Protein profile

PA3920

metal transporting P-type ATPase

Genome: NC_002516.2

Gene: PA3920 Structure source: AlphaFold UniProt Q9HX93

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Amino acids 792

Annotations 14

Features 92

PDB binders 6

Druggability 0.762

Overview

Basic information about this protein and its source genome.

Accession: PA3920
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3920
Status: annotated
Amino acids: 792
Structure source: AlphaFold

7.2.2.9

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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. 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:0005507 Binding to a copper (Cu) ion.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 40.603
Human E-value: 5.91e-110
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.762

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MNSATLTELDLPVSGMTCASCAGRVERALKKVPGVAAASVNLASEQARVQAPADSLPALVAAVEQAGYQVPARSLELSIEGMTCASCVGRVERALKKVPGVREVSVNLASERAHLELLGAVDSQALLQAVEQAGYKARLLDAGQPRQDDAERRLRRERWWVIAALLLALPLVLPMLVEWAGLHWMLPPWAQFLLATPVQFVIGARFYVSAWRAVKAGAGNMDLLVALGTSAGYGLSVYLWLTAPPGHMPHLYFEASTVVIALILLGKYLESRAKRQTASAIRALEALRPERAVRLRDGREEEVAIAELRLGDEVVVRPGERFPVDGEVLDGSSHADEALITGESLPVPKAPGDKVTGGAINGEGRLLLRTTALGGETVLAKIIRLVEDAQAAKAPIQKLVDKVSQVFVPVVILIALVTLGAWLVAGVGLEQALVNAVAVLVIACPCALGLATPTAIMAGTGVAARHGILIKDAESLEVAHAVTSVAFDKTGTLTSGRPQIIHLGGDDQEQLLRLAGALQRGSEHPLAKAVLERCAERDLEVPPVNASQALSGRGIQGEVEGRRLALGNRRLLDEQELKPGALASAAADWEAEGRTLSWLLELAPEKRVLGLFAFGDSLKDGAAEAVEALRGRDIHSHLITGDNRGSAAVVAKALGIDDVHAEVLPADKAATVAELKGRGRVVAMVGDGINDAPALAAADVGIAMGGGTDVAMHAAGITLMRGDPRLVPAALDISRRTYAKIRQNLFWAFIYNVIGIPLAAFGLLNPMVAGAAMAFSSVSVVGNALLLRRWKP

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Enzyme Commission (EC)

7.2.2.9

Gene Ontology (GO)

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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
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: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:0055070 Any process involved in the maintenance of an internal steady state of copper ions within an organism or cell.
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:0046872 Binding to a metal ion.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

