Protein profile

PA1803

Lon protease

Genome: NC_002516.2

Gene: lon PA1803 Structure source: AlphaFold UniProt Q9I2T9

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Amino acids 798

Annotations 17

Features 51

PDB binders 8

Druggability 0.482

Overview

Basic information about this protein and its source genome.

Accession: PA1803
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: lon PA1803
Status: annotated
Amino acids: 798
Structure source: AlphaFold

3.4.21.53

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. 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:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. GO:0043565 Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 52.492
Human E-value: 5.03e-111
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 0.482

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 16 GO

Enzyme Commission (EC)

3.4.21.53

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
GO:0043565 Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO:0071978 Bacterial-type flagellum-dependent cell motility in which the action of numerous flagella results in the smooth movement of a group of cells along a solid surface. Swarming motility is observed in groups of bacteria.
GO:0071977 Bacterial-type flagellum-dependent cell motility that results in the smooth movement of a cell through a liquid medium.
GO:0071236 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
GO:0034605 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
GO:0006515 The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
GO:0030254 The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
GO:0044010 A process in which planktonically growing microorganisms of the same species grow at a liquid-air interface or on a solid substrate under the flow of a liquid and produce extracellular polymers that facilitate matrix formation, resulting in a change in the organisms' growth rate and gene transcription.
GO:0043107 Any process involved in the controlled movement of a bacterial cell which is dependent on the presence of type IV pili. Includes social gliding motility and twitching motility.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

51 records

Show feature table

Start	End	DB	Term	Name
233	253	Coils	Coil	Coil
590	765	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
590	765	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold
7	198	ProSiteProfiles	PS51787	Lon N-terminal domain profile.
7	198	InterPro	IPR003111	Lon protease, N-terminal domain
2	114	Gene3D	G3DSA:2.30.130.40	-
2	114	InterPro	IPR046336	Lon protease, N-terminal domain superfamily
117	241	Gene3D	G3DSA:1.20.58.1480	-
775	798	MobiDBLite	mobidb-lite	consensus disorder prediction
487	575	Gene3D	G3DSA:1.10.8.60	-
565	767	Pfam	PF05362	Lon protease (S16) C-terminal proteolytic domain
565	767	InterPro	IPR008269	Peptidase S16, Lon proteolytic domain
348	484	Pfam	PF00004	ATPase family associated with various cellular activities (AAA)
348	484	InterPro	IPR003959	ATPase, AAA-type, core
8	766	NCBIfam	TIGR00763	endopeptidase La
8	766	InterPro	IPR004815	Lon protease, bacterial/eukaryotic-type
309	489	CDD	cd19500	RecA-like_Lon
6	198	SMART	SM00464	lon_5
6	198	InterPro	IPR003111	Lon protease, N-terminal domain
1	770	PIRSF	PIRSF001174	Lon_proteas
1	770	InterPro	IPR004815	Lon protease, bacterial/eukaryotic-type
344	488	SMART	SM00382	AAA_5
344	488	InterPro	IPR003593	AAA+ ATPase domain
576	781	Gene3D	G3DSA:3.30.230.10	-
576	781	InterPro	IPR014721	Ribosomal protein S5 domain 2-type fold, subgroup
7	767	Hamap	MF_01973	Lon protease [lon].
7	767	InterPro	IPR027543	Lon protease, bacterial
778	798	MobiDBLite	mobidb-lite	consensus disorder prediction
8	773	PANTHER	PTHR10046	ATP DEPENDENT LON PROTEASE FAMILY MEMBER
8	773	InterPro	IPR027065	Lon protease
6	197	Pfam	PF02190	ATP-dependent protease La (LON) substrate-binding domain
6	197	InterPro	IPR003111	Lon protease, N-terminal domain
698	717	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
590	606	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
721	739	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
352	371	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
668	687	PRINTS	PR00830	Endopeptidase La (Lon) serine protease (S16) signature
248	296	Gene3D	G3DSA:1.20.5.5270	-
1	114	FunFam	G3DSA:2.30.130.40:FF:000001	Lon protease
116	241	FunFam	G3DSA:1.20.58.1480:FF:000001	Lon protease
309	581	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
309	581	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
580	767	FunFam	G3DSA:3.30.230.10:FF:000010	Lon protease
587	768	ProSiteProfiles	PS51786	Lon proteolytic domain profile.
587	768	InterPro	IPR008269	Peptidase S16, Lon proteolytic domain
248	297	FunFam	G3DSA:1.20.5.5270:FF:000002	Lon protease homolog
6	197	SUPERFAMILY	SSF88697	PUA domain-like
6	197	InterPro	IPR015947	PUA-like superfamily
309	486	FunFam	G3DSA:3.40.50.300:FF:000021	Lon protease homolog
310	486	Gene3D	G3DSA:3.40.50.300	-
310	486	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase

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 + 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 PA1803	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				0.482
4				0.223

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.

