Protein profile

PA4825

Mg(2+) transport ATPase

Genome: NC_002516.2

Gene: mgtA PA4825 Structure source: AlphaFold UniProt Q9HUY5

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Amino acids 903

Annotations 10

Features 84

PDB binders 6

Druggability 0.651

Overview

Basic information about this protein and its source genome.

Accession: PA4825
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: mgtA PA4825
Status: annotated
Amino acids: 903
Structure source: AlphaFold

7.2.2.14

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: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:0015444 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Mg2+(out) = ADP + phosphate + Mg2+(in). GO:0015693 The directed movement of magnesium (Mg) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 37.037
Human E-value: 2.85e-07
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 0.651

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

7.2.2.14

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: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:0015444 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Mg2+(out) = ADP + phosphate + Mg2+(in).
GO:0015693 The directed movement of magnesium (Mg) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
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.

84 records

Show feature table

Start	End	DB	Term	Name
35	813	PANTHER	PTHR42861	CALCIUM-TRANSPORTING ATPASE
148	261	Gene3D	G3DSA:2.70.150.10	-
1	82	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
896	903	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
345	701	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
147	353	Pfam	PF00122	E1-E2 ATPase
355	694	SFLD	SFLDS00003	Haloacid Dehalogenase
702	724	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
17	902	NCBIfam	TIGR01524	magnesium-translocating P-type ATPase
17	902	InterPro	IPR006415	P-type ATPase, subfamily IIIB
290	308	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
375	381	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
375	381	InterPro	IPR018303	P-type ATPase, phosphorylation site
1	27	MobiDBLite	mobidb-lite	consensus disorder prediction
102	112	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
111	130	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
161	273	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
161	273	InterPro	IPR008250	P-type ATPase, A domain superfamily
113	130	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
752	771	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
874	896	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
796	806	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
858	872	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
83	101	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
131	289	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
832	854	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
837	857	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
873	895	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
730	751	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
710	732	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
368	551	SUPERFAMILY	SSF81660	Metal cation-transporting ATPase, ATP-binding domain N
368	551	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
385	548	Gene3D	G3DSA:3.40.1110.10	-
385	548	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
774	796	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
726	893	Pfam	PF00689	Cation transporting ATPase, C-terminus
726	893	InterPro	IPR006068	Cation-transporting P-type ATPase, C-terminal
45	832	CDD	cd02077	P-type_ATPase_Mg
45	832	InterPro	IPR006415	P-type ATPase, subfamily IIIB
771	787	PRINTS	PR01836	Magnesium-transporting ATPase signature
771	787	InterPro	IPR006415	P-type ATPase, subfamily IIIB
286	302	PRINTS	PR01836	Magnesium-transporting ATPase signature
286	302	InterPro	IPR006415	P-type ATPase, subfamily IIIB
719	730	PRINTS	PR01836	Magnesium-transporting ATPase signature
719	730	InterPro	IPR006415	P-type ATPase, subfamily IIIB
407	420	PRINTS	PR01836	Magnesium-transporting ATPase signature
407	420	InterPro	IPR006415	P-type ATPase, subfamily IIIB
303	322	PRINTS	PR01836	Magnesium-transporting ATPase signature
303	322	InterPro	IPR006415	P-type ATPase, subfamily IIIB
856	877	PRINTS	PR01836	Magnesium-transporting ATPase signature
856	877	InterPro	IPR006415	P-type ATPase, subfamily IIIB
701	716	PRINTS	PR01836	Magnesium-transporting ATPase signature
701	716	InterPro	IPR006415	P-type ATPase, subfamily IIIB
806	827	PRINTS	PR01836	Magnesium-transporting ATPase signature
806	827	InterPro	IPR006415	P-type ATPase, subfamily IIIB
751	764	PRINTS	PR01836	Magnesium-transporting ATPase signature
751	764	InterPro	IPR006415	P-type ATPase, subfamily IIIB
290	312	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
79	101	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
355	694	SFLD	SFLDF00027	p-type atpase
355	694	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
322	344	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
267	392	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
267	392	InterPro	IPR001757	P-type ATPase
609	732	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
609	732	InterPro	IPR001757	P-type ATPase
26	99	SMART	SM00831	Cation_ATPase_N_a_2
26	99	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
320	344	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
371	742	SUPERFAMILY	SSF56784	HAD-like
371	742	InterPro	IPR036412	HAD-like superfamily
725	729	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
113	854	Gene3D	G3DSA:1.20.1110.10	-
369	657	Pfam	PF00702	haloacid dehalogenase-like hydrolase
309	319	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
42	900	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
42	900	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
772	795	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
370	680	Gene3D	G3DSA:3.40.50.1000	-
370	680	InterPro	IPR023214	HAD superfamily
807	825	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
826	836	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
29	94	Pfam	PF00690	Cation transporter/ATPase, N-terminus
29	94	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal

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 PA4825	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
6				0.651
19				0.347
1				0.284

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.

