Protein target profile

KP13_03674

ATP-dependent protease La

Genome: KpKP13 Gene: AHE46014.1 lon 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GJ60

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Length 784

Pocket druggability 0.758

Direct ligand evidence 0 74 total records

Functional annotation 1 EC 10 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: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.76, P2Rank 0.78). 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 0.76. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.78. 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 (%): 54.762 Lower values reduce human off-target concern.
Human E-value: 9.05e-63
Gut microbiome similarity: 11.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.98 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 88.68 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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 0.758

Structure A0A0H3GJ60

Pocket Pocket 7

P2Rank 0.783

Structure A0A0H3GJ60

Pocket Pocket 1

ColabFold model

FPocket 0.438 · Pocket 5

P2Rank 0.77 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 556 / 4744 genomes with a hit

Prevalence 11.7%

Cross-references

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

Sequence

UniProt A0A0H3GJ60

Chemistry

ChEMBL UKS ChEMBL CHEMBL4856865 ChEMBL CHEMBL4864108 ChEMBL CHEMBL4877126 ChEMBL CHEMBL4870013 ChEMBL CHEMBL4862424 ChEMBL CHEMBL4870902 ChEMBL CHEMBL4850612 ChEMBL CHEMBL4876920 ChEMBL CHEMBL4856768 ChEMBL CHEMBL4847335 ChEMBL CHEMBL4863384 ChEMBL CHEMBL4847763 ChEMBL CHEMBL4861871 ChEMBL CHEMBL4853599 ChEMBL CHEMBL4864045 ChEMBL CHEMBL4859172 ChEMBL CHEMBL4850826

Sequence

Primary amino-acid sequence viewer.

MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLDSPAIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKRKIDAAKMPKEAKEKTEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFNDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLLDKSLKHIEINGENLHDYLGVQRFDYGRADSENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRSRADKLGINADFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPDENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPFGMQVVTAK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

3.4.21.53

Gene Ontology (GO)

GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO:0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
GO:0043565 Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0034605 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
GO:0006515 The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

52 records

Show feature table

Start	End	DB	Term	Name
313	490	Gene3D	G3DSA:3.40.50.300	-
313	490	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
1	775	PIRSF	PIRSF001174	Lon_proteas
1	775	InterPro	IPR004815	Lon protease, bacterial/eukaryotic-type
348	492	SMART	SM00382	AAA_5
348	492	InterPro	IPR003593	AAA+ ATPase domain
120	245	FunFam	G3DSA:1.20.58.1480:FF:000001	Lon protease
313	493	CDD	cd19500	RecA-like_Lon
356	375	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
726	744	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
595	611	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
673	692	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
703	722	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
12	778	PANTHER	PTHR10046	ATP DEPENDENT LON PROTEASE FAMILY MEMBER
12	778	InterPro	IPR027065	Lon protease
1	118	FunFam	G3DSA:2.30.130.40:FF:000001	Lon protease
190	227	Coils	Coil	Coil
595	771	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
595	771	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold
11	772	Hamap	MF_01973	Lon protease [lon].
11	772	InterPro	IPR027543	Lon protease, bacterial
592	773	ProSiteProfiles	PS51786	Lon proteolytic domain profile.
592	773	InterPro	IPR008269	Peptidase S16, Lon proteolytic domain
676	684	ProSitePatterns	PS01046	ATP-dependent serine proteases, lon family, serine active site.
676	684	InterPro	IPR008268	Peptidase S16, active site
352	489	Pfam	PF00004	ATPase family associated with various cellular activities (AAA)
352	489	InterPro	IPR003959	ATPase, AAA-type, core
12	771	NCBIfam	TIGR00763	endopeptidase La
12	771	InterPro	IPR004815	Lon protease, bacterial/eukaryotic-type
313	490	FunFam	G3DSA:3.40.50.300:FF:000021	Lon protease homolog
120	245	Gene3D	G3DSA:1.20.58.1480	-
491	584	Gene3D	G3DSA:1.10.8.60	-
10	202	SMART	SM00464	lon_5
10	202	InterPro	IPR003111	Lon protease, N-terminal domain
585	772	FunFam	G3DSA:3.30.230.10:FF:000010	Lon protease
10	201	Pfam	PF02190	ATP-dependent protease La (LON) substrate-binding domain
10	201	InterPro	IPR003111	Lon protease, N-terminal domain
585	772	Gene3D	G3DSA:3.30.230.10	-
585	772	InterPro	IPR014721	Ribosomal protein S5 domain 2-type fold, subgroup
491	584	FunFam	G3DSA:1.10.8.60:FF:000035	Lon protease
570	772	Pfam	PF05362	Lon protease (S16) C-terminal proteolytic domain
570	772	InterPro	IPR008269	Peptidase S16, Lon proteolytic domain
313	587	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
313	587	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
11	202	ProSiteProfiles	PS51787	Lon N-terminal domain profile.
11	202	InterPro	IPR003111	Lon protease, N-terminal domain
253	300	Gene3D	G3DSA:1.20.5.5270	-
252	301	FunFam	G3DSA:1.20.5.5270:FF:000002	Lon protease homolog
1	118	Gene3D	G3DSA:2.30.130.40	-
1	118	InterPro	IPR046336	Lon protease, N-terminal domain superfamily
10	201	SUPERFAMILY	SSF88697	PUA domain-like
10	201	InterPro	IPR015947	PUA-like superfamily

