KpKP13 Protein target profile

Lysyl-tRNA synthetase

Accession: KP13_02199

Gene: AHE42768.1 lysS 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H2L3

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Length 505

Pocket druggability (P2Rank · AlphaFold DB model) 0.947

Direct ligand evidence 0 70 total records

Functional annotation 1 EC 12 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.95, FPocket 0.80). 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 0.80. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.95. 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 (%): 53.75 Lower values reduce human off-target concern.
Human E-value: 2.09e-18
Gut microbiome similarity: 31.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 94.653 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.19 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) 0.947

Structure A0A0H3H2L3

Pocket Pocket 1

Druggability (FPocket) 0.799

Structure A0A0H3H2L3

Pocket Pocket 1

ColabFold model

P2Rank 0.923 · Pocket 1

FPocket 0.659 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1485 / 4744 genomes with a hit

Prevalence 31.3%

Sequence

Primary amino-acid sequence viewer.

MSEQQAQGADAAIDLNNELKTRREKLAALREQGVAFPNDFRRDHTSDQLHADFDGKENEELEALNVEVAVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDDLAEGVYNDQFKKWDLGDIIAARGKLFKTKTGELSIHCTELRLLTKALRPLPDKFHGLQDQEARYRQRYLDLISNDESRKTFKVRSQILAGIRQFMVGRGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQDILGNTEVPYGDQVFDFGKPFEKLTMREAIKKYRPETEMADLDNFDSAKAIAESIGIKVEKSWGLGRIVTEIFEEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRFQDQVDAKAAGDDEAMFYDEDYVTALEHGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFPAMRPQK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

6.1.1.6

Gene Ontology (GO)

GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0003676 Binding to a nucleic acid.
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: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.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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:0004824 Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
12	32	Coils	Coil	Coil
155	501	Gene3D	G3DSA:3.30.930.10	Bira Bifunctional Protein; Domain 2
155	501	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
262	279	PRINTS	PR00982	Lysyl-tRNA synthetase signature
262	279	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
215	231	PRINTS	PR00982	Lysyl-tRNA synthetase signature
215	231	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
199	209	PRINTS	PR00982	Lysyl-tRNA synthetase signature
199	209	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
244	257	PRINTS	PR00982	Lysyl-tRNA synthetase signature
244	257	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
386	402	PRINTS	PR00982	Lysyl-tRNA synthetase signature
386	402	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
184	503	ProSiteProfiles	PS50862	Aminoacyl-transfer RNA synthetases class-II family profile.
184	503	InterPro	IPR006195	Aminoacyl-tRNA synthetase, class II
67	174	CDD	cd04322	LysRS_N
67	174	InterPro	IPR044136	Lysine-tRNA ligase, class II, N-terminal
177	503	CDD	cd00775	LysRS_core
177	503	InterPro	IPR018149	Lysyl-tRNA synthetase, class II, C-terminal
68	146	Pfam	PF01336	OB-fold nucleic acid binding domain
68	146	InterPro	IPR004365	OB-fold nucleic acid binding domain, AA-tRNA synthetase-type
21	505	Hamap	MF_00252	Lysine--tRNA ligase [lysS].
21	505	InterPro	IPR002313	Lysine-tRNA ligase, class II
13	155	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
13	155	InterPro	IPR012340	Nucleic acid-binding, OB-fold
15	155	FunFam	G3DSA:2.40.50.140:FF:000024	Lysine--tRNA ligase
162	502	SUPERFAMILY	SSF55681	Class II aaRS and biotin synthetases
162	502	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
162	501	Pfam	PF00152	tRNA synthetases class II (D, K and N)
162	501	InterPro	IPR004364	Aminoacyl-tRNA synthetase, class II (D/K/N)
1	505	PIRSF	PIRSF039101	LysRS2
1	505	InterPro	IPR034762	Bacterial/eukaryotic lysine-tRNA ligase, class II
14	505	NCBIfam	TIGR00499	lysine--tRNA ligase
14	505	InterPro	IPR002313	Lysine-tRNA ligase, class II
15	154	Gene3D	G3DSA:2.40.50.140	-
15	154	InterPro	IPR012340	Nucleic acid-binding, OB-fold
4	505	PANTHER	PTHR42918	LYSYL-TRNA SYNTHETASE
156	501	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.

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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

0.947

Likely same site as FPocket 1 4.2 Å 21 shared residues 84% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.123

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Surrounding area

Pocket 3 P2Rank #3

0.03

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Surrounding area

Pocket 4 P2Rank #4

0.018

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Surrounding area

Pocket 5 P2Rank #5

0.016

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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

0.799

Likely same site as P2Rank 1 4.2 Å 21 shared residues 84% of smaller site

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Surrounding area

Pocket 2 FPocket #23

0.467

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Surrounding area

Residue sets

UniProt: Binding site:415-415

UniProt: Binding site:422-422

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.923

Likely same site as FPocket 1 1.8 Å 31 shared residues 84% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.074

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Surrounding area

Pocket 3 P2Rank #3

0.019

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Surrounding area

Pocket 4 P2Rank #4

0.007

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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

0.659 Unusual size

Likely same site as P2Rank 1 1.8 Å 31 shared residues 84% of smaller site

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Surrounding area

Pocket 2 FPocket #26

0.305

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Surrounding area

Pocket 3 FPocket #23

0.202

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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_A0A0H3H2L3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02199	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.

70 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 20 records from similar proteins

Structural ligands 18 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

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

9X0 PDB via homolog Detail RCSB PDB

ACP PDB via homolog Detail RCSB PDB

ADN PDB via homolog Detail RCSB PDB

APC 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
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)…`
ADN RCSB PDB	6BNI	Q5CR27	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ 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	5YZX	P0A8N5	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 ~288.4 nM	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 ~288.4 nM	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…`
ZINC105469665 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…`
ZINC13527614 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)…`
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)…`
ZINC3873852 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)…`
ZINC3873853 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…`
ZINC3873854 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)…`
ZINC3873855 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…`
ZINC12360002 ZINC	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964 ZINC	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.768	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	0.754	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	0.750	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	0.750	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	0.750	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	0.750	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833 ZINC	0.737	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	0.737	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	0.737	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	0.737	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC3219369 ZINC	0.735	343.4 Da LogP 2.65 TPSA 85.6	✓ Ro5	✓ Clean	`O=C(COC(=O)c1cc(=O)c2ccccc2o1)NCC1CCCCC1`
ZINC31475423 ZINC	0.726	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC67822081 ZINC	0.717	342.4 Da LogP 2.89 TPSA 62.6	✓ Ro5	✓ Clean	`CC(C)CN1CCC[C@H](CNC(=O)c2cc(=O)c3ccccc3o2)C1`
ZINC67822082 ZINC	0.717	342.4 Da LogP 2.89 TPSA 62.6	✓ Ro5	✓ Clean	`CC(C)CN1CCC[C@@H](CNC(=O)c2cc(=O)c3ccccc3o2)C1`

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.

Sequence

UniProt A0A0H3H2L3

Chemistry

ChEMBL CHEMBL4211492 ChEMBL GUI