Protein target profile

KP13_00023

ATP synthase subunit alpha

Genome: KpKP13 Gene: AHE47132.1 atpA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GZ37

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Length 513

Pocket druggability 0.735

Direct ligand evidence 0 62 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.73. This is a computational pocket signal, not binding validation. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 11 structural and 1 bioactivity records.

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 (%): 56.579 Lower values reduce human off-target concern.
Human E-value: 5.549999999999999e-48
Gut microbiome similarity: 66.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.246 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: 93.89 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 0.735

Structure A0A0H3GZ37

Pocket Pocket 3

P2Rank 0.466

Structure A0A0H3GZ37

Pocket Pocket 1

ColabFold model

FPocket 0.738 · Pocket 14

P2Rank 0.504 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3157 / 4744 genomes with a hit

Prevalence 66.5%

Cross-references

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

Sequence

UniProt A0A0H3GZ37

Chemistry

ChEMBL CHEMBL2063416

Sequence

Primary amino-acid sequence viewer.

MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLAECMQGEMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLENDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIDAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELAKIGSFEAALLAYVDRDHAPLMQEINQSGGYNDEIEGKLKGILDSFKATQSW

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

7.1.2.2

Gene Ontology (GO)

GO:0046034 The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
GO:1902600 The directed movement of a proton across a membrane.
GO:0032559 Binding to an adenyl ribonucleotide, any compound consisting of adenosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.
GO:0015986 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a membrane to generate an electrochemical gradient (proton-motive force).
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0045261 OBSOLETE. The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.
GO:0046933 Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + phosphate + 5 H+(out) => ATP + H2O + 4 H+(in).
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0045259 A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient.
GO:0043531 Binding to ADP, adenosine 5'-diphosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
149	375	Pfam	PF00006	ATP synthase alpha/beta family, nucleotide-binding domain
149	375	InterPro	IPR000194	ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
27	93	CDD	cd18116	ATP-synt_F1_alpha_N
2	512	NCBIfam	TIGR00962	F0F1 ATP synthase subunit alpha
2	512	InterPro	IPR005294	ATP synthase, F1 complex, alpha subunit
1	512	Hamap	MF_01346	ATP synthase subunit alpha [atpA].
1	512	InterPro	IPR005294	ATP synthase, F1 complex, alpha subunit
382	507	Pfam	PF00306	ATP synthase alpha/beta chain, C terminal domain
382	507	InterPro	IPR000793	ATP synthase, alpha subunit, C-terminal
10	94	SUPERFAMILY	SSF50615	N-terminal domain of alpha and beta subunits of F1 ATP synthase
10	94	InterPro	IPR036121	ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily
94	378	CDD	cd01132	F1-ATPase_alpha_CD
94	378	InterPro	IPR033732	ATP synthase, F1 complex, alpha subunit nucleotide-binding domain
383	511	SUPERFAMILY	SSF47917	C-terminal domain of alpha and beta subunits of F1 ATP synthase
1	93	FunFam	G3DSA:2.40.30.20:FF:000001	ATP synthase subunit alpha
366	375	ProSitePatterns	PS00152	ATP synthase alpha and beta subunits signature.
366	375	InterPro	IPR020003	ATPase, alpha/beta subunit, nucleotide-binding domain, active site
94	382	FunFam	G3DSA:3.40.50.300:FF:000002	ATP synthase subunit alpha
383	513	FunFam	G3DSA:1.20.150.20:FF:000001	ATP synthase subunit alpha
383	513	Gene3D	G3DSA:1.20.150.20	-
383	513	InterPro	IPR038376	ATP synthase, alpha subunit, C-terminal domain superfamily
3	510	PANTHER	PTHR48082	ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
3	510	InterPro	IPR005294	ATP synthase, F1 complex, alpha subunit
29	92	Pfam	PF02874	ATP synthase alpha/beta family, beta-barrel domain
29	92	InterPro	IPR004100	ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain
386	510	CDD	cd18113	ATP-synt_F1_alpha_C
386	510	InterPro	IPR000793	ATP synthase, alpha subunit, C-terminal
94	382	Gene3D	G3DSA:3.40.50.300	-
94	382	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
96	381	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
96	381	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
1	93	Gene3D	G3DSA:2.40.30.20	-
1	93	InterPro	IPR023366	ATP synthase subunit alpha, N-terminal domain-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 #3

0.735

Likely same site as P2Rank 4 0.7 Å 11 shared residues 100% of smaller site

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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

0.466

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Surrounding area

Site 2 P2Rank #2

0.258

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Surrounding area

Site 3 P2Rank #3

0.163

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Surrounding area

Site 4 P2Rank #4

0.151

Likely same site as FPocket 3 0.7 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.079

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Surrounding area

Residue sets

UniProt: Binding site:169-176

UniProt: Site:373-373 Required for activity

Binding pockets · FPocket

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

Site 1 FPocket #14

0.738

Likely same site as P2Rank 3 1.8 Å 12 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #1

0.25

Unusual size

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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

0.504

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Surrounding area

Site 2 P2Rank #2

0.294

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Surrounding area

Site 3 P2Rank #3

0.189

Likely same site as FPocket 14 1.8 Å 12 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.105

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Surrounding area

Site 5 P2Rank #5

0.078

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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_A0A0H3GZ37	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00023	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.

