Protein profile

PA2967

3-oxoacyl-[acyl-carrier-protein] reductase FabG

Genome: NC_002516.2

Gene: fabG PA2967 Structure source: Experimental + AlphaFold UniProt O54438

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Amino acids 247

Annotations 8

Features 28

PDB binders 19

Druggability 0.811

Overview

Basic information about this protein and its source genome.

Accession: PA2967
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: fabG PA2967
Status: annotated
Amino acids: 247
Structure source: Experimental + AlphaFold

1.1.1.100

GO:0004316 Catalysis of the reaction: (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = 3-oxoacyl-[acyl-carrier protein] + NADPH + H+. GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP. GO:0030497 The elongation of a fatty acid chain by the sequential addition of two-carbon units. GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 43.662
Human E-value: 5.11e-08
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

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 0.811

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1.1.1.100

Gene Ontology (GO)

GO:0004316 Catalysis of the reaction: (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = 3-oxoacyl-[acyl-carrier protein] + NADPH + H+.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0030497 The elongation of a fatty acid chain by the sequential addition of two-carbon units.
GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
12	244	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
208	228	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
208	228	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
81	92	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
81	92	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
128	144	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
128	144	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
7	24	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
7	24	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
175	192	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
175	192	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
154	173	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
154	173	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
6	185	SMART	SM00822	This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
1	247	Gene3D	G3DSA:3.40.50.720	-
141	169	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
141	169	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
8	245	NCBIfam	TIGR01830	3-oxoacyl-[acyl-carrier-protein] reductase
8	245	InterPro	IPR011284	3-oxoacyl-(acyl-carrier-protein) reductase
6	245	CDD	cd05333	BKR_SDR_c
1	245	PANTHER	PTHR42879	3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE
1	247	FunFam	G3DSA:3.40.50.720:FF:000037	3-oxoacyl-[acyl-carrier-protein] reductase FabG
134	142	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
134	142	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
154	173	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
81	92	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
4	246	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
4	246	InterPro	IPR036291	NAD(P)-binding domain superfamily

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

19 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 4BNW	X-ray	1.60 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Viewing
PDB 4AG3	X-ray	1.80 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BNY	X-ray	1.80 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO2	X-ray	1.90 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BNU	X-ray	2.00 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO1	X-ray	2.20 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4AFN	X-ray	2.30 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BNT	X-ray	2.30 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BNX	X-ray	2.30 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO0	X-ray	2.40 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BNV	X-ray	2.50 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BNZ	X-ray	2.50 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO3	X-ray	2.50 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO5	X-ray	2.60 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO7	X-ray	2.60 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO4	X-ray	2.70 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO8	X-ray	2.70 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO6	X-ray	2.80 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
PDB 4BO9	X-ray	2.90 Å	A,B,C,D	100.0% 1-247	PDBe RCSB PDBj File	Loaded
AlphaFold PA2967	AlphaFold	—	—	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
1				0.811
2				0.759

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	9.39	0.504
2	4.95	0.224
3	4.0	0.16
4	1.31	0.014

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
7				0.344
1				0.311

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.

74 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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
34X	4BO8 2.70 Å Open crystal	311.3 Da LogP 3.05 TPSA 85.0	✓ Ro5	✓ Clean	`c1ccc(cc1)c2cn(c(n2)N)NC(=O)Nc3ccccc3F`
36E	4BNT 2.30 Å Open crystal	186.1 Da LogP 2.58 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]c(n2)C(F)(F)F`
36G	4BO4 2.70 Å Open crystal	282.3 Da LogP 3.68 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N2CCCc3c2cccc3`
36I	4BNY 1.80 Å Open crystal	297.4 Da LogP 3.19 TPSA 38.2	✓ Ro5	✓ Clean	`c1ccc(cc1)c2nc3ccsc3c(n2)N4CCOCC4`
36K	4BO2 1.90 Å Open crystal	310.4 Da LogP 3.71 TPSA 68.2	✓ Ro5	✓ Clean	`CCn1c2ccccc2nc1NC(=O)Nc3ccccc3OC`
36P	4BO6 2.80 Å Open crystal	312.4 Da LogP 4.07 TPSA 33.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)CCN2C(=O)c3csc(n3)c4ccsc4`
3X3	4BO9 2.90 Å Open crystal	318.3 Da LogP 3.50 TPSA 66.0	✓ Ro5	✓ Clean	`c1ccc(cc1)n2nc(nn2)c3ccccc3OCc4ccco4`
8M5	4BNZ 2.50 Å Open crystal	250.3 Da LogP 3.43 TPSA 34.0	✓ Ro5	✓ Clean	`Cn1cc(c2c1cccc2)C(=O)Nc3ccccc3`
9KQ	4BNU 2.00 Å Open crystal	273.3 Da LogP 2.88 TPSA 56.5	✓ Ro5	✓ Clean	`c1ccc(cc1)c2nc3ccccc3c(n2)n4cnnc4`
FXE	4BO0 2.40 Å Open crystal	326.4 Da LogP 3.23 TPSA 77.4	✓ Ro5	✓ Clean	`Cn1c2cccc(c2c(n1)NC(=O)Nc3ccccc3OC)OC`
J2T	4BO7 2.60 Å Open crystal	252.3 Da LogP 1.75 TPSA 68.0	✓ Ro5	✓ Clean	`c1cc2c(cc1Nc3ccc4nnnn4n3)CCC2`
NKH	4BO1 2.20 Å Open crystal	342.8 Da LogP 4.16 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(c(cc1Cl)OC)NC(=O)c2cccc3c2nccc3`
O74	4BNX 2.30 Å Open crystal	347.8 Da LogP 4.53 TPSA 53.5	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=N/C(=C/3\C=CC=CC3=O)/N2)Nc4ccccc4…`
Q7U	4BNV 2.50 Å Open crystal	300.7 Da LogP 3.87 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c2ccccc2nc1NC(=O)Nc3ccccc3Cl`
U98	4BO3 2.50 Å Open crystal	317.3 Da LogP 2.49 TPSA 85.1	✓ Ro5	✓ Clean	`c1cc(cc(c1)Nc2c(cccn2)S(=O)(=O)N)C(F)(F)F`
WI4	4BO5 2.60 Å Open crystal	271.7 Da LogP 3.06 TPSA 55.6	✓ Ro5	✓ Clean	`c1ccc(c(c1)Nc2ncnc(n2)n3cccc3)Cl`

