Protein target profile

PA3700

lysine--tRNA ligase

Genome: NC_002516.2

Gene: lysS PA3700 3D evidence: AlphaFold DB model UniProt Q9HXU0

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Length 501

Pocket druggability 0.729

Ligand records 69

EC / GO 1 / 12

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

4 signals

How to read 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 TPW 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.

Overview

Basic information about this protein and its source genome.

Accession: PA3700
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: lysS PA3700
Status: annotated
Amino acids: 501
3D evidence: AlphaFold DB model

6.1.1.6

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0004824 Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). GO:0000287 Binding to a magnesium (Mg) ion. GO:0042803 Binding to an identical protein to form a homodimer.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 48.864
Human E-value: 5.860000000000001e-21
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected pocket evidence

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 0.729

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MSDQQLDQHELQQEENKLIAQRKEKLAAVREARAIAFPNDFRRDAYFADLQKQYADKTKEELEAAAIPVKVAGRIMLNRGSFIVLQDSSERLQVYVNRKTLPEETLAEIKTWDLGDIIGAEGVLARSGKGDLYVDMTSVRLLTKSLRPLPDKHHGLTDTEQRYRQRYVDLMVNEETRHTFRVRSQVIAHIRRFLSERGFLEVETPMLQTIPGGAAAKPFETHHNALDMAMFLRIAPELYLKRLVVGGFEKVFEINRNFRNEGVSTRHNPEFTMLEFYQAYADYEDNMDLTEELFRELAQSVLGTTDVPYGDKVFHFGEPFVRLSVFDSILKYNPEITAADLNDVEKARAIAKKAGAKVLGHEGLGKLQVMIFEELVEHKLEQPHFITRYPFEVSPLARRNDEDPSVTDRFELFIGGREIANAYSELNDAEDQAERFMLQVKEKDAGDDEAMHYDADFINALEYGMPPTAGEGIGIDRLVMLLTNSPSIRDVILFPHMRPQA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

6.1.1.6

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004824 Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0042803 Binding to an identical protein to form a homodimer.
GO:0000049 Binding to a transfer RNA.
GO:0006430 The process of coupling lysine to lysyl-tRNA, catalyzed by lysyl-tRNA synthetase. The lysyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a lysine-accetping tRNA.
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:0003676 Binding to a nucleic acid.
GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0006418 The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, to be used in ribosome-mediated polypeptide synthesis.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
154	501	Gene3D	G3DSA:3.30.930.10	Bira Bifunctional Protein; Domain 2
154	501	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
180	499	ProSiteProfiles	PS50862	Aminoacyl-transfer RNA synthetases class-II family profile.
180	499	InterPro	IPR006195	Aminoacyl-tRNA synthetase, class II
69	142	Pfam	PF01336	OB-fold nucleic acid binding domain
69	142	InterPro	IPR004365	OB-fold nucleic acid binding domain, AA-tRNA synthetase-type
173	499	CDD	cd00775	LysRS_core
173	499	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
8	500	PANTHER	PTHR42918	LYSYL-TRNA SYNTHETASE
15	151	FunFam	G3DSA:2.40.50.140:FF:000024	Lysine--tRNA ligase
419	439	Coils	Coil	Coil
21	500	Hamap	MF_00252	Lysine--tRNA ligase [lysS].
21	500	InterPro	IPR002313	Lysine-tRNA ligase, class II
13	151	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
13	151	InterPro	IPR012340	Nucleic acid-binding, OB-fold
69	170	CDD	cd04322	LysRS_N
69	170	InterPro	IPR044136	Lysine-tRNA ligase, class II, N-terminal
280	300	Coils	Coil	Coil
159	497	Pfam	PF00152	tRNA synthetases class II (D, K and N)
159	497	InterPro	IPR004364	Aminoacyl-tRNA synthetase, class II (D/K/N)
15	151	Gene3D	G3DSA:2.40.50.140	-
15	151	InterPro	IPR012340	Nucleic acid-binding, OB-fold
258	275	PRINTS	PR00982	Lysyl-tRNA synthetase signature
258	275	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
240	253	PRINTS	PR00982	Lysyl-tRNA synthetase signature
240	253	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
211	227	PRINTS	PR00982	Lysyl-tRNA synthetase signature
211	227	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
195	205	PRINTS	PR00982	Lysyl-tRNA synthetase signature
195	205	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
382	398	PRINTS	PR00982	Lysyl-tRNA synthetase signature
382	398	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
11	31	Coils	Coil	Coil
158	498	SUPERFAMILY	SSF55681	Class II aaRS and biotin synthetases
158	498	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
16	500	NCBIfam	TIGR00499	lysine--tRNA ligase
16	500	InterPro	IPR002313	Lysine-tRNA ligase, class II
152	497	FunFam	G3DSA:3.30.930.10:FF:000001	Lysine--tRNA ligase

