Protein profile

PA1893

hypothetical protein

Genome: NC_002516.2

Gene: PA1893 Structure source: AlphaFold UniProt Q9I2K4

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Amino acids 809

Annotations 7

Features 24

PDB binders 27

Druggability 0.799

Overview

Basic information about this protein and its source genome.

Accession: PA1893
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1893
Status: annotated
Amino acids: 809
Structure source: AlphaFold

3.5.1.97

GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). GO:0016811 Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide. GO:0046872 Binding to a metal ion. GO:0017000 The chemical reactions and pathways resulting in the formation of an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms. GO:0009372 The cell-cell signaling process in which single-celled organisms carry out coordinated responses by monitoring their own population density, and often also that of other microbes, by producing small, diffusible, signal molecules, detecting the concentration of these molecules, and triggering a signal transduction pathway when a certain threshold is reached. Quorum sensing can occur amongst microbial communities in the environment or within host organisms. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Periplasmic

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 0.799

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

3.5.1.97

Gene Ontology (GO)

GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0016811 Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
GO:0046872 Binding to a metal ion.
GO:0017000 The chemical reactions and pathways resulting in the formation of an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms.
GO:0009372 The cell-cell signaling process in which single-celled organisms carry out coordinated responses by monitoring their own population density, and often also that of other microbes, by producing small, diffusible, signal molecules, detecting the concentration of these molecules, and triggering a signal transduction pathway when a certain threshold is reached. Quorum sensing can occur amongst microbial communities in the environment or within host organisms.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
1	12	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
13	24	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
7	29	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
34	181	Gene3D	G3DSA:1.10.439.10	Penicillin Amidohydrolase, domain 1
34	181	InterPro	IPR023343	Penicillin amidase type, domain 1
254	781	Gene3D	G3DSA:3.60.20.10	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
254	781	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
1	23	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
16	794	PIRSF	PIRSF001227	Pen_acylase
16	794	InterPro	IPR014395	Penicillin/GL-7-ACA/AHL acylase
1	29	Phobius	SIGNAL_PEPTIDE	Signal peptide region
25	29	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
9	787	PANTHER	PTHR34218	PEPTIDASE S45 PENICILLIN AMIDASE
9	787	InterPro	IPR002692	Penicillin/GL-7-ACA/AHL/aculeacin-A acylase
254	554	CDD	cd03747	Ntn_PGA_like
50	783	Pfam	PF01804	Penicillin amidase
50	783	InterPro	IPR002692	Penicillin/GL-7-ACA/AHL/aculeacin-A acylase
556	687	Gene3D	G3DSA:1.10.1400.10	-
556	687	InterPro	IPR043147	Penicillin amidase type, A-knob
44	790	SUPERFAMILY	SSF56235	N-terminal nucleophile aminohydrolases (Ntn hydrolases)
44	790	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
326	403	Gene3D	G3DSA:2.30.120.10	-
326	403	InterPro	IPR043146	Penicillin amidase type, N-terminal domain, B-knob
30	809	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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 PA1893	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
1				0.72

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.

