Protein profile

KP13_03557

DNA ligase

Genome: KpKP13

Gene: ligA AHE43363.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GVW8

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Amino acids 671

Annotations 7

Features 62

PDB binders 9

Druggability 0.815

Overview

Basic information about this protein and its source genome.

Accession: KP13_03557
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: ligA AHE43363.1
Status: annotated
Amino acids: 671
Structure source: AlphaFold + ColabFold

6.5.1.2

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 42.254
Human E-value: 4.52e-08
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 92.239
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 88.98

Selected Druggability evidence

AlphaFold / UniProt model

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 0.815

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

Normalized 0.049

Sequence

Primary amino-acid sequence viewer.

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 Features

Domain/signature hits 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; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GVW8	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03557	ColabFold	—	—	full sequence	—	Loaded

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
26				0.815

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	19.49	0.84
2	6.89	0.354
3	2.08	0.047
4	1.4	0.017
5	1.22	0.011

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
10				0.439

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	24.55	0.899
2	5.45	0.259
3	2.21	0.053
4	1.99	0.042
5	1.36	0.016

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

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`
DKR	6KKV	P9WNV1	214.3 Da LogP 2.25 TPSA 44.9	✓ Ro5	✓ Clean	`Cc1ccc(cc1)CNC(=O)c2ccc[nH]2`
EWO	6LW8	P9WNV1	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`c1cc(ccc1[C@@H]2c3c([nH]cn3)CCN2)F`
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	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	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…`
ZINC1404028	1.000	214.3 Da LogP 2.25 TPSA 44.9	✓ Ro5	✓ Clean	`Cc1ccc(CNC(=O)c2ccc[nH]2)cc1`
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…`
ZINC5886621	1.000	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`Fc1ccc([C@H]2NCCc3[nH]cnc32)cc1`
ZINC5886640	1.000	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`Fc1ccc([C@@H]2NCCc3[nH]cnc32)cc1`
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]…`
ZINC1730854	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	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	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	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(…`
ZINC1404025	0.750	218.2 Da LogP 2.08 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NCc1ccc(F)cc1)c1ccc[nH]1`
ZINC4637217	0.743	213.3 Da LogP 1.95 TPSA 40.7	✓ Ro5	✓ Clean	`Cc1ccc([C@@H]2NCCc3[nH]cnc32)cc1`
ZINC4637218	0.743	213.3 Da LogP 1.95 TPSA 40.7	✓ Ro5	✓ Clean	`Cc1ccc([C@H]2NCCc3[nH]cnc32)cc1`
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…`
ZINC1404011	0.718	230.3 Da LogP 1.95 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC32744798	0.718	243.3 Da LogP 2.01 TPSA 48.1	✓ Ro5	Alert	`CN(C)c1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC32901157	0.718	257.3 Da LogP 1.90 TPSA 74.0	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC6847206	0.718	257.3 Da LogP 2.01 TPSA 48.1	✓ Ro5	✓ Clean	`CN(C)Cc1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC5928269	0.711	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`Fc1cccc([C@H]2NCCc3[nH]cnc32)c1`
ZINC5928273	0.711	217.2 Da LogP 1.78 TPSA 40.7	✓ Ro5	✓ Clean	`Fc1cccc([C@@H]2NCCc3[nH]cnc32)c1`
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…`
ZINC32743681	0.700	258.3 Da LogP 1.73 TPSA 71.2	✓ Ro5	✓ Clean	`COC(=O)c1ccc(CNC(=O)c2ccc[nH]2)cc1`
ZINC4637222	0.684	229.3 Da LogP 1.65 TPSA 49.9	✓ Ro5	✓ Clean	`COc1ccc([C@@H]2NCCc3[nH]cnc32)cc1`
ZINC4637223	0.684	229.3 Da LogP 1.65 TPSA 49.9	✓ Ro5	✓ Clean	`COc1ccc([C@H]2NCCc3[nH]cnc32)cc1`
ZINC95992137	0.683	292.4 Da LogP 1.74 TPSA 79.0	✓ Ro5	✓ Clean	`CCS(=O)(=O)c1ccc(CNC(=O)c2ccc[nH]2)cc1`
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]…`
ZINC12981859	0.675	242.3 Da LogP 1.61 TPSA 62.0	✓ Ro5	✓ Clean	`Cc1ccc(CNC(=O)c2ccc[nH]c2=O)cc1`
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…`
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…`
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…`

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.