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.

Loading 3D structure...

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Structural evidence

0 + 1

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 PA3700	AlphaFold DB	—	—	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
2				0.729
1				0.29
6				0.286
3				0.208

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.

69 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 69 via homologs

Structural ligands 17 0 loaded crystals

Bioactive compounds 2 50 ZINC proposed compounds

Drug-like & clean 37 0 PAINS alerts

Best available ligand signal

45A PDB via homolog 345.3 Da · LogP -1.14 · TPSA 165.8 Open detail RCSB PDB

Detail RCSB PDB 45A PDB via homolog

Detail RCSB PDB 9X0 PDB via homolog

Detail RCSB PDB ACP PDB via homolog

Detail RCSB PDB APC PDB via homolog

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
45A RCSB PDB	6ILD	Q15046	345.3 Da LogP -1.14 TPSA 165.8	✓ Ro5	✓ Clean	`CP(=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c…`
9X0 RCSB PDB	6AGT	Q8IDJ8	285.3 Da LogP 3.10 TPSA 59.3	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=O)C=C(O2)C(=O)NCC3CCCCC3`
ACP RCSB PDB	1E22	P0A8N5	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
APC RCSB PDB	4DPG	Q15046	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
B4P RCSB PDB	3A74	Q9RHV9	836.4 Da LogP -2.45 TPSA 434.0	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
D4O RCSB PDB	6KA6	W7JP72	290.4 Da LogP 3.40 TPSA 66.8	✓ Ro5	✓ Clean	`C[C@H]1CCC[C@@H](C1)C[C@H]2Cc3cc(cc(c3C(=O)O2)O…`
D4U RCSB PDB	6KAB	W7JP72	276.3 Da LogP 3.15 TPSA 66.8	✓ Ro5	✓ Clean	`c1c(cc(c2c1C[C@@H](OC2=O)CC3CCCCC3)O)O`
D4X RCSB PDB	6KBF	W7JP72	289.4 Da LogP 2.97 TPSA 69.6	✓ Ro5	✓ Clean	`C[C@H]1CCC[C@@H](C1)C[C@H]2Cc3cc(cc(c3C(=O)N2)O…`
D5F RCSB PDB	6KCN	W7JP72	288.3 Da LogP 3.57 TPSA 70.7	✓ Ro5	✓ Clean	`C[C@H]1CCC[C@@H](C1)CC2=Cc3cc(cc(c3C(=O)O2)O)O`
D5O RCSB PDB	6KCT	W7JP72	274.3 Da LogP 3.33 TPSA 70.7	✓ Ro5	✓ Clean	`c1c(cc(c2c1C=C(OC2=O)CC3CCCCC3)O)O`
EZ3 RCSB PDB	6M0T	Q8IDJ8	308.3 Da LogP 1.50 TPSA 96.2	✓ Ro5	✓ Clean	`C[C@H]1CCC[C@@H](O1)[C@H]([C@H]2Cc3cc(cc(c3C(=O…`
F6O RCSB PDB	7BT5	Q8IDJ8	580.8 Da LogP 3.77 TPSA 115.8	2 viol.	✓ Clean	`CC(C)S(=O)(=O)c1ccccc1Nc2ncnc(n2)Nc3ccc(cc3OC)N…`
FYB RCSB PDB	6HCU	Q8IDJ8	355.3 Da LogP 2.60 TPSA 79.5	✓ Ro5	✓ Clean	`c1cc2c(cc1F)C(=O)C=C(O2)C(=O)NCC3(CCC(CC3)(F)F)O`
KAA RCSB PDB	3E9H	Q9RHV9	474.5 Da LogP -3.14 TPSA 243.8	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
KRS RCSB PDB	4PG3	Q8IDJ8	292.3 Da LogP 2.53 TPSA 76.0	✓ Ro5	✓ Clean	`C[C@H]1CCC[C@@H](O1)C[C@H]2Cc3cc(cc(c3C(=O)O2)O…`
LYN RCSB PDB	3A74	Q9RHV9	146.2 Da LogP -1.79 TPSA 96.8	✓ Ro5	✓ Clean	`C(CC[NH3+])C[C@@H](C(=O)N)N`
XAH RCSB PDB	3E9I	Q9RHV9	490.4 Da LogP -2.35 TPSA 256.2	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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
CHEMBL4211492 ChEMBL	Q8IDJ8	6.54	292.3 Da LogP 2.53 TPSA 76.0	✓ Ro5	✓ Clean	`C[C@@H]1CCC[C@H](C[C@H]2Cc3cc(O)cc(O)c3C(=O)O2)…`
GUI ChEMBL	Q15046	6.54	614.2 Da LogP 5.02 TPSA 102.9	2 viol.	✓ Clean	`CC(C)S(=O)(=O)c1ccccc1Nc2c(cnc(n2)Nc3ccc(cc3OC)…`

