Protein profile

KP13_01287

Magnesium-transporting ATPase, P-type 1

Genome: KpKP13

Gene: AHE46647.1 mgtA Structure source: AlphaFold + ColabFold UniProt A0A0H3GQU9

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Amino acids 902

Annotations 10

Features 83

PDB binders 6

Druggability 0.611

Overview

Basic information about this protein and its source genome.

Accession: KP13_01287
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE46647.1 mgtA
Status: annotated
Amino acids: 902
Structure source: AlphaFold + ColabFold

7.2.2.14

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: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: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: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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 38.889
Human E-value: 1.14e-08
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 85.0

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 0.611

Structure A0A0H3GQU9

Pocket Pocket 27

P2Rank 0.298

Structure A0A0H3GQU9

Pocket Pocket 1

ColabFold model

FPocket 0.981 · Pocket 49

P2Rank 0.48 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 275 / 4744 genomes with a hit

Normalized 0.058

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: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: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: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: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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

83 records

Show feature table

Start	End	DB	Term	Name
862	872	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
387	548	Gene3D	G3DSA:3.40.1110.10	-
387	548	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
295	313	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
370	551	SUPERFAMILY	SSF81660	Metal cation-transporting ATPase, ATP-binding domain N
370	551	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
117	121	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
93	116	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
873	895	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
372	680	Gene3D	G3DSA:3.40.50.1000	-
372	680	InterPro	IPR023214	HAD superfamily
730	751	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
726	892	Pfam	PF00689	Cation transporting ATPase, C-terminus
726	892	InterPro	IPR006068	Cation-transporting P-type ATPase, C-terminal
371	657	Pfam	PF00702	haloacid dehalogenase-like hydrolase
725	729	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
357	695	SFLD	SFLDG00002	C1.7: P-type atpase like
159	262	FunFam	G3DSA:2.70.150.10:FF:000045	Magnesium-translocating P-type ATPase
873	895	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
896	902	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
536	687	SUPERFAMILY	SSF56784	HAD-like
536	687	InterPro	IPR036412	HAD-like superfamily
773	795	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
172	274	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
172	274	InterPro	IPR008250	P-type ATPase, A domain superfamily
122	141	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
751	764	PRINTS	PR01836	Magnesium-transporting ATPase signature
751	764	InterPro	IPR006415	P-type ATPase, subfamily IIIB
806	827	PRINTS	PR01836	Magnesium-transporting ATPase signature
806	827	InterPro	IPR006415	P-type ATPase, subfamily IIIB
856	877	PRINTS	PR01836	Magnesium-transporting ATPase signature
856	877	InterPro	IPR006415	P-type ATPase, subfamily IIIB
305	324	PRINTS	PR01836	Magnesium-transporting ATPase signature
305	324	InterPro	IPR006415	P-type ATPase, subfamily IIIB
771	787	PRINTS	PR01836	Magnesium-transporting ATPase signature
771	787	InterPro	IPR006415	P-type ATPase, subfamily IIIB
288	304	PRINTS	PR01836	Magnesium-transporting ATPase signature
288	304	InterPro	IPR006415	P-type ATPase, subfamily IIIB
701	716	PRINTS	PR01836	Magnesium-transporting ATPase signature
701	716	InterPro	IPR006415	P-type ATPase, subfamily IIIB
409	422	PRINTS	PR01836	Magnesium-transporting ATPase signature
409	422	InterPro	IPR006415	P-type ATPase, subfamily IIIB
719	730	PRINTS	PR01836	Magnesium-transporting ATPase signature
719	730	InterPro	IPR006415	P-type ATPase, subfamily IIIB
752	771	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
357	695	SFLD	SFLDF00027	p-type atpase
357	695	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
142	294	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
48	121	SMART	SM00831	Cation_ATPase_N_a_2
48	121	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
796	806	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
295	314	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
61	894	PANTHER	PTHR42861	CALCIUM-TRANSPORTING ATPASE
1	92	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
324	346	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
122	141	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
51	116	Pfam	PF00690	Cation transporter/ATPase, N-terminus
51	116	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
49	900	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
49	900	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
837	861	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
347	701	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
163	355	Pfam	PF00122	E1-E2 ATPase
314	318	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
702	724	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
124	855	Gene3D	G3DSA:1.20.1110.10	-
39	902	NCBIfam	TIGR01524	magnesium-translocating P-type ATPase
39	902	InterPro	IPR006415	P-type ATPase, subfamily IIIB
67	832	CDD	cd02077	P-type_ATPase_Mg
67	832	InterPro	IPR006415	P-type ATPase, subfamily IIIB
714	736	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
127	408	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
127	408	InterPro	IPR001757	P-type ATPase
610	732	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
610	732	InterPro	IPR001757	P-type ATPase
772	795	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
319	346	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.
807	825	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
159	262	Gene3D	G3DSA:2.70.150.10	-
377	383	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
377	383	InterPro	IPR018303	P-type ATPase, phosphorylation site
836	858	TMHMM	TMhelix	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.

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_A0A0H3GQU9	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01287	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
68				0.249
1				0.069
66				0.012
70				0.001

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	6.9	0.298
2	5.71	0.229
3	5.66	0.226
4	5.61	0.224
5	5.15	0.196

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
49				0.981
62				0.667

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	7.51	0.395
2	5.84	0.286
3	5.42	0.257
4	4.64	0.202
5	4.46	0.189

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.

65 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	4XE5	Q08DA1	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	4XE5	Q08DA1	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
CHEMBL254219	P50997	8.10	765.0 Da LogP 3.25 TPSA 182.8	2 viol.	✓ Clean	`C[C@H]1O[C@@H](O[C@H]2[C@@H](O)C[C@H](O[C@H]3[C…`
CHEMBL2069115	P50997	8.08	509.6 Da LogP 2.76 TPSA 142.5	1 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2CC[C@@]3(C)[C@H](CC[C@@H…`
CHEMBL2069118	P50997	7.89	508.7 Da LogP 2.61 TPSA 136.7	1 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2CC[C@@]3(C)[C@H](CC[C@@H…`
CHEMBL2069066	P50997	7.52	541.7 Da LogP 2.26 TPSA 151.8	1 viol.	✓ Clean	`COC(C[N+](=O)[O-])[C@H]1CC[C@]2(O)[C@@H]3CC[C@@…`
CHEMBL2069075	P50997	7.34	511.7 Da LogP 2.64 TPSA 142.5	1 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2CC[C@@]3(C)[C@H](CC[C@@H…`
CHEMBL2069070	P50997	6.64	510.7 Da LogP 2.84 TPSA 136.7	1 viol.	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2CC[C@@]3(C)[C@H](CC[C@@H…`
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…`
CHEMBL1453	P50997	6.30	374.5 Da LogP 3.60 TPSA 66.8	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@H]1CC[C@@H]1[C@@H]2CC[C@]2…`
CHEMBL2069067	P50997	6.18	482.7 Da LogP 2.36 TPSA 119.6	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](O[C@H]2CC[C@@]3(C)[C@H](CC[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…`
ZINC253475945	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)[…`
ZINC3814414	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…`
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…`
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.