92 records

Show feature table

Start	End	DB	Term	Name
426	430	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
486	500	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
708	720	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
685	704	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
336	350	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
632	642	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
685	707	ProSitePatterns	PS01229	Hypothetical cof family signature 2.
73	138	ProSiteProfiles	PS50846	Heavy-metal-associated domain profile.
73	138	InterPro	IPR006121	Heavy metal-associated domain, HMA
159	177	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
5	72	FunFam	G3DSA:3.30.70.100:FF:000005	Copper-exporting P-type ATPase A
257	762	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
257	762	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
452	744	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
178	188	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
76	138	CDD	cd00371	HMA
76	138	InterPro	IPR006121	Heavy metal-associated domain, HMA
6	71	SUPERFAMILY	SSF55008	HMA, heavy metal-associated domain
6	71	InterPro	IPR036163	Heavy metal-associated domain superfamily
274	390	FunFam	G3DSA:2.70.150.10:FF:000002	Copper-transporting ATPase 1, putative
407	429	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
12	69	Pfam	PF00403	Heavy-metal-associated domain
12	69	InterPro	IPR006121	Heavy metal-associated domain, HMA
77	136	Pfam	PF00403	Heavy-metal-associated domain
77	136	InterPro	IPR006121	Heavy metal-associated domain, HMA
75	145	SUPERFAMILY	SSF55008	HMA, heavy metal-associated domain
75	145	InterPro	IPR036163	Heavy metal-associated domain superfamily
788	792	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
6	791	PANTHER	PTHR43520	ATP7, ISOFORM B
7	71	ProSiteProfiles	PS50846	Heavy-metal-associated domain profile.
7	71	InterPro	IPR006121	Heavy metal-associated domain, HMA
223	242	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
468	737	SFLD	SFLDF00027	p-type atpase
468	737	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
179	789	CDD	cd02094	P-type_ATPase_Cu-like
439	461	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
765	769	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
79	108	ProSitePatterns	PS01047	Heavy-metal-associated domain.
79	108	InterPro	IPR017969	Heavy-metal-associated, conserved site
289	386	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
289	386	InterPro	IPR008250	P-type ATPase, A domain superfamily
13	42	ProSitePatterns	PS01047	Heavy-metal-associated domain.
13	42	InterPro	IPR017969	Heavy-metal-associated, conserved site
10	70	CDD	cd00371	HMA
10	70	InterPro	IPR006121	Heavy metal-associated domain, HMA
488	494	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
488	494	InterPro	IPR018303	P-type ATPase, phosphorylation site
1	158	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
240	250	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
75	142	Gene3D	G3DSA:3.30.70.100	-
484	699	Pfam	PF00702	haloacid dehalogenase-like hydrolase
252	269	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
220	239	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
7	73	Gene3D	G3DSA:3.30.70.100	-
270	405	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
192	211	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
73	140	FunFam	G3DSA:3.30.70.100:FF:000005	Copper-exporting P-type ATPase A
221	787	NCBIfam	TIGR01525	heavy metal translocating P-type ATPase
221	787	InterPro	IPR027256	P-type ATPase, subfamily IB
259	765	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
259	765	InterPro	IPR001757	P-type ATPase
251	269	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
160	182	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
431	451	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
274	390	Gene3D	G3DSA:2.70.150.10	-
469	484	PRINTS	PR00943	Copper-transporting ATPase signature
276	294	PRINTS	PR00943	Copper-transporting ATPase signature
409	423	PRINTS	PR00943	Copper-transporting ATPase signature
206	225	PRINTS	PR00943	Copper-transporting ATPase signature
662	679	PRINTS	PR00943	Copper-transporting ATPase signature
89	103	PRINTS	PR00943	Copper-transporting ATPase signature
256	275	PRINTS	PR00943	Copper-transporting ATPase signature
189	208	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
499	616	Gene3D	G3DSA:3.40.1110.10	-
499	616	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
202	788	NCBIfam	TIGR01511	copper-translocating P-type ATPase
76	137	NCBIfam	TIGR00003	copper ion binding protein
76	137	InterPro	IPR006122	Heavy metal-associated domain, copper ion-binding
10	70	NCBIfam	TIGR00003	copper ion binding protein
10	70	InterPro	IPR006122	Heavy metal-associated domain, copper ion-binding
485	785	SUPERFAMILY	SSF56784	HAD-like
485	785	InterPro	IPR036412	HAD-like superfamily
745	764	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
770	787	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
745	764	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
453	742	Gene3D	G3DSA:3.40.50.1000	-
453	742	InterPro	IPR023214	HAD superfamily
768	787	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
468	737	SFLD	SFLDS00003	Haloacid Dehalogenase
287	466	Pfam	PF00122	E1-E2 ATPase
209	219	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
406	425	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.

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

0 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA3920	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
3				0.762
4				0.248
20				0.231

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

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
9UX	6A71	P35670	292.0 Da LogP -0.02 TPSA 34.1	✓ Ro5	✓ Clean	`O=[MoH2]1S[MoH2](=O)S1`
ACP	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	4UMW	Q3YW59	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
BEF	4UMV	Q3YW59	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
MGF	4BEV	Q5ZWR1	81.3 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-](F)F`
NH4	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	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…`
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(=…`
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…`
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…`
ZINC17107643	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	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	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	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	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	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	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	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	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	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	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	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.