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
ZINC1772635095 ZINC	1.000	355.3 Da LogP 2.60 TPSA 79.5	✓ Ro5	✓ Clean	`O=C(NCC1(O)CCC(F)(F)CC1)c1cc(=O)c2cc(F)ccc2o1`
ZINC203258028 ZINC	1.000	292.3 Da LogP 2.53 TPSA 76.0	✓ Ro5	✓ Clean	`C[C@@H]1CCC[C@H](C[C@H]2Cc3cc(O)cc(O)c3C(=O)O2)…`
ZINC28539087 ZINC	1.000	292.3 Da LogP 2.53 TPSA 76.0	✓ Ro5	✓ Clean	`C[C@H]1CCC[C@H](C[C@H]2Cc3cc(O)cc(O)c3C(=O)O2)O1`
ZINC45301277 ZINC	1.000	292.3 Da LogP 2.53 TPSA 76.0	✓ Ro5	✓ Clean	`C[C@@H]1CCC[C@@H](C[C@H]2Cc3cc(O)cc(O)c3C(=O)O2…`
ZINC5735691 ZINC	1.000	292.3 Da LogP 2.53 TPSA 76.0	✓ Ro5	✓ Clean	`C[C@@H]1CCC[C@H](C[C@@H]2Cc3cc(O)cc(O)c3C(=O)O2…`
ZINC5735704 ZINC	1.000	292.3 Da LogP 2.53 TPSA 76.0	✓ Ro5	✓ Clean	`C[C@@H]1CCC[C@@H](C[C@@H]2Cc3cc(O)cc(O)c3C(=O)O…`
ZINC84585448 ZINC	1.000	313.4 Da LogP 3.88 TPSA 59.3	✓ Ro5	✓ Clean	`O=C(NCC1CCCCCCC1)c1cc(=O)c2ccccc2o1`
ZINC12360002 ZINC	0.922	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	0.922	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	0.922	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	0.922	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	0.922	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.922	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	0.922	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	0.922	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	0.922	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	0.922	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	0.922	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC219330894 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC13518964 ZINC	0.843	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.843	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.843	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.843	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.843	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	0.843	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	0.843	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	0.843	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	0.843	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	0.843	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	0.843	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	0.843	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.843	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224 ZINC	0.827	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.818	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.818	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.818	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.818	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC168710640 ZINC	0.809	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC168710738 ZINC	0.809	474.5 Da LogP -4.00 TPSA 260.9	2 viol.	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NS(=O)(=O)OC[C@H]1O[C@@H](…`
ZINC105372833 ZINC	0.808	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.808	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.808	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.808	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.789	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC105469665 ZINC	0.782	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.782	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.782	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.782	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.782	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.782	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=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.