94 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
28N	3SRC	Q9I194	269.1 Da LogP 1.48 TPSA 57.3	✓ Ro5	✓ Clean	`c1cc2c(cc1Br)N3C(=NOC3=O)CO2`
28S	3SRB	Q9I194	264.1 Da LogP 2.99 TPSA 37.8	✓ Ro5	✓ Clean	`C=CCNc1c2cc(ccc2ncn1)Br`
3LA	2WYC	Q9I194	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CC(=O)O`
3QD	4WKS	Q9I194	73.9 Da LogP -0.52 TPSA 40.5	✓ Ro5	✓ Clean	`B(CC)(O)O`
3QJ	4WKU	Q9I194	147.0 Da LogP 0.48 TPSA 60.7	✓ Ro5	✓ Clean	`[B-](CCCCCC)(O)(O)O`
3QK	4WKV	Q9I194	175.1 Da LogP 1.26 TPSA 60.7	✓ Ro5	✓ Clean	`[B-](CCCCCCCC)(O)(O)O`
4HP	1AI6	P06875	152.1 Da LogP 1.02 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(ccc1CC(=O)O)O`
83M	5UBK	Q9I194	658.8 Da LogP 2.83 TPSA 212.3	2 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)N[C@@H](CCC(=O)N[C@H](Cc1ccc(…`
A08	4K2F	Q9I194	263.1 Da LogP 4.04 TPSA 36.7	✓ Ro5	✓ Clean	`c1cc(nc(c1)Cl)C(C#N)c2ccc(cc2)Cl`
AAN	1AJN	P06875	181.1 Da LogP 1.22 TPSA 80.4	✓ Ro5	✓ Clean	`c1cc(ccc1CC(=O)O)[N+](=O)[O-]`
B0S	4M1J	Q9I194	228.2 Da LogP 3.77 TPSA 40.5	✓ Ro5	✓ Clean	`B(CCCCCCCCCCCCC)(O)O`
BUB	4WKT	Q9I194	101.9 Da LogP 0.26 TPSA 40.5	✓ Ro5	✓ Clean	`B(CCCC)(O)O`
CEN	1JVZ	Q9L5D6	386.4 Da LogP -0.46 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(N2[C@@H]([C@@H](C2=O)NC(=O)CCCC(=O…`
DAO	2WYB	Q9I194	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
DHY	1AI4	P06875	168.1 Da LogP 0.72 TPSA 77.8	✓ Ro5	Alert	`c1cc(c(cc1CC(=O)O)O)O`
GRO	1K5S	P06875	150.2 Da LogP 1.87 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](c1ccccc1)C(=O)O`
GUA	1JW0	Q9L5D6	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
IPH	1AI7	P06875	94.1 Da LogP 1.39 TPSA 20.2	✓ Ro5	✓ Clean	`c1ccc(cc1)O`
MNP	1AI5	P06875	181.1 Da LogP 1.22 TPSA 80.4	✓ Ro5	✓ Clean	`c1cc(cc(c1)[N+](=O)[O-])CC(=O)O`
MYR	3L94	Q9I194	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
OCA	3L91	Q9I194	144.2 Da LogP 2.43 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCC(=O)O`
OMD	1AJP	P06875	168.1 Da LogP 0.72 TPSA 77.8	✓ Ro5	✓ Clean	`c1cc(c(cc1O)CC(=O)O)O`
PAC	1FXH	P06875	136.1 Da LogP 1.31 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)CC(=O)O`