58 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
ALF	3WGV	P05024	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
CLR	3KDP	P05024	386.7 Da LogP 7.39 TPSA 20.2	1 viol.	✓ Clean	`CC(C)CCC[C@@H](C)[C@H]1CC[C@@H]2[C@@]1(CC[C@H]3…`
EFO	3WGV	P05024	791.1 Da LogP 5.88 TPSA 180.0	3 viol.	✓ Clean	`CC[C@@H]\1CC[C@H]2[C@H]([C@H]([C@@H]([C@]3(O2)C…`
MF4	3B8E	P05024	100.3 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-2](F)(F)F`
OBN	3N23	P05024	584.7 Da LogP -1.51 TPSA 206.6	3 viol.	✓ Clean	`C[C@H]1[C@@H]([C@H]([C@H]([C@@H](O1)O[C@H]2C[C@…`
PC1	3WGV	P05024	790.2 Da LogP 12.17 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=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
CHEMBL1751	P05023	6.54	780.9 Da LogP 2.22 TPSA 203.1	3 viol.	✓ Clean	`C[C@H]1O[C@@H](O[C@H]2[C@@H](O)C[C@H](O[C@H]3[C…`
CHEMBL4081196	Q64541	—	513.6 Da LogP 0.96 TPSA 152.1	2 viol.	✓ Clean	`C[C@]12C[C@@H](O)[C@H]3[C@@H](CC[C@]4(O)C[C@@H]…`

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
ZINC13544781	0.780	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	0.780	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)…`
ZINC13543439	0.760	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	0.760	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…`
ZINC238809171	0.724	780.9 Da LogP 2.22 TPSA 203.1	3 viol.	✓ Clean	`C[C@H]1O[C@@H](O[C@H]2[C@@H](O)C[C@H](O[C@H]3[C…`
ZINC248380422	0.717	318.5 Da LogP 4.31 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@@H]2[C@H]3CC=C4C[C@@H](O)C…`
ZINC253611286	0.717	318.5 Da LogP 4.31 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@@H]2[C@H]3CC=C4C[C@@H](O)…`
ZINC253611289	0.717	318.5 Da LogP 4.31 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@@H]2[C@H]3CC=C4C[C@@H](O)C…`
ZINC2563573	0.717	318.5 Da LogP 4.31 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H](O)C…`
ZINC2564677	0.717	318.5 Da LogP 4.31 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H](O)…`
ZINC36323242	0.717	318.5 Da LogP 4.31 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@@H]2[C@H]3CC=C4C[C@@H](O)…`
ZINC6030248	0.717	318.5 Da LogP 4.31 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H](O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H](O)CC…`
ZINC6037028	0.717	318.5 Da LogP 4.31 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H](O)C…`
ZINC33822387	0.706	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	0.706	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)…`
ZINC13475048	0.703	438.5 Da LogP -0.37 TPSA 147.7	1 viol.	✓ Clean	`C[C@]12C[C@@H](O)[C@H]3[C@@H](CC[C@]4(O)C[C@@H]…`
ZINC136721343	0.703	438.5 Da LogP -0.37 TPSA 147.7	1 viol.	✓ Clean	`C[C@]12C[C@H](O)[C@H]3[C@@H](CC[C@@]4(O)C[C@@H]…`
ZINC256072887	0.703	438.5 Da LogP -0.37 TPSA 147.7	1 viol.	✓ Clean	`C[C@@]12C[C@@H](O)[C@@H]3[C@H](CC[C@@]4(O)C[C@@…`
ZINC256072890	0.703	438.5 Da LogP -0.37 TPSA 147.7	1 viol.	✓ Clean	`C[C@@]12C[C@H](O)[C@@H]3[C@H](CC[C@@]4(O)C[C@@H…`
ZINC256072893	0.703	438.5 Da LogP -0.37 TPSA 147.7	1 viol.	✓ Clean	`C[C@]12C[C@@H](O)[C@@H]3[C@H](CC[C@@]4(O)C[C@@H…`
ZINC256072896	0.703	438.5 Da LogP -0.37 TPSA 147.7	1 viol.	✓ Clean	`C[C@]12C[C@H](O)[C@@H]3[C@H](CC[C@@]4(O)C[C@@H]…`
ZINC118926312	0.679	334.5 Da LogP 3.28 TPSA 60.7	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC118926317	0.679	334.5 Da LogP 3.28 TPSA 60.7	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC118931103	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@H](…`
ZINC118931104	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@H]…`
ZINC1772491619	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@@H]1CC[C@@H]2[C@@H]3CC=C4C[C@@…`
ZINC1772491620	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@@H]1CC[C@@H]2[C@@H]3CC=C4C[C@@…`
ZINC2097326	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@@H]1CC[C@@H]2[C@@H]3CC=C4C[C@H…`
ZINC2097329	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@@H]1CC[C@@H]2[C@@H]3CC=C4C[C@H…`
ZINC2382312726	0.679	334.5 Da LogP 3.28 TPSA 60.7	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC2382312727	0.679	334.5 Da LogP 3.28 TPSA 60.7	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC253595413	0.679	334.5 Da LogP 3.28 TPSA 60.7	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC253595414	0.679	334.5 Da LogP 3.28 TPSA 60.7	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)CC1=CC[C@H]1[C@H]2CC[C@@]2(C)[…`
ZINC253595415	0.679	334.5 Da LogP 3.28 TPSA 60.7	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC253595416	0.679	334.5 Da LogP 3.28 TPSA 60.7	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)CC1=CC[C@H]1[C@H]2CC[C@@]2(C)[…`
ZINC4024647	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H]…`
ZINC4024648	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@H]1CC[C@@H]2[C@@H]3CC=C4C[C@@H…`
ZINC4024650	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H]…`
ZINC4024651	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@H]1CC[C@@H]2[C@@H]3CC=C4C[C@@H…`
ZINC4921433	0.679	346.5 Da LogP 4.65 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H…`
ZINC1857524366	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC253475946	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC253527899	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)CC1=CC[C@H]1[C@H]2CC[C@@]2(C)[…`
ZINC253527901	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)CC1=CC[C@H]1[C@H]2CC[C@@]2(C)[…`
ZINC4026334	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43…`
ZINC4026335	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43…`
ZINC4026336	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC6067929	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@@H](O)CC[C@@]43C…`
ZINC6472608	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@H](O)CC[C@@]43C)…`
ZINC6472629	0.654	290.4 Da LogP 3.67 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC=C4C[C@H](O)CC[C@@]43C)…`

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.