Protein profile

PA3247

aminopeptidase

Genome: NC_002516.2

Gene: PA3247 apeB Structure source: Experimental + AlphaFold UniProt Q9HYZ3

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Amino acids 429

Annotations 6

Features 25

PDB binders 3

Druggability 0.535

Overview

Basic information about this protein and its source genome.

Accession: PA3247
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3247 apeB
Status: annotated
Amino acids: 429
Structure source: Experimental + AlphaFold

3.4.11.-

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004177 Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain. GO:0008237 Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. GO:0008270 Binding to a zinc ion (Zn). GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 51.786
Human E-value: 6.940000000000001e-31
Gut microbiome off-target: hit
Essential (DEG): N
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 0.535

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

3.4.11.-

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004177 Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
GO:0008237 Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
GO:0008270 Binding to a zinc ion (Zn).
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
301	317	PRINTS	PR00932	Aminopeptidase I zinc metalloprotease (M18) signature
301	317	InterPro	IPR001948	Peptidase M18
109	129	PRINTS	PR00932	Aminopeptidase I zinc metalloprotease (M18) signature
109	129	InterPro	IPR001948	Peptidase M18
76	92	PRINTS	PR00932	Aminopeptidase I zinc metalloprotease (M18) signature
76	92	InterPro	IPR001948	Peptidase M18
144	161	PRINTS	PR00932	Aminopeptidase I zinc metalloprotease (M18) signature
144	161	InterPro	IPR001948	Peptidase M18
390	405	PRINTS	PR00932	Aminopeptidase I zinc metalloprotease (M18) signature
390	405	InterPro	IPR001948	Peptidase M18
262	280	PRINTS	PR00932	Aminopeptidase I zinc metalloprotease (M18) signature
262	280	InterPro	IPR001948	Peptidase M18
86	218	Gene3D	G3DSA:2.30.250.10	Aminopeptidase i, Domain 2
86	218	InterPro	IPR023358	Peptidase M18, domain 2
1	425	Hamap	MF_00467	Probable M18 family aminopeptidase 2 [apeB].
1	425	InterPro	IPR022984	M18 family aminopeptidase 2, putative
86	218	FunFam	G3DSA:2.30.250.10:FF:000003	Probable M18 family aminopeptidase 2
88	213	SUPERFAMILY	SSF101821	Aminopeptidase/glucanase lid domain
12	423	Pfam	PF02127	Aminopeptidase I zinc metalloprotease (M18)
12	423	InterPro	IPR001948	Peptidase M18
4	423	SUPERFAMILY	SSF53187	Zn-dependent exopeptidases
4	425	PANTHER	PTHR28570	ASPARTYL AMINOPEPTIDASE
4	425	InterPro	IPR001948	Peptidase M18
10	422	Gene3D	G3DSA:3.40.630.10	Zn peptidases
6	424	CDD	cd05639	M18

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

6 + 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 3WT4	X-ray	2.30 Å	A,B,C,D	100.0% 1-429	PDBe RCSB PDBj File	Viewing
PDB 4NJR	X-ray	2.30 Å	A,B,C,D	100.0% 1-429	PDBe RCSB PDBj File	Loaded
PDB 4OID	X-ray	2.30 Å	A,B,C,D	100.0% 1-429	PDBe RCSB PDBj File	Loaded
PDB 4OIW	X-ray	2.44 Å	A,B,C,D,E,F	100.0% 1-429	PDBe RCSB PDBj File	Loaded
PDB 4NJQ	X-ray	2.70 Å	A,B,C,D	100.0% 1-429	PDBe RCSB PDBj File	Loaded
PDB 2IJZ	X-ray	3.00 Å	A,B,C,D,E,F,G,H,I,J,K,L	99.8% 2-429	PDBe RCSB PDBj File	Loaded
AlphaFold PA3247	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
9				0.387
2				0.248
5				0.205

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	30.52	0.935
2	25.7	0.908
3	22.65	0.882
4	22.22	0.879
5	17.22	0.799

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
4				0.366
7				0.255

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.

