Protein profile

VK055_3334

ATP synthase F1, alpha subunit

Genome: KpATCC43816

Gene: atpA AIK81891.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GZ37

Export view

Amino acids 513

Annotations 11

Features 33

PDB binders 11

Druggability 0.735

Overview

Basic information about this protein and its source genome.

Accession: VK055_3334
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: atpA AIK81891.1
Status: annotated
Amino acids: 513
Structure source: AlphaFold + ColabFold

7.1.2.2

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0015986 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a membrane to generate an electrochemical gradient (proton-motive force). GO:0045261 OBSOLETE. The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled. GO:0046034 The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator. GO:0046933 Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + phosphate + 5 H+(out) => ATP + H2O + 4 H+(in). GO:0032559 Binding to an adenyl ribonucleotide, any compound consisting of adenosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 56.579
Human E-value: 5.549999999999999e-48
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 98.246
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 93.88

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 0.735

Structure A0A0H3GZ37

Pocket Pocket 3

P2Rank 0.466

Structure A0A0H3GZ37

Pocket Pocket 1

ColabFold model

FPocket 0.658 · Pocket 10

P2Rank 0.386 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3157 / 4744 genomes with a hit

Normalized 0.665

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

7.1.2.2

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0015986 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a membrane to generate an electrochemical gradient (proton-motive force).
GO:0045261 OBSOLETE. The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.
GO:0046034 The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator.
GO:0046933 Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + phosphate + 5 H+(out) => ATP + H2O + 4 H+(in).
GO:0032559 Binding to an adenyl ribonucleotide, any compound consisting of adenosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.
GO:1902600 The directed movement of a proton across a membrane.
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:0045259 A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient.
GO:0043531 Binding to ADP, adenosine 5'-diphosphate.

Sequence Features

Domain/signature hits from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
27	93	CDD	cd18116	ATP-synt_F1_alpha_N
3	510	PANTHER	PTHR48082	ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
3	510	InterPro	IPR005294	ATP synthase, F1 complex, alpha subunit
386	510	CDD	cd18113	ATP-synt_F1_alpha_C
386	510	InterPro	IPR000793	ATP synthase, alpha subunit, C-terminal
382	507	Pfam	PF00306	ATP synthase alpha/beta chain, C terminal domain
382	507	InterPro	IPR000793	ATP synthase, alpha subunit, C-terminal
10	94	SUPERFAMILY	SSF50615	N-terminal domain of alpha and beta subunits of F1 ATP synthase
10	94	InterPro	IPR036121	ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily
1	512	Hamap	MF_01346	ATP synthase subunit alpha [atpA].
1	512	InterPro	IPR005294	ATP synthase, F1 complex, alpha subunit
94	378	CDD	cd01132	F1-ATPase_alpha_CD
94	378	InterPro	IPR033732	ATP synthase, F1 complex, alpha subunit nucleotide-binding domain
383	511	SUPERFAMILY	SSF47917	C-terminal domain of alpha and beta subunits of F1 ATP synthase
383	513	FunFam	G3DSA:1.20.150.20:FF:000001	ATP synthase subunit alpha
149	375	Pfam	PF00006	ATP synthase alpha/beta family, nucleotide-binding domain
149	375	InterPro	IPR000194	ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
383	513	Gene3D	G3DSA:1.20.150.20	-
383	513	InterPro	IPR038376	ATP synthase, alpha subunit, C-terminal domain superfamily
1	93	Gene3D	G3DSA:2.40.30.20	-
1	93	InterPro	IPR023366	ATP synthase subunit alpha, N-terminal domain-like superfamily
94	382	FunFam	G3DSA:3.40.50.300:FF:000002	ATP synthase subunit alpha
94	382	Gene3D	G3DSA:3.40.50.300	-
94	382	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
2	512	NCBIfam	TIGR00962	F0F1 ATP synthase subunit alpha
2	512	InterPro	IPR005294	ATP synthase, F1 complex, alpha subunit
96	381	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
96	381	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
29	92	Pfam	PF02874	ATP synthase alpha/beta family, beta-barrel domain
29	92	InterPro	IPR004100	ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain
366	375	ProSitePatterns	PS00152	ATP synthase alpha and beta subunits signature.
366	375	InterPro	IPR020003	ATPase, alpha/beta subunit, nucleotide-binding domain, active site
1	93	FunFam	G3DSA:2.40.30.20:FF:000001	ATP synthase subunit alpha

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...