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 · FPocket

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

Site 1 FPocket #7

0.758

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Surrounding area

Site 2 FPocket #44

0.29

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.783

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Surrounding area

Site 2 P2Rank #2

0.302

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Surrounding area

Site 3 P2Rank #3

0.108

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Surrounding area

Site 4 P2Rank #4

0.074

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Surrounding area

Site 5 P2Rank #5

0.022

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Surrounding area

Residue sets

UniProt: Active site:636-636

UniProt: Active site:679-679

UniProt: Binding site:313-320

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.77

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Surrounding area

Site 2 P2Rank #2

0.349

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Surrounding area

Site 3 P2Rank #3

0.131

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Surrounding area

Site 4 P2Rank #4

0.114

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Surrounding area

Site 5 P2Rank #5

0.055

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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_A0A0H3GJ60	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03674	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.

74 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 24 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 18 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

4KZ PDB via homolog 418.3 Da · LogP 0.56 · TPSA 124.4 Open detail RCSB PDB

AGS PDB via homolog Detail RCSB PDB

BO2 PDB via homolog Detail RCSB PDB

PE4 PDB via homolog Detail RCSB PDB

PE8 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
4KZ RCSB PDB	4YPL	A0A059VAZ3	418.3 Da LogP 0.56 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](Cc1ccccc1)NC(=O)[C@H](Cc2ccccc2)NC(=O)c…`
AGS RCSB PDB	6WQH	A0A059VAZ3	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BO2 RCSB PDB	6X27	P36776	384.2 Da LogP 0.36 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)c2cn…`
PE4 RCSB PDB	3K1J	B6YU74	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
PE8 RCSB PDB	3K1J	B6YU74	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCCOCCO)O`
UFY RCSB PDB	6WZV	P36776	384.2 Da LogP 0.36 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](CC(C)C)NC(=O)[C@@H](Cc1ccccc1)NC(=O)c2c…`

