Protein profile

PA1429

cation-transporting P-type ATPase

Genome: NC_002516.2

Gene: PA1429 Structure source: AlphaFold UniProt Q9I3R5

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Amino acids 902

Annotations 7

Features 81

PDB binders 5

Druggability 0.898

Overview

Basic information about this protein and its source genome.

Accession: PA1429
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1429
Status: annotated
Amino acids: 902
Structure source: AlphaFold

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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. 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:0005388 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Ca2+(in) = ADP + phosphate + Ca2+(out). 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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 53.488
Human E-value: 1.2500000000000001e-22
Gut microbiome off-target: hit
Essential (DEG): N
Localization: CytoplasmicMembrane

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.898

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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:0005388 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Ca2+(in) = ADP + phosphate + Ca2+(out).
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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

81 records

Show feature table

Start	End	DB	Term	Name
329	650	Pfam	PF00702	haloacid dehalogenase-like hydrolase
11	84	SMART	SM00831	Cation_ATPase_N_a_2
11	84	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
13	78	Pfam	PF00690	Cation transporter/ATPase, N-terminus
13	78	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
790	800	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
19	879	PANTHER	PTHR42861	CALCIUM-TRANSPORTING ATPASE
251	272	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
329	681	Gene3D	G3DSA:3.40.50.1000	-
329	681	InterPro	IPR023214	HAD superfamily
839	856	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
305	695	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
342	542	Gene3D	G3DSA:3.40.1110.10	-
342	542	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
857	875	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
314	688	SFLD	SFLDF00027	p-type atpase
314	688	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
90	107	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
668	693	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
668	693	InterPro	IPR001757	P-type ATPase
636	652	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
636	652	InterPro	IPR001757	P-type ATPase
608	624	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
608	624	InterPro	IPR001757	P-type ATPase
493	511	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
493	511	InterPro	IPR001757	P-type ATPase
30	891	CDD	cd02080	P-type_ATPase_cation
801	818	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
696	718	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
728	745	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
121	312	Pfam	PF00122	E1-E2 ATPase
273	277	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
91	110	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
11	898	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
11	898	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
876	894	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
819	838	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
334	340	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
334	340	InterPro	IPR018303	P-type ATPase, phosphorylation site
895	902	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
283	305	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
607	728	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
607	728	InterPro	IPR001757	P-type ATPase
90	353	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
90	353	InterPro	IPR001757	P-type ATPase
67	85	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
871	893	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
839	856	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
332	346	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
169	183	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
535	546	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
660	672	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
636	655	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
557	567	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
251	273	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
111	250	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
746	764	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
342	542	FunFam	G3DSA:3.40.1110.10:FF:000094	Cation-transporting P-type ATPase
122	229	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
122	229	InterPro	IPR008250	P-type ATPase, A domain superfamily
330	740	SUPERFAMILY	SSF56784	HAD-like
330	740	InterPro	IPR036412	HAD-like superfamily
696	721	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
314	688	SFLD	SFLDG00002	C1.7: P-type atpase like
721	893	Pfam	PF00689	Cation transporting ATPase, C-terminus
721	893	InterPro	IPR006068	Cation-transporting P-type ATPase, C-terminal
278	304	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
765	789	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	66	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
339	539	SUPERFAMILY	SSF81660	Metal cation-transporting ATPase, ATP-binding domain N
339	539	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
329	341	FunFam	G3DSA:3.40.50.1000:FF:000001	Phospholipid-transporting ATPase IC
768	790	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
30	232	Gene3D	G3DSA:2.70.150.10	-
86	90	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
62	895	Gene3D	G3DSA:1.20.1110.10	-
722	726	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
800	819	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
727	745	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
64	86	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
899	902	Coils	Coil	Coil

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA1429	AlphaFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
14				0.747
17				0.689
21				0.452
22				0.304

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.

63 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	6ZHG	Q8Y8Q5	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
CZA	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	5MPM	P11607-2	81.3 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-](F)F`
PCW	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
TG1	O14983	10.00	650.8 Da LogP 3.93 TPSA 172.0	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C([C@@H]1OC(=O)/C(=…`
CHEMBL365703	O14983	8.92	823.0 Da LogP 4.03 TPSA 255.1	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@@H]1C(=O)C(C)=C2[C@H]1[C@@](C)(…`
CHEMBL191633	O14983	8.68	708.8 Da LogP 4.80 TPSA 200.0	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@@H]1C(=O)C(C)=C2[C@H]1[C@@](C)(…`
7BL	O14983	7.77	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…`
7BS	O14983	7.72	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…`
CHEMBL191927	O14983	7.70	610.7 Da LogP 2.07 TPSA 200.0	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@@H]1C(=O)C(C)=C2[C@H]1[C@@](C)(…`
CHEMBL468766	Q93084	7.05	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	Q93084	6.68	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	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	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	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	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	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…`
ZINC3977769	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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…`
ZINC204538551	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](…`

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.