PMS	1PNM	P06875	172.2 Da LogP 1.07 TPSA 54.4	✓ Ro5	✓ Clean	`c1ccc(cc1)CS(=O)(=O)O`
PNN	1FXV	P06875	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1([C@@H](N2[C@H](S1)[C@@H](C2=O)NC(=O)Cc3cccc…`
SOX	1GM8	P06875	352.4 Da LogP 0.60 TPSA 106.9	✓ Ro5	✓ Clean	`CC1([C@@H](N2[C@H]([S@H]1O)[C@@H](C2=O)NC(=O)Cc…`
SPA	1AJQ	P06875	142.2 Da LogP 1.38 TPSA 37.3	✓ Ro5	✓ Clean	`c1cc(sc1)CC(=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
1OQ	Q9I194	9.72	280.2 Da LogP 3.89 TPSA 36.7	✓ Ro5	✓ Clean	`c1cc(nc(c1)C(F)(F)F)C(C#N)c2ccc(cc2)F`
CHEMBL1522037	Q9I194	6.35	274.3 Da LogP 3.79 TPSA 35.5	✓ Ro5	✓ Clean	`CCOC(=O)c1cc2c(s1)-c1c(C)cccc1OC2`
CHEMBL1518307	Q9I194	6.19	298.6 Da LogP 4.09 TPSA 49.6	✓ Ro5	✓ Clean	`N#CC(c1ccc(Cl)nn1)c1ccc(Cl)cc1Cl`
CHEMBL1523811	Q9I194	6.17	233.2 Da LogP 2.14 TPSA 61.6	✓ Ro5	✓ Clean	`COC(=O)c1cc(-c2ccc(OC)cc2)on1`
CHEMBL1471416	Q9I194	6.07	258.7 Da LogP 3.40 TPSA 45.9	✓ Ro5	✓ Clean	`COc1ccccc1C(C#N)c1cccc(Cl)n1`
CHEMBL1305969	Q9I194	6.03	331.1 Da LogP 5.06 TPSA 36.7	1 viol.	✓ Clean	`N#CC(c1ccc(Cl)cc1)c1ncc(C(F)(F)F)cc1Cl`
CHEMBL1408848	Q9I194	6.03	264.1 Da LogP 3.44 TPSA 49.6	✓ Ro5	✓ Clean	`N#CC(c1ccc(Cl)nn1)c1ccccc1Cl`
CHEMBL1594533	Q9I194	6.02	268.7 Da LogP 2.92 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(NC1CCCC1)c1cc(Cl)ccc1[N+](=O)[O-]`
CHEMBL1532304	Q9I194	6.00	264.1 Da LogP 3.44 TPSA 49.6	✓ Ro5	✓ Clean	`N#CC(c1ccc(Cl)cc1)c1ccc(Cl)nn1`
CHEMBL1331685	Q9I194	—	282.1 Da LogP 2.89 TPSA 52.3	✓ Ro5	✓ Clean	`COC(=O)c1cc(-c2ccc(Br)cc2)on1`
CHEMBL1346274	Q9I194	—	226.3 Da LogP 2.87 TPSA 25.8	✓ Ro5	✓ Clean	`C#CCSc1ncc(-c2ccccc2)cn1`
CHEMBL1373207	Q9I194	—	266.3 Da LogP 3.24 TPSA 35.5	✓ Ro5	✓ Clean	`COc1ccc(C2=C(C=O)Cc3ccccc3O2)cc1`
CHEMBL1415756	Q9I194	—	243.3 Da LogP 1.90 TPSA 78.1	✓ Ro5	✓ Clean	`CCOC(=O)c1cnc(-c2ccccc2)nc1N`
CHEMBL1447543	Q9I194	—	222.3 Da LogP 3.17 TPSA 27.0	✓ Ro5	✓ Clean	`N#CN(Cc1ccccc1)Cc1ccccc1`
CHEMBL1460259	Q9I194	—	217.2 Da LogP 2.07 TPSA 70.2	✓ Ro5	Alert	`N#Cc1cc([N+](=O)[O-])ccc1N1CCCC1`
CHEMBL1481107	Q9I194	—	244.3 Da LogP 1.31 TPSA 69.9	✓ Ro5	✓ Clean	`C=CCOC(=O)c1ccc(-n2cnc(C)n2)nc1`
CHEMBL1504742	Q9I194	—	214.7 Da LogP 3.27 TPSA 36.7	✓ Ro5	✓ Clean	`N#Cc1cc(-c2ccccc2)cnc1Cl`

