Protein profile

VK055_1980

HAD ATPase, P-type, IC family protein

Genome: KpATCC43816

Gene: AIK80586.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GJR1

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Amino acids 879

Annotations 14

Features 83

PDB binders 6

Druggability 0.994

Overview

Basic information about this protein and its source genome.

Accession: VK055_1980
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: AIK80586.1
Status: annotated
Amino acids: 879
Structure source: AlphaFold + ColabFold

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 47.727
Human E-value: 7.170000000000001e-21
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 38.453
Localization: CytoplasmicMembrane
ColabFold pLDDT: 88.09

Selected Druggability evidence

AlphaFold / UniProt model

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 0.994

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

Normalized 0.011

Sequence

Primary amino-acid sequence viewer.

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 Features

Domain/signature hits 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; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GJR1	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_1980	ColabFold	—	—	full sequence	—	Loaded

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
16				0.994
13				0.614

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	6.56	0.332
2	5.91	0.29
3	5.09	0.233
4	4.0	0.16
5	3.98	0.158

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
3				0.874

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	8.43	0.45
2	5.17	0.238
3	4.33	0.18
4	3.87	0.151
5	3.86	0.15

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

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`
BEF	6LN8	P16615	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](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
CHEMBL4514624	P16615	8.89	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	P16615	7.96	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	P16615	7.57	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	P16615	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	P16615	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…`
ZINC29084193	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	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…`
ZINC105372837	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.