Protein target profile

VK055_1980

HAD ATPase, P-type, IC family protein

Genome: KpATCC43816 Gene: AIK80586.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GJR1

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Length 879

Pocket druggability 0.994

Direct ligand evidence 0 61 total records

Functional annotation 0 EC 14 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Second pocket predictor agrees P2Rank predicted binding-site probability 0.55. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 6 structural and 5 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 (%): 47.727 Lower values reduce human off-target concern.
Human E-value: 7.170000000000001e-21
Gut microbiome similarity: 1.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 38.453 Higher values support similarity to known essential genes.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 88.09 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 0.994

Structure A0A0H3GJR1

Pocket Pocket 16

P2Rank 0.547

Structure A0A0H3GJR1

Pocket Pocket 1

ColabFold model

FPocket 0.874 · Pocket 3

P2Rank 0.585 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 50 / 4744 genomes with a hit

Prevalence 1.1%

Cross-references

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

Sequence

UniProt A0A0H3GJR1

Chemistry

ChEMBL CHEMBL4514624 ChEMBL 7BS ChEMBL 7BL ChEMBL CHEMBL468766 ChEMBL CHEMBL4534285

Sequence

Primary amino-acid sequence viewer.

MLAQTKSQAAGLSSADAAERLNTCGPNALPEKKGKPGWLRFLAHFNDVLIYVLLAAAALTAIMGHWVDTLVILGVTVINALIGHIQESNAEKSLQGIRNMLSSDARVQRNGKHETIPTRDLVPGDIVILRAGDRVPADMRLIETHNLRVEEAILTGESTVVDKITDALEGDLPLGDRVNMVFSGTTVSAGGGVGVVTATGAQTELGHINQMMAGIEKHRTPLLVQMDKLGKAIFAIILAMMVALFIFSLALRDIPMGELLLSLISLAVAAVPEGLPAIISIILSLGVQTMARKRAIIRKLPTVETLGAMTVVCSDKTGTLTMNEMTVKAIITADCCYRVEGDSYEPQGRIFLEGSDEPVQVQPGTVLETWLRTIDLCNDSQLTQDERGLWGITGGPTEGALKVLAAKAQLPAVEARLVAKIPFDSQYKYMSTLQHIDGNARVLITGAPDVIFAMCREQMSRHGAVPFEAQYWEEEMARFARQGLRMVAAACKPASLDATTLNHEDLQEGLIFLGIAGMMDPPRPEAIDAIHACQTAGIRVKMITGDHPQTAMSIGQMLGITNSSQAMTGYQLEHMDDAALAKAAVEYDIFARTSPEHKLRLVKALQDNGEVVGMTGDGVNDAPALRQADVGIAMGIKGTEVTKEAADMVLTDDNFATIASSVKEGRRVYDNLKKTILFIMPTNLAQGLLIIIALLAGNIIPLTPVLILWMNMATSATLSFGLAFEAAERNVMNRPPRKTGQHVMDGFAVWRVAFVGSMIAIAAFILEAWLAPRGHSPEFIRTVLLQMLVTAQWVYMINCRSSDSFSLSMGLLRNKGIWLVTGVLLLMQLVIIYVPLMQSMFGTEALPLRYWFVTLVIGVAMFLVVEIEKRLTRRFRKTA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

14 GO

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
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: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: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:0012505 A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
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:0046872 Binding to a metal ion.
GO:0005391 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) + K+(out) = ADP + phosphate + Na+(out) + K+(in).
GO:0030007 A homeostatic process involved in the maintenance of a steady state level of potassium ions within a cell.
GO:0006883 A homeostatic process involved in the maintenance of a steady state level of sodium ions within a cell.
GO:1990573 The directed movement of potassium ions from outside of a cell, across the plasma membrane and into the cytosol.
GO:1902600 The directed movement of a proton across a membrane.
GO:0036376 The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

83 records

Show feature table

Start	End	DB	Term	Name
837	847	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
311	718	SUPERFAMILY	SSF56784	HAD-like
311	718	InterPro	IPR036412	HAD-like superfamily
5	59	Pfam	PF00690	Cation transporter/ATPase, N-terminus
5	59	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
310	322	FunFam	G3DSA:3.40.50.1000:FF:000001	Phospholipid-transporting ATPase IC
320	518	SUPERFAMILY	SSF81660	Metal cation-transporting ATPase, ATP-binding domain N
320	518	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
817	836	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
309	629	Pfam	PF00702	haloacid dehalogenase-like hydrolase
747	769	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
104	212	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
104	212	InterPro	IPR008250	P-type ATPase, A domain superfamily
779	796	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
266	288	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
11	869	CDD	cd02080	P-type_ATPase_cation
748	766	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
816	838	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
702	724	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
263	287	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
848	867	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
323	521	Gene3D	G3DSA:3.40.1110.10	-
323	521	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
868	879	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1	40	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
676	700	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
9	877	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
9	877	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
797	816	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
67	85	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
701	705	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
69	85	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
767	777	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
315	321	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
315	321	InterPro	IPR018303	P-type ATPase, phosphorylation site
295	668	SFLD	SFLDF00027	p-type atpase
295	668	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
229	251	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
615	631	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
615	631	InterPro	IPR001757	P-type ATPase
587	603	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
587	603	InterPro	IPR001757	P-type ATPase
784	805	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
784	805	InterPro	IPR001757	P-type ATPase
472	490	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
472	490	InterPro	IPR001757	P-type ATPase
647	672	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
647	672	InterPro	IPR001757	P-type ATPase
232	251	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
86	231	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
252	262	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
848	867	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
2	65	SMART	SM00831	Cation_ATPase_N_a_2
2	65	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
5	866	PANTHER	PTHR42861	CALCIUM-TRANSPORTING ATPASE
310	660	Gene3D	G3DSA:3.40.50.1000	-
310	660	InterPro	IPR023214	HAD superfamily
81	213	FunFam	G3DSA:2.70.150.10:FF:000160	Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
513	660	FunFam	G3DSA:3.40.50.1000:FF:000028	Calcium-transporting P-type ATPase, putative
706	727	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
100	293	Pfam	PF00122	E1-E2 ATPase
675	697	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
295	668	SFLD	SFLDG00002	C1.7: P-type atpase like
64	68	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
71	333	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
71	333	InterPro	IPR001757	P-type ATPase
583	708	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
583	708	InterPro	IPR001757	P-type ATPase
41	63	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
700	871	Pfam	PF00689	Cation transporting ATPase, C-terminus
700	871	InterPro	IPR006068	Cation-transporting P-type ATPase, C-terminal
288	675	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
41	63	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
11	213	Gene3D	G3DSA:2.70.150.10	-
778	796	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
313	327	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
514	525	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
536	546	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
150	164	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
639	651	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
615	634	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
43	873	Gene3D	G3DSA:1.20.1110.10	-
728	747	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.