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
CAA	3VZS	P14697	851.6 Da LogP -1.36 TPSA 380.7	3 viol.	✓ Clean	`CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
MLH	6T65	V5VHN7	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c2cc(c(cc2n(c1CN(C)C)c3ccccc3)Br)O`
P4C	3EZL	Q3JRS9	324.4 Da LogP -0.72 TPSA 92.7	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCC=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
KDH	Q8I2S7	6.50	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`c1c(cc(c(c1O)O)O)[C@@H]2[C@@H](Cc3c(cc(cc3O2)O)…`
LU2	Q965D6	6.10	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`c1cc(c(cc1C2=CC(=O)c3c(cc(cc3O2)O)O)O)O`
CHEMBL129451	Q965D6	6.00	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
CHEMBL36327	Q965D6	6.00	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
NAR	Q965D6	—	272.3 Da LogP 2.51 TPSA 87.0	✓ Ro5	✓ Clean	`c1cc(ccc1[C@@H]2CC(=O)c3c(cc(cc3O2)O)O)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
ZINC1233995	1.000	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(O)cc12`
ZINC13152723	1.000	310.4 Da LogP 3.71 TPSA 68.2	✓ Ro5	✓ Clean	`CCn1c(NC(=O)Nc2ccccc2OC)nc2ccccc21`
ZINC1399281	1.000	297.4 Da LogP 3.19 TPSA 38.2	✓ Ro5	✓ Clean	`c1ccc(-c2nc(N3CCOCC3)c3sccc3n2)cc1`
ZINC18185774	1.000	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC27923853	1.000	300.7 Da LogP 3.87 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c(NC(=O)Nc2ccccc2Cl)nc2ccccc21`
ZINC318945	1.000	282.3 Da LogP 3.68 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N1CCCc2ccccc21`
ZINC3870412	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC3870413	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC3870414	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC3870415	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC481463	1.000	317.3 Da LogP 2.49 TPSA 85.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1cccnc1Nc1cccc(C(F)(F)F)c1`
ZINC7913991	1.000	250.3 Da LogP 3.43 TPSA 34.0	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccccc2)c2ccccc21`
ZINC8231765	1.000	342.8 Da LogP 4.16 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(NC(=O)c2cccc3cccnc23)c(OC)cc1Cl`
ZINC8429509	1.000	312.4 Da LogP 4.07 TPSA 33.2	✓ Ro5	✓ Clean	`O=C(c1csc(-c2ccsc2)n1)N1CCc2ccccc21`
ZINC8723457	1.000	252.3 Da LogP 1.75 TPSA 68.0	✓ Ro5	✓ Clean	`c1cc2c(cc1Nc1ccc3nnnn3n1)CCC2`
ZINC8726387	1.000	273.3 Da LogP 2.88 TPSA 56.5	✓ Ro5	✓ Clean	`c1ccc(-c2nc(-n3cnnc3)c3ccccc3n2)cc1`
ZINC89647	1.000	271.7 Da LogP 3.06 TPSA 55.6	✓ Ro5	✓ Clean	`Clc1ccccc1Nc1ncnc(-n2cccc2)n1`
ZINC9338279	1.000	311.3 Da LogP 3.05 TPSA 85.0	✓ Ro5	✓ Clean	`Nc1nc(-c2ccccc2)cn1NC(=O)Nc1ccccc1F`
ZINC451821	0.857	268.3 Da LogP 3.29 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N1CCc2ccccc21`
ZINC14436185	0.854	472.4 Da LogP 2.54 TPSA 186.4	2 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC3978503	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
ZINC4534390	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)c…`