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
UKS ChEMBL	P36776	7.77 ~17.0 nM	398.3 Da LogP 0.89 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](CCCc1ccccc1)NC(=O)[C@@H](CCC)NC(=O)c2cn…`
CHEMBL4856865 ChEMBL	P36776	7.75 ~17.8 nM	446.3 Da LogP 1.34 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](CCCc1ccccc1)B…`
CHEMBL4864108 ChEMBL	P36776	7.47 ~33.9 nM	432.3 Da LogP 0.95 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](CCc1ccccc1)B(…`
CHEMBL4877126 ChEMBL	P36776	7.42 ~38.0 nM	336.2 Da LogP 0.06 TPSA 124.4	✓ Ro5	✓ Clean	`CCCC[C@H](NC(=O)[C@@H](CCC)NC(=O)c1cnccn1)B(O)O`
CHEMBL4870013 ChEMBL	P36776	7.23 ~58.9 nM	415.3 Da LogP 1.71 TPSA 124.7	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1oc(C)nc1C)C(=O)N[C@@H](CCCc1c…`
CHEMBL4862424 ChEMBL	P36776	7.19 ~64.6 nM	412.3 Da LogP 1.14 TPSA 124.4	✓ Ro5	✓ Clean	`CC(C)CCC[C@H](NC(=O)[C@@H](Cc1ccccc1)NC(=O)c1cn…`
CHEMBL4870902 ChEMBL	P36776	7.11 ~77.6 nM	477.2 Da LogP 1.27 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](CCCCCBr)B(O)O…`
CHEMBL4850612 ChEMBL	P36776	7.04 ~91.2 nM	424.3 Da LogP 1.28 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](CC1CCCCC1)B(O…`
CHEMBL4876920 ChEMBL	P36776	7.04 ~91.2 nM	384.2 Da LogP 0.50 TPSA 124.4	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CCc1ccccc…`
CHEMBL4856768 ChEMBL	P36776	7.03 ~93.3 nM	350.2 Da LogP 0.31 TPSA 124.4	✓ Ro5	✓ Clean	`CCCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CC(C)C)B…`
CHEMBL4847335 ChEMBL	P36776	6.96 ~109.6 nM	418.3 Da LogP 0.56 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)B(O…`
CHEMBL4863384 ChEMBL	P36776	6.87 ~134.9 nM	376.3 Da LogP 0.84 TPSA 124.4	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CC1CCCCC1…`
CHEMBL4847763 ChEMBL	P36776	6.86 ~138.0 nM	390.3 Da LogP 1.09 TPSA 124.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](CC1CCCCC1)NC(=O)c1cncc…`
CHEMBL4861871 ChEMBL	P36776	6.73 ~186.2 nM	336.2 Da LogP -0.08 TPSA 124.4	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CC(C)C)B(…`
CHEMBL4853599 ChEMBL	P36776	6.39 ~407.4 nM	322.2 Da LogP -0.47 TPSA 124.4	✓ Ro5	✓ Clean	`CC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CC(C)C)B(O…`
CHEMBL4864045 ChEMBL	P36776	6.36 ~436.5 nM	308.1 Da LogP -0.86 TPSA 124.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](C)NC(=O)c1cnccn1)B(O)O`
CHEMBL4859172 ChEMBL	P36776	6.26 ~549.5 nM	336.2 Da LogP -0.23 TPSA 124.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](NC(=O)c1cnccn1)C(C)C)B(…`
CHEMBL4850826 ChEMBL	P36776	6.25 ~562.3 nM	370.2 Da LogP 0.11 TPSA 124.4	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](Cc1ccccc1…`

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
ZINC12501520 ZINC	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716 ZINC	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5650743 ZINC	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC12360002 ZINC	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.768	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	0.763	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	0.763	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	0.763	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	0.763	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	0.750	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	0.750	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	0.750	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	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC16698311 ZINC	0.739	271.3 Da LogP 0.90 TPSA 92.2	✓ Ro5	✓ Clean	`O=C(N[C@@H](Cc1ccccc1)C(=O)O)c1cnccn1`
ZINC22146066 ZINC	0.739	271.3 Da LogP 0.90 TPSA 92.2	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)O)c1cnccn1`
ZINC31475423 ZINC	0.738	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC31516918 ZINC	0.730	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC105469665 ZINC	0.729	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	0.729	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	0.729	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	0.729	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	0.729	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.