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
ZINC1396396	1.000	264.1 Da LogP 3.44 TPSA 49.6	✓ Ro5	✓ Clean	`N#C[C@@H](c1ccc(Cl)nn1)c1ccccc1Cl`
ZINC1396397	1.000	264.1 Da LogP 3.44 TPSA 49.6	✓ Ro5	✓ Clean	`N#C[C@H](c1ccc(Cl)nn1)c1ccccc1Cl`
ZINC1396404	1.000	264.1 Da LogP 3.44 TPSA 49.6	✓ Ro5	✓ Clean	`N#C[C@H](c1ccc(Cl)cc1)c1ccc(Cl)nn1`
ZINC1396405	1.000	264.1 Da LogP 3.44 TPSA 49.6	✓ Ro5	✓ Clean	`N#C[C@@H](c1ccc(Cl)cc1)c1ccc(Cl)nn1`
ZINC1403103	1.000	263.1 Da LogP 4.04 TPSA 36.7	✓ Ro5	✓ Clean	`N#C[C@@H](c1ccc(Cl)cc1)c1cccc(Cl)n1`
ZINC1403104	1.000	263.1 Da LogP 4.04 TPSA 36.7	✓ Ro5	✓ Clean	`N#C[C@H](c1ccc(Cl)cc1)c1cccc(Cl)n1`
ZINC1403113	1.000	258.7 Da LogP 3.40 TPSA 45.9	✓ Ro5	✓ Clean	`COc1ccccc1[C@@H](C#N)c1cccc(Cl)n1`
ZINC1403114	1.000	258.7 Da LogP 3.40 TPSA 45.9	✓ Ro5	✓ Clean	`COc1ccccc1[C@H](C#N)c1cccc(Cl)n1`
ZINC1530218	1.000	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](NC(=O)Cc3ccccc3)C(=O)N2[C@…`
ZINC169455	1.000	214.7 Da LogP 3.27 TPSA 36.7	✓ Ro5	✓ Clean	`N#Cc1cc(-c2ccccc2)cnc1Cl`
ZINC169583	1.000	298.6 Da LogP 4.09 TPSA 49.6	✓ Ro5	✓ Clean	`N#C[C@@H](c1ccc(Cl)nn1)c1ccc(Cl)cc1Cl`
ZINC169584	1.000	298.6 Da LogP 4.09 TPSA 49.6	✓ Ro5	✓ Clean	`N#C[C@H](c1ccc(Cl)nn1)c1ccc(Cl)cc1Cl`
ZINC1718678	1.000	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@@H](NC(=O)Cc3ccccc3)C(=O)N2[C@H…`
ZINC1766166	1.000	264.1 Da LogP 2.99 TPSA 37.8	✓ Ro5	✓ Clean	`C=CCNc1ncnc2ccc(Br)cc12`
ZINC204272	1.000	233.2 Da LogP 2.14 TPSA 61.6	✓ Ro5	✓ Clean	`COC(=O)c1cc(-c2ccc(OC)cc2)on1`
ZINC2503034	1.000	282.1 Da LogP 2.89 TPSA 52.3	✓ Ro5	✓ Clean	`COC(=O)c1cc(-c2ccc(Br)cc2)on1`
ZINC2572643	1.000	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@@H](NC(=O)Cc3ccccc3)C(=O)N2[C@…`
ZINC3133757	1.000	226.3 Da LogP 2.87 TPSA 25.8	✓ Ro5	✓ Clean	`C#CCSc1ncc(-c2ccccc2)cn1`
ZINC3642681	1.000	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@@H](NC(=O)Cc3ccccc3)C(=O)N2[C@@…`
ZINC375641	1.000	268.7 Da LogP 2.92 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(NC1CCCC1)c1cc(Cl)ccc1[N+](=O)[O-]`
ZINC3871699	1.000	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)Cc3ccccc3)C(=O)N2[C@H]…`
ZINC3871700	1.000	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)Cc3ccccc3)C(=O)N2[C@@H…`
ZINC3871701	1.000	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)Cc3ccccc3)C(=O)N2[C@H…`
ZINC3871702	1.000	334.4 Da LogP 0.86 TPSA 86.7	✓ Ro5	✓ Clean	`CC1(C)S[C@@H]2[C@H](NC(=O)Cc3ccccc3)C(=O)N2[C@@…`
ZINC3880689	1.000	243.3 Da LogP 1.90 TPSA 78.1	✓ Ro5	✓ Clean	`CCOC(=O)c1cnc(-c2ccccc2)nc1N`
ZINC400096	1.000	222.3 Da LogP 3.17 TPSA 27.0	✓ Ro5	✓ Clean	`N#CN(Cc1ccccc1)Cc1ccccc1`
ZINC4702037	1.000	217.2 Da LogP 2.07 TPSA 70.2	✓ Ro5	Alert	`N#Cc1cc([N+](=O)[O-])ccc1N1CCCC1`