ZINC4544252	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c1…`
ZINC8681494	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
ZINC8453886	0.849	431.3 Da LogP 4.65 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccc(C)cc2)c2cc(Br)c(O)c…`
ZINC14727965	0.848	426.4 Da LogP 2.82 TPSA 156.9	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)cc1)…`
ZINC12534489	0.833	307.4 Da LogP 3.39 TPSA 63.1	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(NC(=O)c2cn(C)c3ccccc23)cc1`
ZINC27923895	0.833	335.2 Da LogP 4.52 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c(NC(=O)Nc2cccc(Cl)c2Cl)nc2ccccc21`
ZINC7917230	0.833	264.3 Da LogP 3.74 TPSA 34.0	✓ Ro5	✓ Clean	`Cc1ccc(NC(=O)c2cn(C)c3ccccc23)cc1`
ZINC32497089	0.811	278.3 Da LogP 2.79 TPSA 51.1	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccccc2)c(=O)c2ccccc21`
ZINC27923339	0.800	340.4 Da LogP 3.72 TPSA 77.4	✓ Ro5	✓ Clean	`CCn1c(NC(=O)Nc2cc(OC)ccc2OC)nc2ccccc21`
ZINC5222178	0.800	431.3 Da LogP 4.64 TPSA 43.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(OC)cc12`
ZINC95453238	0.800	360.8 Da LogP 4.30 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(NC(=O)c2cc(F)cc3cccnc23)c(OC)cc1Cl`
ZINC8074404	0.795	293.3 Da LogP 2.53 TPSA 77.1	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccc(C(N)=O)cc2)c2ccccc21`
ZINC32726013	0.789	251.3 Da LogP 2.83 TPSA 46.9	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccncc2)c2ccccc21`
ZINC15934558	0.787	312.4 Da LogP 3.69 TPSA 50.8	✓ Ro5	✓ Clean	`COc1ccc(OC)c(NC(=O)N2CCCc3ccccc32)c1`
ZINC15934559	0.787	312.4 Da LogP 3.69 TPSA 50.8	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)N2CCCc3ccccc32)c(OC)c1`
ZINC27923428	0.784	344.8 Da LogP 4.36 TPSA 68.2	✓ Ro5	✓ Clean	`CCn1c(NC(=O)Nc2cc(Cl)ccc2OC)nc2ccccc21`
ZINC5875060	0.780	281.4 Da LogP 3.96 TPSA 29.0	✓ Ro5	✓ Clean	`c1ccc(-c2nc(N3CCCC3)c3sccc3n2)cc1`
ZINC3871576	0.778	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1cc(-c2ccc(O)cc2)oc2cc(O)cc(O)c12`
ZINC4348965	0.775	270.3 Da LogP 3.11 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)O[C@H](c1ccc(O)cc1)CC2=O`
ZINC4348970	0.775	270.3 Da LogP 3.11 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)O[C@@H](c1ccc(O)cc1)CC2=O`
ZINC2027558	0.773	318.3 Da LogP 3.09 TPSA 79.3	✓ Ro5	✓ Clean	`O=S(=O)(O)c1cccnc1Nc1cccc(C(F)(F)F)c1`
ZINC16552269	0.771	296.4 Da LogP 3.99 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N1CCCc2cc(C)ccc21`
ZINC6726962	0.771	296.4 Da LogP 3.99 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccc(C)cc1NC(=O)N1CCCc2ccccc21`
ZINC12515506	0.769	307.4 Da LogP 3.39 TPSA 63.1	✓ Ro5	✓ Clean	`CC(=O)Nc1cccc(NC(=O)c2cn(C)c3ccccc23)c1`
ZINC15934557	0.766	296.4 Da LogP 4.07 TPSA 41.6	✓ Ro5	✓ Clean	`CCOc1ccccc1NC(=O)N1CCCc2ccccc21`
ZINC5903093	0.762	309.4 Da LogP 4.74 TPSA 29.0	✓ Ro5	✓ Clean	`c1ccc(-c2nc(N3CCCCCC3)c3sccc3n2)cc1`
ZINC27646798	0.761	313.4 Da LogP 2.90 TPSA 58.5	✓ Ro5	✓ Clean	`Oc1cccc(-c2nc(N3CCOCC3)c3sccc3n2)c1`
ZINC21992198	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`

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.