87 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
NHE	4NJQ 2.70 Å Open crystal	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`

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
CAC	5JH9	P14904	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
SD4	4DYO	Q9ULA0	148.1 Da LogP -1.71 TPSA 112.6	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)N)C(=O)NO`

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
CHEMBL1491188	Q8I2J3	6.70	159.2 Da LogP -0.02 TPSA 78.9	✓ Ro5	✓ Clean	`O=C(O)CSc1nc[nH]n1`
CHEMBL1411184	Q8I2J3	6.46	318.3 Da LogP 0.69 TPSA 105.2	✓ Ro5	✓ Clean	`O=C(CSc1nc[nH]n1)OCN1C(=O)c2ccccc2C1=O`
CHEMBL1454448	Q8I2J3	6.46	310.3 Da LogP 0.09 TPSA 94.4	✓ Ro5	✓ Clean	`COC(=O)CN(n1cnnc1)S(=O)(=O)c1ccc(C)cc1`
CHEMBL1472465	Q8I2J3	6.45	278.2 Da LogP 0.97 TPSA 124.2	✓ Ro5	✓ Clean	`COc1cc([N+](=O)[O-])ccc1NC(=O)Nn1cnnc1`
CHEMBL1577602	Q8I2J3	6.42	330.8 Da LogP 0.43 TPSA 94.4	✓ Ro5	✓ Clean	`COC(=O)CN(n1cnnc1)S(=O)(=O)c1ccccc1Cl`
CHEMBL1173475	Q8I2J3	6.41	320.3 Da LogP 1.16 TPSA 162.9	✓ Ro5	Alert	`O.O=c1c(O)c(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c12`
CHEMBL1454686	Q8I2J3	6.35	318.4 Da LogP 2.05 TPSA 96.5	✓ Ro5	✓ Clean	`O=C(CSc1nc[nH]n1)Nc1nc(-c2ccccc2)ns1`
DHB	Q8I2J3	6.32	154.1 Da LogP 0.80 TPSA 77.8	✓ Ro5	Alert	`c1cc(c(cc1C(=O)O)O)O`
CHEMBL1580760	Q8I2J3	6.30	296.3 Da LogP -0.22 TPSA 94.4	✓ Ro5	✓ Clean	`COC(=O)CN(n1cnnc1)S(=O)(=O)c1ccccc1`
CHEMBL1587839	Q8I2J3	6.30	272.1 Da LogP 2.36 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1cc(Cl)ccc1Cl)Nn1cnnc1`
CHEMBL309130	Q9ULA0	6.29	264.4 Da LogP 1.08 TPSA 75.3	✓ Ro5	✓ Clean	`CC(C)CCNC(=O)[C@@H](O)[C@H](N)Cc1ccccc1`
CHEMBL1300187	Q8I2J3	6.22	279.3 Da LogP 0.17 TPSA 125.5	✓ Ro5	✓ Clean	`O=C(O)C(=O)O.OC(Cn1cnnc1)c1ccccc1`
CHEMBL1595557	Q8I2J3	6.21	395.4 Da LogP 1.29 TPSA 166.4	✓ Ro5	✓ Clean	`CCOC(=O)NC(=O)COC(=O)c1ccc(Sc2nc[nH]n2)c([N+](=…`
CHEMBL1428639	Q8I2J3	6.20	272.1 Da LogP 2.36 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1cccc(Cl)c1Cl)Nn1cnnc1`
CHEMBL1310318	Q8I2J3	6.19	259.3 Da LogP 3.50 TPSA 22.0	✓ Ro5	✓ Clean	`Cc1ccccc1-n1sc2cc(F)ccc2c1=O`