Legend High Medium Low

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_A0A0H3GZ37	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_3334	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
3				0.735

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	3.92	0.154
2	3.62	0.135
3	2.32	0.06
4	2.18	0.052
5	1.1	0.008

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
10				0.658
1				0.341

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	4.89	0.22
2	3.77	0.145
3	2.46	0.067
4	2.16	0.051
5	1.67	0.028

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.

62 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
AF3	1E1R	P19483	84.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al](F)F`
ALF	1H8E	P19483	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
ANP	3OAA	P0ABB0	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
AUR	1COW	P19483	460.5 Da LogP 3.10 TPSA 104.4	✓ Ro5	✓ Clean	`CC[C@@H]1[C@]2([C@H]([C@@](O1)([C@H]([C@@H](O2)…`
AZI	2CK3	P19483	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BEF	1W0J	P19483	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
QUE	2JJ2	P19483	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	Alert	`c1cc(c(cc1C2=C(C(=O)c3c(cc(cc3O2)O)O)O)O)O`
STL	2JIZ	P19483	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`c1cc(ccc1\C=C\c2cc(cc(c2)O)O)O`
TS6	4YXW	P19483	114.1 Da LogP 0.01 TPSA 57.5	✓ Ro5	✓ Clean	`OP(=O)(O)S`
TTX	1KMH	P06450	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`C[C@H]1C(=O)N[C@H](C(=O)N(/C(=C\c2ccccc2)/C(=O)…`
VO4	2F43	P15999	114.9 Da LogP -3.69 TPSA 86.2	✓ Ro5	✓ Clean	`[O-][V](=O)([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
CHEMBL2063416	P25705	—	716.8 Da LogP 1.65 TPSA 238.1	3 viol.	Alert	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]21)NCCOCCO…`

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
ZINC100230999	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@H](C)N(C)C(=O)CNC(=O)/C(=…`
ZINC12353732	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2cc(O)cc(O)c2)cc1`
ZINC1531101	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@H]1NC(=O)[C@@H](C)N(C)C(=O)CNC(=O)C(=C…`
ZINC1857524289	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2cc(O)cc(O)c2)cc1`
ZINC2356469567	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@@H](C)N(C)C(=O)CNC(=O)C(=…`
ZINC33955459	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@H](C)N(C)C(=O)CNC(=O)/C(=…`
ZINC3875061	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@H]1NC(=O)[C@H](C)N(C)C(=O)CNC(=O)C(=Cc…`
ZINC4097591	1.000	414.5 Da LogP 0.99 TPSA 98.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H]1NC(=O)[C@H](C)N(C)C(=O)CNC(=O)C(=C…`
ZINC6787	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2cc(O)cc(O)c2)cc1`
ZINC12360002	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	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	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.810	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	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.810	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	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC3874317	0.757	318.2 Da LogP 1.69 TPSA 151.6	1 viol.	Alert	`O=c1c(O)c(-c2cc(O)c(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC13518964	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.741	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	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.741	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	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.741	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	0.741	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	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC13319959	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2ccc(O)cc2)cc1`
ZINC1510311	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2ccc(O)cc2)cc1`
ZINC1875408805	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2ccc(O)cc2)cc1`
ZINC4096224	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.726	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	0.726	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	0.726	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	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC34544488	0.720	230.2 Da LogP 3.41 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2cc(O)cc(F)c2)cc1`
ZINC120273	0.718	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)cc(O)c12`
ZINC105372833	0.712	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	0.712	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	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC49588452	0.708	246.7 Da LogP 3.92 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C/c2ccc(Cl)cc2)c1`
ZINC71622042	0.708	246.7 Da LogP 3.92 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C\c2ccc(Cl)cc2)c1`

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.