ZINC6925410	1.000	244.3 Da LogP 1.31 TPSA 69.9	✓ Ro5	✓ Clean	`C=CCOC(=O)c1ccc(-n2cnc(C)n2)nc1`
ZINC7253	1.000	269.1 Da LogP 1.48 TPSA 57.3	✓ Ro5	✓ Clean	`O=c1onc2n1-c1cc(Br)ccc1OC2`
ZINC8927232	1.000	386.4 Da LogP -0.46 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(C(=O)O)N2C(=O)[C@@H](NC(=O)CCCC(=O…`
ZINC8927234	1.000	386.4 Da LogP -0.46 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(C(=O)O)N2C(=O)[C@@H](NC(=O)CCCC(=O…`
ZINC8927236	1.000	386.4 Da LogP -0.46 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(C(=O)O)N2C(=O)[C@H](NC(=O)CCCC(=O)…`
ZINC8927238	1.000	386.4 Da LogP -0.46 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(C(=O)O)N2C(=O)[C@H](NC(=O)CCCC(=O)…`
ZINC95872307	1.000	280.2 Da LogP 3.89 TPSA 36.7	✓ Ro5	✓ Clean	`N#C[C@@H](c1ccc(F)cc1)c1cccc(C(F)(F)F)n1`
ZINC95872308	1.000	280.2 Da LogP 3.89 TPSA 36.7	✓ Ro5	✓ Clean	`N#C[C@H](c1ccc(F)cc1)c1cccc(C(F)(F)F)n1`
ZINC441668	0.974	282.7 Da LogP 3.31 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(NC1CCCCC1)c1cc(Cl)ccc1[N+](=O)[O-]`
ZINC449879	0.974	296.8 Da LogP 3.70 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(NC1CCCCCC1)c1cc(Cl)ccc1[N+](=O)[O-]`
ZINC4905271	0.968	231.3 Da LogP 2.46 TPSA 70.2	✓ Ro5	Alert	`N#Cc1cc([N+](=O)[O-])ccc1N1CCCCC1`
ZINC6335324	0.968	259.3 Da LogP 3.24 TPSA 70.2	✓ Ro5	Alert	`N#Cc1cc([N+](=O)[O-])ccc1N1CCCCCCC1`
ZINC8054836	0.968	245.3 Da LogP 2.85 TPSA 70.2	✓ Ro5	Alert	`N#Cc1cc([N+](=O)[O-])ccc1N1CCCCCC1`
ZINC9851542	0.902	372.4 Da LogP -0.85 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(C(=O)O)N2C(=O)[C@@H](NC(=O)CCC(=O)…`
ZINC9851543	0.902	372.4 Da LogP -0.85 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(C(=O)O)N2C(=O)[C@@H](NC(=O)CCC(=O)…`
ZINC9851544	0.902	372.4 Da LogP -0.85 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(C(=O)O)N2C(=O)[C@H](NC(=O)CCC(=O)O…`
ZINC9851545	0.902	372.4 Da LogP -0.85 TPSA 150.3	✓ Ro5	✓ Clean	`CC(=O)OCC1=C(C(=O)O)N2C(=O)[C@H](NC(=O)CCC(=O)O…`
ZINC483086	0.895	240.6 Da LogP 2.14 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(NC1CC1)c1cc(Cl)ccc1[N+](=O)[O-]`
ZINC33427634	0.889	257.2 Da LogP 2.89 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccc([N+](=O)[O-])cc2)cc1`
ZINC32222424	0.864	228.2 Da LogP 2.69 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccc(O)cc2)cc1`
ZINC1857794104	0.838	283.3 Da LogP 3.29 TPSA 61.6	✓ Ro5	✓ Clean	`COC(=O)c1cc(-c2ccc3cc(OC)ccc3c2)on1`
ZINC6617263	0.826	333.4 Da LogP 0.26 TPSA 92.5	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)Cc3ccccc3)C(=O)N2[C@H]…`
ZINC6617300	0.826	333.4 Da LogP 0.26 TPSA 92.5	✓ Ro5	✓ Clean	`CC1(C)S[C@H]2[C@H](NC(=O)Cc3ccccc3)C(=O)N2[C@@H…`

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.