KpKP13 Protein target profile

Copper-exporting P-type ATPase A

Accession: KP13_03607

Gene: AHE45950.1 copA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GJB4

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Length 851

Pocket druggability (P2Rank · AlphaFold DB model) 0.971

Direct ligand evidence 0 56 total records

Functional annotation 1 EC 16 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 0.97, FPocket 0.82). 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 0.82. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. 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 (%): 41.284 Lower values reduce human off-target concern.
Human E-value: 1.09e-10
Gut microbiome similarity: 2.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 85.21 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) 0.971

Structure A0A0H3GJB4

Pocket Pocket 1

Druggability (FPocket) 0.82

Structure A0A0H3GJB4

Pocket Pocket 33

ColabFold model

P2Rank 0.758 · Pocket 1

FPocket 0.965 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 116 / 4744 genomes with a hit

Prevalence 2.4%

Cross-references

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

Sequence

UniProt A0A0H3GJB4

Sequence

Primary amino-acid sequence viewer.

MKEWVWSIVDRKIIQELFMSNTIDLTLDGLSCGHCVKRVKESLEQRPDVEQAEVTLTEAHVTGSASAQALIDTVKQAGYGAELSHPKAKPLAESSIPSEALTAATPELPAAHDEDDSQQLLINGMSCASCVSRVQNALAAVPGVSQARVNLAERTALVMGSASAAELVQAVEKAGYGAEAIEDDLQRRERQQETALATMKRFRWQAIVALLVGVPVMVWGMIGDNMMVSDDNRSLWLVIGLVTLAVMVFAGDHFYRSAWKSLKNGTATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPSARVVTPEGEKDLPLAEVQAGMTLRLTTGDRVPVDGMISQGEAWFDEAMLTGEPVPQQKGDGDAIHAGTVVQDGSVLFTASAVGSQTTLARIIRMVRQAQSSKPEIGQLADKISAVFVPAVVVIALISAAIWYFFGPAPQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEYGVLVRDADALQRASELDTLVFDKTGTLTEGKPQVVAVKTFAGVDEHTALRLAAALEQGSSHPLARAILDKAADGPLPEVSGFRTLRGLGVNGEAEGHRLLLGNQALLNEQHINTAEVESEMTAQASRGATPVLLAVDGQAAALFAIRDPLREDSVDALARLHRQGYRLVMLTGDNPTTAKAIAKEAGIDEVIAGVLPDGKADAIKRLQSQGHKVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLHGVADALAISKATLRNMKQNLLGAFVYNSLGIPIAAGILWPLTGTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 16 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

7.2.2.8

Gene Ontology (GO)

GO:0006812 The directed movement of a monoatomic cation, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Monatomic cations (also called simple cations) are positively charged ions consisting of exactly one atom.
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:0046872 Binding to a metal ion.
GO:0005215 Enables the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, accross or in between cells.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
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:0019829 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + cation(out) = ADP + phosphate + cation(in).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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:0005507 Binding to a copper (Cu) ion.
GO:0043682 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cu2+(in) = ADP + phosphate + Cu2+(out).
GO:0140581 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cu+(in) = ADP + phosphate + Cu+(out).
GO:0060003 The directed movement of copper ions out of a cell or organelle.
GO:0055070 Any process involved in the maintenance of an internal steady state of copper ions within an organism or cell.
GO:0075523 A process which occurs during viral translation, which involves a translational recoding mechanism called programmed ribosomal frameshifting. This causes the ribosome to alter its reading of the mRNA to an a different open reading frame to produce alternate viral proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