62 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AF3 PDB via homolog 84.0 Da · LogP 0.88 · TPSA 0.0 Open detail RCSB PDB

ALF PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

AUR PDB via homolog Detail RCSB PDB

AZI 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
AF3 RCSB PDB	1E1R	P19483	84.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al](F)F`
ALF RCSB PDB	1H8E	P19483	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
ANP RCSB PDB	3OAA	P0ABB0	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
AUR RCSB PDB	1COW	P19483	460.5 Da LogP 3.10 TPSA 104.4	✓ Ro5	✓ Clean	`CC[C@@H]1[C@]2([C@H]([C@@](O1)([C@H]([C@@H](O2)…`
AZI RCSB PDB	2CK3	P19483	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BEF RCSB PDB	1W0J	P19483	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
QUE RCSB PDB	2JJ2	P19483	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	Alert	`c1cc(c(cc1C2=C(C(=O)c3c(cc(cc3O2)O)O)O)O)O`
STL RCSB PDB	2JIZ	P19483	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`c1cc(ccc1\C=C\c2cc(cc(c2)O)O)O`
TS6 RCSB PDB	4YXW	P19483	114.1 Da LogP 0.01 TPSA 57.5	✓ Ro5	✓ Clean	`OP(=O)(O)S`
TTX RCSB PDB	1KMH	P06450	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`C[C@H]1C(=O)N[C@H](C(=O)N(/C(=C\c2ccccc2)/C(=O)…`
VO4 RCSB PDB	2F43	P15999	114.9 Da LogP -3.69 TPSA 86.2	✓ Ro5	✓ Clean	`[O-][V](=O)([O-])[O-]`

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
CHEMBL2063416 ChEMBL	P25705	—	716.8 Da LogP 1.65 TPSA 238.1	3 viol.	Alert	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]21)NCCOCCO…`

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
ZINC100230999 ZINC	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@H](C)N(C)C(=O)CNC(=O)/C(=…`
ZINC12353732 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2cc(O)cc(O)c2)cc1`
ZINC1531101 ZINC	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@H]1NC(=O)[C@@H](C)N(C)C(=O)CNC(=O)C(=C…`
ZINC1857524289 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2cc(O)cc(O)c2)cc1`
ZINC2356469567 ZINC	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@@H](C)N(C)C(=O)CNC(=O)C(=…`
ZINC33955459 ZINC	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@H](C)N(C)C(=O)CNC(=O)/C(=…`
ZINC3875061 ZINC	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@H]1NC(=O)[C@H](C)N(C)C(=O)CNC(=O)C(=Cc…`
ZINC4097591 ZINC	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@H](C)N(C)C(=O)CNC(=O)C(=C…`
ZINC6787 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2cc(O)cc(O)c2)cc1`
ZINC12360002 ZINC	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC3874317 ZINC	0.757	318.2 Da LogP 1.69 TPSA 151.6	1 viol.	Alert	`O=c1c(O)c(-c2cc(O)c(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC13518964 ZINC	0.741	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	0.741	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	0.741	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	0.741	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	0.741	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	0.741	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	0.741	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	0.741	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	0.741	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	0.741	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	0.741	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	0.741	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	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC13319959 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2ccc(O)cc2)cc1`
ZINC1510311 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2ccc(O)cc2)cc1`
ZINC1875408805 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2ccc(O)cc2)cc1`
ZINC4096224 ZINC	0.729	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	0.726	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	0.726	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	0.726	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	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC34544488 ZINC	0.720	230.2 Da LogP 3.41 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2cc(O)cc(F)c2)cc1`
ZINC120273 ZINC	0.718	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)cc(O)c12`
ZINC105372833 ZINC	0.712	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	0.712	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	0.712	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	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC49588452 ZINC	0.708	246.7 Da LogP 3.92 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C/c2ccc(Cl)cc2)c1`
ZINC71622042 ZINC	0.708	246.7 Da LogP 3.92 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C\c2ccc(Cl)cc2)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.