CHEMBL1378617	Q8I2J3	6.18	242.2 Da LogP 1.72 TPSA 73.0	✓ Ro5	✓ Clean	`Cc1c(C(=O)Nn2cnnc2)oc2ccccc12`
CHEMBL1534622	Q8I2J3	6.18	288.2 Da LogP 2.53 TPSA 54.8	✓ Ro5	✓ Clean	`S=C(Nc1cc(Cl)ccc1Cl)Nn1cnnc1`
CHEMBL1333659	Q8I2J3	6.17	291.2 Da LogP 1.38 TPSA 149.8	✓ Ro5	Alert	`O=[N+]([O-])c1c(O)nc(/C=C\c2ccc(O)c(O)c2)nc1O`
CHEMBL1444299	Q8I2J3	6.15	316.5 Da LogP 2.47 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Br)cc1Cl)Nn1cnnc1`
CHEMBL1574908	Q8I2J3	6.15	346.4 Da LogP 3.57 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)/C1=C\c1cn(-c2ccccc2)nc1-c1ccc(F)cc1`
CHEMBL1412741	Q8I2J3	6.10	272.1 Da LogP 2.36 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Cl)cc1Cl)Nn1cnnc1`
CHEMBL3189719	Q8I2J3	6.09	348.2 Da LogP 4.91 TPSA 52.8	✓ Ro5	Alert	`CC(C)(C)c1ccc(O)c(/N=C/c2cc(Br)ccc2O)c1`
CHEMBL1345210	Q8I2J3	6.08	259.3 Da LogP 1.75 TPSA 87.6	✓ Ro5	✓ Clean	`Oc1nc(CSc2nc[nH]n2)nc2ccccc12`
CHEMBL1491018	Q8I2J3	6.08	267.7 Da LogP 1.72 TPSA 81.1	✓ Ro5	✓ Clean	`COc1ccc(Cl)cc1NC(=O)Nn1cnnc1`
CHEMBL1529736	Q8I2J3	6.08	272.1 Da LogP 2.36 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Cl)c(Cl)c1)Nn1cnnc1`
CHEMBL1502569	Q8I2J3	6.07	294.3 Da LogP 1.36 TPSA 107.5	✓ Ro5	✓ Clean	`COc1cc([N+](=O)[O-])ccc1N=C(S)Nn1cnnc1`
CHEMBL1588469	Q8I2J3	6.06	265.2 Da LogP 0.96 TPSA 124.7	✓ Ro5	Alert	`CC1=C([N+](=O)[O-])C(c2ccc(O)c(O)c2)NC(=O)N1`
CHEMBL1348865	Q8I2J3	6.04	379.4 Da LogP 1.73 TPSA 99.5	✓ Ro5	✓ Clean	`CCOc1cc(C(=O)NC(=S)Nn2cnnc2)cc(OCC)c1OCC`
CHEMBL1382638	Q8I2J3	6.03	248.2 Da LogP 0.96 TPSA 115.0	✓ Ro5	✓ Clean	`O=C(Nc1cccc([N+](=O)[O-])c1)Nn1cnnc1`
CHEMBL1412811	Q8I2J3	6.01	394.6 Da LogP 2.63 TPSA 113.8	✓ Ro5	✓ Clean	`Cl.O=C(CSc1nc[nH]n1)Nc1ccc([N+](=O)[O-])cc1Br`
CHEMBL143589	Q9ULA0	6.00	262.4 Da LogP 1.29 TPSA 72.2	✓ Ro5	✓ Clean	`CC(C)CCNC(=O)C(=O)C(N)Cc1ccccc1`
CHEMBL3195950	Q8I2J3	6.00	204.2 Da LogP 0.57 TPSA 83.5	✓ Ro5	Alert	`Oc1ccc(/C=N/n2cncn2)cc1O`
CHEMBL1377903	Q8I2J3	—	331.3 Da LogP 2.93 TPSA 108.3	✓ Ro5	✓ Clean	`O=c1c2c([N+](=O)[O-])cc([N+](=O)[O-])cc2sn1Cc1c…`
CHEMBL4129274	Q9ULA0	—	851.5 Da LogP 4.76 TPSA 183.3	3 viol.	Alert	`C=CC(=O)Nc1ccccc1Nc1nc(Nc2ccc(N3CCN(CCOCCOCCOCC…`