76 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
4KZ	4YPL	A0A059VAZ3	418.3 Da LogP 0.56 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](Cc1ccccc1)NC(=O)[C@H](Cc2ccccc2)NC(=O)c…`
AGS	6WQH	A0A059VAZ3	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BO2	6X27	P36776	384.2 Da LogP 0.36 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)c2cn…`
CIX	4FWH	C9DRU9	491.4 Da LogP 2.40 TPSA 137.0	✓ Ro5	✓ Clean	`B([C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C…`
PE4	3K1J	B6YU74	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
PE8	3K1J	B6YU74	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCCOCCO)O`
SLA	4FWG	C9DRU9	215.2 Da LogP -0.93 TPSA 86.6	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H]([C@@](NC1=O)(C=O)[C@H](C(C)C)O)O`
UFY	6WZV	P36776	384.2 Da LogP 0.36 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](CC(C)C)NC(=O)[C@@H](Cc1ccccc1)NC(=O)c2c…`

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
UKS	P36776	7.77	398.3 Da LogP 0.89 TPSA 124.4	✓ Ro5	✓ Clean	`B([C@H](CCCc1ccccc1)NC(=O)[C@@H](CCC)NC(=O)c2cn…`
CHEMBL4856865	P36776	7.75	446.3 Da LogP 1.34 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](CCCc1ccccc1)B…`
CHEMBL4864108	P36776	7.47	432.3 Da LogP 0.95 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](CCc1ccccc1)B(…`
CHEMBL4877126	P36776	7.42	336.2 Da LogP 0.06 TPSA 124.4	✓ Ro5	✓ Clean	`CCCC[C@H](NC(=O)[C@@H](CCC)NC(=O)c1cnccn1)B(O)O`
CHEMBL4870013	P36776	7.23	415.3 Da LogP 1.71 TPSA 124.7	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1oc(C)nc1C)C(=O)N[C@@H](CCCc1c…`
CHEMBL4862424	P36776	7.19	412.3 Da LogP 1.14 TPSA 124.4	✓ Ro5	✓ Clean	`CC(C)CCC[C@H](NC(=O)[C@@H](Cc1ccccc1)NC(=O)c1cn…`
CHEMBL4870902	P36776	7.11	477.2 Da LogP 1.27 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](CCCCCBr)B(O)O…`
CHEMBL4850612	P36776	7.04	424.3 Da LogP 1.28 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](CC1CCCCC1)B(O…`
CHEMBL4876920	P36776	7.04	384.2 Da LogP 0.50 TPSA 124.4	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CCc1ccccc…`
CHEMBL4856768	P36776	7.03	350.2 Da LogP 0.31 TPSA 124.4	✓ Ro5	✓ Clean	`CCCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CC(C)C)B…`
CHEMBL4847335	P36776	6.96	418.3 Da LogP 0.56 TPSA 124.4	✓ Ro5	✓ Clean	`O=C(N[C@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)B(O…`
CHEMBL4863384	P36776	6.87	376.3 Da LogP 0.84 TPSA 124.4	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CC1CCCCC1…`
CHEMBL4847763	P36776	6.86	390.3 Da LogP 1.09 TPSA 124.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](CC1CCCCC1)NC(=O)c1cncc…`
CHEMBL4861871	P36776	6.73	336.2 Da LogP -0.08 TPSA 124.4	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CC(C)C)B(…`
CHEMBL4853599	P36776	6.39	322.2 Da LogP -0.47 TPSA 124.4	✓ Ro5	✓ Clean	`CC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](CC(C)C)B(O…`
CHEMBL4864045	P36776	6.36	308.1 Da LogP -0.86 TPSA 124.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@@H](C)NC(=O)c1cnccn1)B(O)O`
CHEMBL4859172	P36776	6.26	336.2 Da LogP -0.23 TPSA 124.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](NC(=O)c1cnccn1)C(C)C)B(…`
CHEMBL4850826	P36776	6.25	370.2 Da LogP 0.11 TPSA 124.4	✓ Ro5	✓ Clean	`CCC[C@@H](NC(=O)c1cnccn1)C(=O)N[C@@H](Cc1ccccc1…`

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
ZINC12501520	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5650743	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC12360002	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.782	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	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.763	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	0.763	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	0.763	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	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833	0.750	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	0.750	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	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423	0.738	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC31516918	0.730	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC105469665	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`

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.