRLDDKRVQRVNVGSVSRWQMLDIGVGDQLQISLAGQGIPRVDAVVWRTAERHKPTPPPAKFNALTCYFATPECSEQFLSRLIWLSSKSALNVDGVGENLWRVIQQQNPMTHIFSWLALTVEQLQAVPGISAARGQHLWHQFDLVRKRPFIRWVLAMGIPVPQGALAQLESENWHLLAAKSEAQWRTLPGVGEIRARQLVAFLHHPDVVALAQWLSGQRIPGF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

6.5.1.2

Gene Ontology (GO)

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:0003911 Catalysis of the reaction: NAD+ + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + nicotinamide nucleotide + deoxyribonucleotide(n+m).
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:0006259 Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
1	19	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
26	84	Gene3D	G3DSA:1.10.287.610	Helix hairpin bin
313	387	Pfam	PF03120	NAD-dependent DNA ligase OB-fold domain
313	387	InterPro	IPR004150	NAD-dependent DNA ligase, OB-fold
15	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
311	388	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
311	388	InterPro	IPR012340	Nucleic acid-binding, OB-fold
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
400	550	SUPERFAMILY	SSF47781	RuvA domain 2-like
400	550	InterPro	IPR010994	RuvA domain 2-like
28	425	SMART	SM00532	ligaN3
28	425	InterPro	IPR013840	NAD-dependent DNA ligase, N-terminal
17	382	PANTHER	PTHR47810	DNA LIGASE
111	282	Pfam	PF01653	NAD-dependent DNA ligase adenylation domain
111	282	InterPro	IPR013839	NAD-dependent DNA ligase, adenylation
6	558	Hamap	MF_01587	DNA ligase B [ligB].
6	558	InterPro	IPR020923	DNA ligase B
20	558	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
4	14	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
310	394	Gene3D	G3DSA:2.40.50.140	-
310	394	InterPro	IPR012340	Nucleic acid-binding, OB-fold
24	306	SUPERFAMILY	SSF56091	DNA ligase/mRNA capping enzyme, catalytic domain
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
89	308	Gene3D	G3DSA:3.30.470.30	DNA ligase/mRNA capping enzyme

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.752

Likely same site as FPocket 25 4.9 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.688

Likely same site as FPocket 1 4.3 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.534

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Surrounding area

Pocket 4 P2Rank #4

0.079

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Surrounding area

Pocket 5 P2Rank #5

0.027

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.836 Unusual size

Likely same site as P2Rank 2 4.3 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 2 FPocket #25

0.367

Likely same site as P2Rank 1 4.9 Å 9 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:124-124 N6-AMP-lysine intermediate

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.748

Likely same site as FPocket 1 6.1 Å 22 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.704

Likely same site as FPocket 1 6.8 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.687

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Surrounding area

Pocket 4 P2Rank #4

0.049

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Surrounding area

Pocket 5 P2Rank #5

0.048

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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_A0A0H3H4K3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3473	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 and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 7 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

IVH 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`
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	4LH6	Q837V6	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…`
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…`
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]…`
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(…`
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…`
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…`
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]…`
ZINC105043122 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]3O…`
ZINC12405468 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…`
ZINC14920360 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…`
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…`
ZINC22048039 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…`
ZINC2383767257 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@@…`
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…`
ZINC4353415 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…`
ZINC4353416 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]…`
ZINC41670453 ZINC	0.659	257.3 Da LogP 2.21 TPSA 59.3	✓ Ro5	✓ Clean	`Cc1ccc(C)c(Cn2cc(C(=O)O)ccc2=O)c1`
ZINC1661187 ZINC	0.636	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H…`
ZINC19939879 ZINC	0.636	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H…`
ZINC2040952 ZINC	0.636	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H…`
ZINC21982895 ZINC	0.636	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@H](CO)[C@H](O)[C@@H]…`
ZINC22059332 ZINC	0.636	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]…`
ZINC26504975 ZINC	0.636	393.1 Da LogP -1.38 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(I)nc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@…`
ZINC26504979 ZINC	0.636	393.1 Da LogP -1.38 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(I)nc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@…`
ZINC27435623 ZINC	0.636	393.1 Da LogP -1.38 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(I)nc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]…`
ZINC3875977 ZINC	0.636	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H…`
ZINC40455052 ZINC	0.636	393.1 Da LogP -1.38 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(I)nc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H…`
ZINC4216238 ZINC	0.636	285.2 Da LogP -1.84 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@…`
ZINC49014899 ZINC	0.636	393.1 Da LogP -1.38 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(I)nc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@H]…`

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.

Cross-references

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

DNA ligase

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

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways