Protein profile

PA1529

NAD-dependent DNA ligase LigA

Genome: NC_002516.2

Gene: lig Structure source: ColabFold

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Amino acids 794

Annotations 3

Features 59

PDB binders 7

Druggability 0.683

Overview

Basic information about this protein and its source genome.

Accession: PA1529
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: lig
Status: annotated
Amino acids: 794
Structure source: ColabFold

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:0003911 Catalysis of the reaction: NAD+ + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + nicotinamide nucleotide + deoxyribonucleotide(n+m).

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 51.389
Human E-value: 3.91e-11
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.683

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MTDTQAAAERIAQLRTELDTHNYRYYVLDEPSIPDAEYDRLFRELQALEAEYPQLLTPDSPTQRVSGTPASAFGEVRHEIPMLSLGNAFEEQDLLDFDRRVREGLADLLPGGDLLGGGAEVEYSCEPKLDGLAVSLLYERGQLVRGATRGDGSTGEDITSNVRTIRNVPLKLHGEGWPEILEVRGEVFMSKAGFEALNAKAVETGGKTFANPRNAAAGSLRQLDSKITASRPLEFCAYGFGQVSGTLPDTQVGILEAFRGWGIPISRELRLVKGAQACRDYYDDIGRRRDALAYEIDGVVFKVNRIAFQRELGFRAREPRWAIAHKFPAREELTELLGVEFQVGRTGAVTPVARLKPVQVAGVTVSNATLHNMDEVARLGLRIGDTVVIRRAGDVIPQVMQVVLERRPADAQAIEVPEHCPVCGSAVERTQLVKRSKGKESISEGAIYRCVGRLSCQAQLKQAIIHFVSRRAMDIDGLGDKIVEQLVDRGLVASPADLYTLTYEQVFELEGFAELSTNNLLTAIADSRKPSLARFIFALGIPDVGEETAKLLARSLGSLERIGKALPEVLTYLPDVGAEVAYEIHNFFADEHNRQVIAQLRDAEHGVQLQEEGEVAAEFAACASLAGFIDKLNIPFIAATGAEKLASRFGSLDGIIRADWLDLRQVERLPERAAKSLRDFFDEPANVQRALAIEAQLREFGMHWQSERKAVEGLPLAGQTWVLTGTLEAMSRDVAKDKLEGLGAKVAGSVSAKTHCVVAGPGAGSKLAKANELGVKVLDEDGLLKLFDEHGVAR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

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: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:0003911 Catalysis of the reaction: NAD+ + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + nicotinamide nucleotide + deoxyribonucleotide(n+m).

Sequence Features

Domain/signature hits from InterPro and related databases.

59 records

Show feature table

Start	End	DB	Term	Name
454	528	Gene3D	G3DSA:1.10.150.20	-
702	788	Gene3D	G3DSA:3.40.50.10190	BRCT domain
702	788	InterPro	IPR036420	BRCT domain superfamily
16	770	PANTHER	PTHR23389	CHROMOSOME TRANSMISSION FIDELITY FACTOR 18
454	529	FunFam	G3DSA:1.10.150.20:FF:000007	DNA ligase
416	603	SUPERFAMILY	SSF47781	RuvA domain 2-like
416	603	InterPro	IPR010994	RuvA domain 2-like
329	402	Gene3D	G3DSA:2.40.50.140	-
329	402	InterPro	IPR012340	Nucleic acid-binding, OB-fold
419	458	Pfam	PF03119	NAD-dependent DNA ligase C4 zinc finger domain
419	458	InterPro	IPR004149	Zinc-finger, NAD-dependent DNA ligase C4-type
330	412	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
330	412	InterPro	IPR012340	Nucleic acid-binding, OB-fold
329	402	FunFam	G3DSA:2.40.50.140:FF:000012	DNA ligase
706	789	FunFam	G3DSA:3.40.50.10190:FF:000069	DNA ligase
624	701	Gene3D	G3DSA:1.10.150.20	-
620	792	PIRSF	PIRSF001604	LigA
620	792	InterPro	IPR001679	NAD-dependent DNA ligase
1	622	PIRSF	PIRSF001604	LigA
1	622	InterPro	IPR001679	NAD-dependent DNA ligase
128	157	ProSitePatterns	PS01055	NAD-dependent DNA ligase signature 1.
128	157	InterPro	IPR018239	NAD-dependent DNA ligase, active site
2	67	FunFam	G3DSA:1.10.287.610:FF:000002	DNA ligase
403	453	Gene3D	G3DSA:6.20.10.30	-
343	358	ProSitePatterns	PS01056	NAD-dependent DNA ligase signature 2.
343	358	InterPro	IPR033136	NAD-dependent DNA ligase, conserved site
714	788	SUPERFAMILY	SSF52113	BRCT domain
714	788	InterPro	IPR036420	BRCT domain superfamily
5	787	Hamap	MF_01588	DNA ligase [ligA].
5	787	InterPro	IPR001679	NAD-dependent DNA ligase
1	67	Gene3D	G3DSA:1.10.287.610	Helix hairpin bin
716	786	CDD	cd17748	BRCT_DNA_ligase_like
713	790	SMART	SM00292	BRCT_7
713	790	InterPro	IPR001357	BRCT domain
6	472	SMART	SM00532	ligaN3
6	472	InterPro	IPR013840	NAD-dependent DNA ligase, N-terminal
7	330	Pfam	PF01653	NAD-dependent DNA ligase adenylation domain
7	330	InterPro	IPR013839	NAD-dependent DNA ligase, adenylation
3	328	SUPERFAMILY	SSF56091	DNA ligase/mRNA capping enzyme, catalytic domain
713	787	Pfam	PF00533	BRCA1 C Terminus (BRCT) domain
713	787	InterPro	IPR001357	BRCT domain
334	410	Pfam	PF03120	NAD-dependent DNA ligase OB-fold domain
334	410	InterPro	IPR004150	NAD-dependent DNA ligase, OB-fold
68	327	Gene3D	G3DSA:3.30.470.30	DNA ligase/mRNA capping enzyme
711	794	ProSiteProfiles	PS50172	BRCT domain profile.
711	794	InterPro	IPR001357	BRCT domain
530	609	FunFam	G3DSA:1.10.150.20:FF:000006	DNA ligase
632	687	Pfam	PF12826	Helix-hairpin-helix motif
632	687	InterPro	IPR041663	DisA/LigA, helix-hairpin-helix motif
534	597	Pfam	PF12826	Helix-hairpin-helix motif
534	597	InterPro	IPR041663	DisA/LigA, helix-hairpin-helix motif
618	704	SUPERFAMILY	SSF47781	RuvA domain 2-like
618	704	InterPro	IPR010994	RuvA domain 2-like
68	327	FunFam	G3DSA:3.30.470.30:FF:000001	DNA ligase
14	617	NCBIfam	TIGR00575	DNA ligase (NAD(+)) LigA
14	617	InterPro	IPR001679	NAD-dependent DNA ligase
529	611	Gene3D	G3DSA:1.10.150.20	-
9	329	CDD	cd00114	LIGANc
9	329	InterPro	IPR013839	NAD-dependent DNA ligase, adenylation

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
ColabFold PA1529	ColabFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.683

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	4GLW	C1CKI0	206.2 Da LogP -0.10 TPSA 112.8	✓ Ro5	✓ Clean	`Cc1c(nc2c(n1)c(nc(n2)N)N)OC`
1X7	4LH6	Q837V6	272.1 Da LogP 1.74 TPSA 82.0	✓ Ro5	✓ Clean	`c1c2c(c(cnc2N)C(=O)N)sc1Br`
1X8	4LH7	Q837V6	236.3 Da LogP 0.08 TPSA 125.1	✓ Ro5	✓ Clean	`c1c2c(c(cnc2N)C(=O)N)sc1C(=O)N`
IVH	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	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	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	Q9AIU7	6.37	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	0.659	257.3 Da LogP 2.21 TPSA 59.3	✓ Ro5	✓ Clean	`Cc1ccc(C)c(Cn2cc(C(=O)O)ccc2=O)c1`
ZINC1661187	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	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	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	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	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	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	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	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	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	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	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	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.