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
ZINC102682503	1.000	346.4 Da LogP 3.57 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)/C1=C/c1cn(-c2ccccc2)nc1-c1ccc(F)cc1`
ZINC13130661	1.000	346.4 Da LogP 3.57 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)/C1=C\c1cn(-c2ccccc2)nc1-c1ccc(F)cc1`
ZINC1430592	1.000	259.3 Da LogP 3.50 TPSA 22.0	✓ Ro5	✓ Clean	`Cc1ccccc1-n1sc2cc(F)ccc2c1=O`
ZINC15933798	1.000	272.1 Da LogP 2.36 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1cc(Cl)ccc1Cl)Nn1cnnc1`
ZINC15952143	1.000	272.1 Da LogP 2.36 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Cl)cc1Cl)Nn1cnnc1`
ZINC1710230	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC2040386982	1.000	346.4 Da LogP 3.57 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)C1=Cc1cn(-c2ccccc2)nc1-c1ccc(F)cc1`
ZINC270481	1.000	330.8 Da LogP 0.43 TPSA 94.4	✓ Ro5	✓ Clean	`COC(=O)CN(n1cnnc1)S(=O)(=O)c1ccccc1Cl`
ZINC3017636	1.000	242.2 Da LogP 1.72 TPSA 73.0	✓ Ro5	✓ Clean	`Cc1c(C(=O)Nn2cnnc2)oc2ccccc12`
ZINC315387	1.000	296.3 Da LogP -0.22 TPSA 94.4	✓ Ro5	✓ Clean	`COC(=O)CN(n1cnnc1)S(=O)(=O)c1ccccc1`
ZINC329887	1.000	272.1 Da LogP 2.36 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Cl)c(Cl)c1)Nn1cnnc1`
ZINC3664447	1.000	331.3 Da LogP 2.93 TPSA 108.3	✓ Ro5	✓ Clean	`O=c1c2c([N+](=O)[O-])cc([N+](=O)[O-])cc2sn1Cc1c…`
ZINC370157	1.000	265.2 Da LogP 0.96 TPSA 124.7	✓ Ro5	Alert	`CC1=C([N+](=O)[O-])[C@@H](c2ccc(O)c(O)c2)NC(=O)…`
ZINC370162	1.000	265.2 Da LogP 0.96 TPSA 124.7	✓ Ro5	Alert	`CC1=C([N+](=O)[O-])[C@H](c2ccc(O)c(O)c2)NC(=O)N1`
ZINC5041912	1.000	278.2 Da LogP 0.97 TPSA 124.2	✓ Ro5	✓ Clean	`COc1cc([N+](=O)[O-])ccc1NC(=O)Nn1cnnc1`
ZINC506138	1.000	310.3 Da LogP 0.09 TPSA 94.4	✓ Ro5	✓ Clean	`COC(=O)CN(n1cnnc1)S(=O)(=O)c1ccc(C)cc1`
ZINC5560695	1.000	379.4 Da LogP 1.73 TPSA 99.5	✓ Ro5	✓ Clean	`CCOc1cc(C(=O)NC(=S)Nn2cnnc2)cc(OCC)c1OCC`
ZINC609288	1.000	272.1 Da LogP 2.36 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1cccc(Cl)c1Cl)Nn1cnnc1`
ZINC610761	1.000	267.7 Da LogP 1.72 TPSA 81.1	✓ Ro5	✓ Clean	`COc1ccc(Cl)cc1NC(=O)Nn1cnnc1`
ZINC621606	1.000	316.5 Da LogP 2.47 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Br)cc1Cl)Nn1cnnc1`
ZINC3869685	0.971	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	Alert	`O=c1c(O)c(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC100529780	0.872	328.4 Da LogP 3.43 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)/C1=C\c1cn(-c2ccccc2)nc1-c1ccccc1`
ZINC13120292	0.872	328.4 Da LogP 3.43 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)/C1=C/c1cn(-c2ccccc2)nc1-c1ccccc1`
ZINC2042434552	0.872	328.4 Da LogP 3.43 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)C1=Cc1cn(-c2ccccc2)nc1-c1ccccc1`