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 #16

0.994

Unusual size

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Surrounding area

Site 2 FPocket #13

0.614

Likely same site as P2Rank 4 0.6 Å 9 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

0.547

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Surrounding area

Site 2 P2Rank #2

0.423

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Surrounding area

Site 3 P2Rank #3

0.293

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Surrounding area

Site 4 P2Rank #4

0.22

Likely same site as FPocket 13 0.6 Å 9 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.21

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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

0.585

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Surrounding area

Site 2 P2Rank #2

0.517

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Surrounding area

Site 3 P2Rank #3

0.331

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Surrounding area

Site 4 P2Rank #4

0.275

Likely same site as FPocket 3 1.2 Å 10 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.26

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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_A0A0H3GJR1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1980	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.

61 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 5 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ACP PDB via homolog 505.2 Da · LogP -1.52 · TPSA 269.9 Open detail RCSB PDB

ALF PDB via homolog Detail RCSB PDB

BEF PDB via homolog Detail RCSB PDB

CZA 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
ACP RCSB PDB	6HXB	P11607-2	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	6ZHG	Q8Y8Q5	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
BEF RCSB PDB	6LN8	P16615	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
CZA RCSB PDB	5MPM	P11607-2	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`CC(=O)C1=C(N2[C@H](C1=O)[C@H]3c4c[nH]c5c4c(ccc5…`
MGF RCSB PDB	5MPM	P11607-2	81.3 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-](F)F`
PCW RCSB PDB	7BT2	P16615-2	787.1 Da LogP 12.36 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@H](CO[P@@](=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
CHEMBL4514624 ChEMBL	P16615	8.89 ~1.3 nM	622.8 Da LogP 3.24 TPSA 142.4	2 viol.	✓ Clean	`C/C=C/C/C(C)=C\[C@@H]1OC(=O)C[C@H](O[C@@H]2O[C@…`
7BS ChEMBL	P16615	7.96 ~11.0 nM	604.8 Da LogP 4.49 TPSA 123.9	1 viol.	✓ Clean	`C/C=C/C/C(=C\[C@H]1C/C=C/C=C/C[C@@H](/C=C(/[C@H…`
7BL ChEMBL	P16615	7.57 ~26.9 nM	428.6 Da LogP 6.01 TPSA 55.8	1 viol.	✓ Clean	`C/C=C/C/C(=C\[C@H]1C/C=C/C=C/C[C@@H](/C=C(/[C@H…`
CHEMBL468766 ChEMBL	P16615	7.05 ~89.1 nM	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`C/C(O)=C1\C(=O)[C@@H]2[C@H]3c4c[nH]c5cccc(c45)C…`
CHEMBL4534285 ChEMBL	P16615	6.68 ~208.9 nM	650.8 Da LogP 3.93 TPSA 172.0	2 viol.	✓ Clean	`C/C=C(/C)C(=O)O[C@H]1C(C)=C2[C@H]([C@@H]1OC(=O)…`

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
ZINC100006436 ZINC	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`C/C(O)=C1\C(=O)[C@H]2[C@@H]3c4c[nH]c5cccc(c45)C…`
ZINC100006437 ZINC	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`C/C(O)=C1\C(=O)[C@@H]2[C@@H]3c4c[nH]c5cccc(c45)…`
ZINC100006438 ZINC	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`C/C(O)=C1\C(=O)[C@H]2[C@@H]3c4c[nH]c5cccc(c45)C…`
ZINC100067111 ZINC	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`C/C(O)=C1\C(=O)[C@@H]2[C@H]3c4c[nH]c5cccc(c45)C…`
ZINC110970687 ZINC	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`C/C(O)=C1/C(=O)[C@@H]2[C@H]3c4c[nH]c5cccc(c45)C…`
ZINC29084193 ZINC	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`CC(=O)C1=C(O)N2[C@H](C1=O)[C@H]1c3c[nH]c4cccc(c…`
ZINC3977769 ZINC	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`C/C(O)=C1\C(=O)[C@@H]2[C@@H]3c4c[nH]c5cccc(c45)…`
ZINC13544781 ZINC	0.880	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	0.880	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
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…`
ZINC13543439 ZINC	0.860	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441 ZINC	0.860	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)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(=…`
ZINC33822387 ZINC	0.804	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC33822389 ZINC	0.804	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)…`
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…`
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…`

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.