87 records

Show feature table

Start	End	DB	Term	Name
1	201	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
453	475	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
269	844	NCBIfam	TIGR01525	heavy metal translocating P-type ATPase
269	844	InterPro	IPR027256	P-type ATPase, subfamily IB
256	266	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
158	178	PRINTS	PR00943	Copper-transporting ATPase signature
254	273	PRINTS	PR00943	Copper-transporting ATPase signature
521	536	PRINTS	PR00943	Copper-transporting ATPase signature
712	729	PRINTS	PR00943	Copper-transporting ATPase signature
459	473	PRINTS	PR00943	Copper-transporting ATPase signature
22	847	PANTHER	PTHR43520	ATP7, ISOFORM B
267	289	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
301	319	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
116	179	ProSiteProfiles	PS50846	Heavy-metal-associated domain profile.
116	179	InterPro	IPR006121	Heavy metal-associated domain, HMA
339	436	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
339	436	InterPro	IPR008250	P-type ATPase, A domain superfamily
453	475	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
819	841	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
530	785	Gene3D	G3DSA:3.40.50.1000	-
530	785	InterPro	IPR023214	HAD superfamily
820	841	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
303	798	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
303	798	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
505	794	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
202	222	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
519	786	SFLD	SFLDF00027	p-type atpase
519	786	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
540	546	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
540	546	InterPro	IPR018303	P-type ATPase, phosphorylation site
233	250	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
480	502	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
549	668	FunFam	G3DSA:3.40.1110.10:FF:000036	Copper-exporting P-type ATPase
119	179	CDD	cd00371	HMA
119	179	InterPro	IPR006121	Heavy metal-associated domain, HMA
324	440	FunFam	G3DSA:2.70.150.10:FF:000020	Copper-exporting P-type ATPase A
842	851	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
21	82	ProSiteProfiles	PS50846	Heavy-metal-associated domain profile.
21	82	InterPro	IPR006121	Heavy metal-associated domain, HMA
22	84	Gene3D	G3DSA:3.30.70.100	-
22	84	FunFam	G3DSA:3.30.70.100:FF:000032	Copper-exporting P-type ATPase
536	841	SUPERFAMILY	SSF56784	HAD-like
536	841	InterPro	IPR036412	HAD-like superfamily
795	814	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
223	233	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
118	182	SUPERFAMILY	SSF55008	HMA, heavy metal-associated domain
118	182	InterPro	IPR036163	Heavy metal-associated domain superfamily
337	517	Pfam	PF00122	E1-E2 ATPase
549	668	Gene3D	G3DSA:3.40.1110.10	-
549	668	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
290	300	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
122	176	Pfam	PF00403	Heavy-metal-associated domain
122	176	InterPro	IPR006121	Heavy metal-associated domain, HMA
26	79	Pfam	PF00403	Heavy-metal-associated domain
26	79	InterPro	IPR006121	Heavy metal-associated domain, HMA
308	812	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
308	812	InterPro	IPR001757	P-type ATPase
535	749	Pfam	PF00702	haloacid dehalogenase-like hydrolase
386	400	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
735	754	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
758	770	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
682	692	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
660	671	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
538	552	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
119	181	Gene3D	G3DSA:3.30.70.100	-
320	452	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
324	440	Gene3D	G3DSA:2.70.150.10	-
206	223	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
119	181	FunFam	G3DSA:3.30.70.100:FF:000030	Copper-exporting P-type ATPase
519	786	SFLD	SFLDS00003	Haloacid Dehalogenase
204	846	CDD	cd02094	P-type_ATPase_Cu-like
21	85	SUPERFAMILY	SSF55008	HMA, heavy metal-associated domain
21	85	InterPro	IPR036163	Heavy metal-associated domain superfamily
300	319	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
795	814	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
250	844	NCBIfam	TIGR01511	copper-translocating P-type ATPase
234	255	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
122	151	ProSitePatterns	PS01047	Heavy-metal-associated domain.
122	151	InterPro	IPR017969	Heavy-metal-associated, conserved site
27	56	ProSitePatterns	PS01047	Heavy-metal-associated domain.
27	56	InterPro	IPR017969	Heavy-metal-associated, conserved site
476	480	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
481	504	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
271	290	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
24	82	CDD	cd00371	HMA
24	82	InterPro	IPR006121	Heavy metal-associated domain, HMA
815	819	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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

0.971

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Surrounding area

Pocket 2 P2Rank #2

0.434

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Surrounding area

Pocket 3 P2Rank #3

0.26

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Surrounding area

Pocket 4 P2Rank #4

0.249

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Surrounding area

Pocket 5 P2Rank #5

0.234

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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 #33

0.82 Unusual size

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Surrounding area

Pocket 2 FPocket #42

0.306

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Surrounding area

Pocket 3 FPocket #24

0.292 Unusual size

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.758

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Surrounding area

Pocket 2 P2Rank #2

0.296

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Surrounding area

Pocket 3 P2Rank #3

0.292

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Surrounding area

Pocket 4 P2Rank #4

0.211

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Surrounding area

Pocket 5 P2Rank #5

0.135

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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

0.965 Unusual size

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Surrounding area

Pocket 2 FPocket #3

0.558

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Surrounding area

Pocket 3 FPocket #41

0.453

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Surrounding area

Pocket 4 FPocket #2

0.435

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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_A0A0H3GJB4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03607	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

9UX PDB via homolog 292.0 Da · LogP -0.02 · TPSA 34.1 Open detail RCSB PDB

ACP PDB via homolog Detail RCSB PDB

ALF PDB via homolog Detail RCSB PDB

BEF PDB via homolog Detail RCSB PDB

MGF 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
9UX RCSB PDB	6A71	P35670	292.0 Da LogP -0.02 TPSA 34.1	✓ Ro5	✓ Clean	`O=[MoH2]1S[MoH2](=O)S1`
ACP RCSB PDB	3A1C	O29777	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)…`
ALF RCSB PDB	4UMW	Q3YW59	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
BEF RCSB PDB	4UMV	Q3YW59	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
MGF RCSB PDB	4BEV	Q5ZWR1	81.3 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-](F)F`
NH4 RCSB PDB	5LBD	Q9SZC9	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`

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).

No ChEMBL hits found through similar proteins.

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
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](…`
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)…`
ZINC5615251 ZINC	0.700	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615253 ZINC	0.700	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC5615258 ZINC	0.700	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615263 ZINC	0.700	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC31516918 ZINC	0.692	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…`
ZINC1582675 ZINC	0.689	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730 ZINC	0.689	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486734 ZINC	0.689	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC5486740 ZINC	0.689	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`

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.