KpATCC43816 Protein target profile

copper-translocating P-type ATPase

Accession: VK055_2084

Gene: AIK80689.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GJB4

Export view

Length 833

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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 6 structural and 0 bioactivity records.

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: 1.14e-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 (%): 55.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 86.32 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 0.899 · Pocket 1

FPocket 0.569 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 115 / 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

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSNTIDLTLDGLSCGHCVKRVKESLEQRPDVEQAEVTLTEAHVTGSASAQALIDTVKQAGYGAELSHPKAKPLAESSIPSEALTAATPELPAAHDEDDSQQLLINGMSCASCVSRVQNALAAVPGVSQARVNLAERTALVMGSASAAELVQAVEKAGYGAEAIEDDLQRRERQQETALATMKRFRWQAIVALLVGVPVMVWGMIGDNMMVSDDNRSLWLVIGLVTLAVMVFAGGHFYRSAWKSLKNGTATMDTLVALGTSVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALEKLLDLTPPSARVVTPEGEKDLPLAEVQAGMTLRLTTGDRVPVDGMISQGEAWFDEAMLTGEPVPQQKGDGDAIHAGTVVQDGSVLFTASAVGSQTTLARIIRMVRQAQSSKPEIGQLADKISAVFVPAVVVIALISAAIWYFFGPAPQIVYTLVIATTVLIIACPCALGLATPMSIISGVGRAAEYGVLVRDADALQRASELDTLVFDKTGTLTEGKPQVVAVKTFAGVDEHTALRLAAALEQGSSHPLARAILDKAADGPLPEVSGFRTLRGLGVSGEAEGHRLLLGNQALLNEQHINTAEVESEMTAQASRGATPVLLAVDGQAAALFAIRDPLREDSVDALARLHRQGYRLVMLTGDNPTTAKAIAKEAGIDEVIAGVLPDGKADAIKRLQSQGHKVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLHGVADALAISKATLRNMKQNLLGAFVYNSLGIPIAAGILWPLTGTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE

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: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: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: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:0046872 Binding to a metal ion.
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: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: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.

86 records

Show feature table

Start	End	DB	Term	Name
140	160	PRINTS	PR00943	Copper-transporting ATPase signature
503	518	PRINTS	PR00943	Copper-transporting ATPase signature
441	455	PRINTS	PR00943	Copper-transporting ATPase signature
694	711	PRINTS	PR00943	Copper-transporting ATPase signature
236	255	PRINTS	PR00943	Copper-transporting ATPase signature
249	271	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
487	776	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
238	248	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
306	422	Gene3D	G3DSA:2.70.150.10	-
435	457	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
501	768	SFLD	SFLDG00002	C1.7: P-type atpase like
522	528	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
522	528	InterPro	IPR018303	P-type ATPase, phosphorylation site
801	823	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
101	163	Gene3D	G3DSA:3.30.70.100	-
531	650	FunFam	G3DSA:3.40.1110.10:FF:000036	Copper-exporting P-type ATPase
285	781	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
285	781	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
6	64	CDD	cd00371	HMA
6	64	InterPro	IPR006121	Heavy metal-associated domain, HMA
215	237	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
98	161	ProSiteProfiles	PS50846	Heavy-metal-associated domain profile.
98	161	InterPro	IPR006121	Heavy metal-associated domain, HMA
283	301	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
531	650	Gene3D	G3DSA:3.40.1110.10	-
531	650	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
100	164	SUPERFAMILY	SSF55008	HMA, heavy metal-associated domain
100	164	InterPro	IPR036163	Heavy metal-associated domain superfamily
462	484	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
463	486	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
205	215	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
458	462	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
251	826	NCBIfam	TIGR01525	heavy metal translocating P-type ATPase
251	826	InterPro	IPR027256	P-type ATPase, subfamily IB
3	67	SUPERFAMILY	SSF55008	HMA, heavy metal-associated domain
3	67	InterPro	IPR036163	Heavy metal-associated domain superfamily
512	767	Gene3D	G3DSA:3.40.50.1000	-
512	767	InterPro	IPR023214	HAD superfamily
797	801	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	183	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
501	768	SFLD	SFLDF00027	p-type atpase
501	768	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
104	133	ProSitePatterns	PS01047	Heavy-metal-associated domain.
104	133	InterPro	IPR017969	Heavy-metal-associated, conserved site
3	64	ProSiteProfiles	PS50846	Heavy-metal-associated domain profile.
3	64	InterPro	IPR006121	Heavy metal-associated domain, HMA
216	237	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
101	163	FunFam	G3DSA:3.30.70.100:FF:000030	Copper-exporting P-type ATPase
254	276	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
518	823	SUPERFAMILY	SSF56784	HAD-like
518	823	InterPro	IPR036412	HAD-like superfamily
232	826	NCBIfam	TIGR01511	copper-translocating P-type ATPase
8	61	Pfam	PF00403	Heavy-metal-associated domain
8	61	InterPro	IPR006121	Heavy metal-associated domain, HMA
104	158	Pfam	PF00403	Heavy-metal-associated domain
104	158	InterPro	IPR006121	Heavy metal-associated domain, HMA
101	161	CDD	cd00371	HMA
101	161	InterPro	IPR006121	Heavy metal-associated domain, HMA
740	752	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
520	534	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
368	382	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
642	653	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
664	674	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
717	736	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
272	282	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
290	794	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
290	794	InterPro	IPR001757	P-type ATPase
321	418	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
321	418	InterPro	IPR008250	P-type ATPase, A domain superfamily
302	434	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
517	731	Pfam	PF00702	haloacid dehalogenase-like hydrolase
306	422	FunFam	G3DSA:2.70.150.10:FF:000020	Copper-exporting P-type ATPase A
802	823	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
186	828	CDD	cd02094	P-type_ATPase_Cu-like
777	796	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
188	205	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
435	457	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
777	796	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
824	833	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
67	87	MobiDBLite	mobidb-lite	consensus disorder prediction
282	301	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
4	829	PANTHER	PTHR43520	ATP7, ISOFORM B
184	204	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
319	499	Pfam	PF00122	E1-E2 ATPase
4	66	FunFam	G3DSA:3.30.70.100:FF:000032	Copper-exporting P-type ATPase
4	66	Gene3D	G3DSA:3.30.70.100	-

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.434

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.26

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.249

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.234

Show in viewer

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

Show in viewer

Surrounding area

Pocket 2 FPocket #42

0.306

Show in viewer

Surrounding area

Pocket 3 FPocket #24

0.292 Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.899

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.389

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.326

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.29

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.244

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.569

Show in viewer

Surrounding area

Pocket 2 FPocket #2

0.526

Show in viewer

Surrounding area

Pocket 3 FPocket #4

0.464

Show in viewer

Surrounding area

Pocket 4 FPocket #39

0.462

Show in viewer

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 VK055_2084	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.