ZINC12558357	0.824	407.3 Da LogP 4.19 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)/C1=C\c1cn(-c2ccccc2)nc1-c1ccc(Br)cc1`
ZINC12574265	0.824	362.8 Da LogP 4.08 TPSA 59.3	✓ Ro5	Alert	`CC1=NNC(=O)/C1=C\c1cn(-c2ccccc2)nc1-c1ccc(Cl)cc1`
ZINC17015135	0.792	358.4 Da LogP 3.44 TPSA 68.5	✓ Ro5	Alert	`COc1ccc(-c2nn(-c3ccccc3)cc2/C=C2\C(=O)NN=C2C)cc1`
ZINC5157307	0.792	358.4 Da LogP 3.44 TPSA 68.5	✓ Ro5	Alert	`COc1ccc(-c2nn(-c3ccccc3)cc2/C=C2/C(=O)NN=C2C)cc1`
ZINC2004372	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC15951951	0.778	237.7 Da LogP 1.71 TPSA 71.8	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1Cl)Nn1cnnc1`
ZINC3276872	0.778	288.2 Da LogP 2.53 TPSA 54.8	✓ Ro5	✓ Clean	`S=C(Nc1ccc(Cl)cc1Cl)Nn1cnnc1`
ZINC6569077	0.771	294.3 Da LogP 1.14 TPSA 107.1	✓ Ro5	✓ Clean	`COc1cc([N+](=O)[O-])ccc1NC(=S)Nn1cnnc1`
ZINC3869768	0.763	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2)oc2cc(O)cc(O)c12`
ZINC3181528	0.762	320.3 Da LogP 1.86 TPSA 87.5	✓ Ro5	✓ Clean	`CCOc1cc(C(=O)Nn2cnnc2)cc(OCC)c1OCC`
ZINC611720	0.762	247.3 Da LogP 1.37 TPSA 81.1	✓ Ro5	✓ Clean	`COc1ccc(C)cc1NC(=O)Nn1cnnc1`
ZINC285073	0.761	279.3 Da LogP 1.26 TPSA 113.7	✓ Ro5	✓ Clean	`COc1cc([C@H]2NC(=O)NC(C)=C2[N+](=O)[O-])ccc1O`
ZINC285074	0.761	279.3 Da LogP 1.26 TPSA 113.7	✓ Ro5	✓ Clean	`COc1cc([C@@H]2NC(=O)NC(C)=C2[N+](=O)[O-])ccc1O`
ZINC4349582	0.750	300.3 Da LogP 2.59 TPSA 111.1	✓ Ro5	Alert	`Cc1c(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c2c1=O`
ZINC15952148	0.744	251.7 Da LogP 2.02 TPSA 71.8	✓ Ro5	✓ Clean	`Cc1c(Cl)cccc1NC(=O)Nn1cnnc1`
ZINC238052	0.738	249.2 Da LogP 1.25 TPSA 104.5	✓ Ro5	✓ Clean	`CC1=C([N+](=O)[O-])[C@@H](c2ccc(O)cc2)NC(=O)N1`
ZINC238054	0.738	249.2 Da LogP 1.25 TPSA 104.5	✓ Ro5	✓ Clean	`CC1=C([N+](=O)[O-])[C@H](c2ccc(O)cc2)NC(=O)N1`
ZINC13839921	0.737	267.7 Da LogP 2.18 TPSA 54.8	✓ Ro5	✓ Clean	`Cc1ccc(Cl)cc1NC(=S)Nn1cnnc1`
ZINC15934254	0.737	251.7 Da LogP 2.02 TPSA 71.8	✓ Ro5	✓ Clean	`Cc1ccc(Cl)cc1NC(=O)Nn1cnnc1`
ZINC3874317	0.737	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`
ZINC101057839	0.735	371.0 Da LogP 4.37 TPSA 52.8	✓ Ro5	Alert	`Oc1ccc(Br)cc1/C=N/c1cc(Br)ccc1O`
ZINC148781474	0.727	274.2 Da LogP 2.16 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(C(=O)O)cc2O)c(O)c1`
ZINC1430602	0.725	273.3 Da LogP 3.81 TPSA 22.0	✓ Ro5	✓ Clean	`Cc1ccc(C)c(-n2sc3cc(F)ccc3c2=O)c1`
ZINC30836214	0.721	362.3 Da LogP 3.16 TPSA 145.9	✓ Ro5	✓ Clean	`COc1cc([N+](=O)[O-])ccc1NC(=O)Nc1ccc([N+](=O)[O…`
ZINC3875620	0.721	316.3 Da LogP 2.29 TPSA 120.4	✓ Ro5	Alert	`COc1cc(O)c2c(=O)c(O)c(-c3ccc(O)c(O)c3)oc2c1`

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.