Protein target profile

KP13_01731

Ubiquinone/menaquinone biosynthesis methyltransferase ubiE

Genome: KpKP13 Gene: AHE46966.1 ubiE 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GLM9

Export view

Length 251

Pocket druggability 0.988

Direct ligand evidence 0 58 total records

Functional annotation 2 EC 6 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.99, P2Rank 0.98). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.99. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.98. Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 56.0 Lower values reduce human off-target concern.
Human E-value: 9.14e-11
Gut microbiome similarity: 5.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.032 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 91.25 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.988

Structure A0A0H3GLM9

Pocket Pocket 1

P2Rank 0.976

Structure A0A0H3GLM9

Pocket Pocket 1

ColabFold model

FPocket 0.986 · Pocket 1

P2Rank 0.948 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 241 / 4744 genomes with a hit

Prevalence 5.1%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GLM9

Sequence

Primary amino-acid sequence viewer.

MVEDSQETTHFGFQTVAKEQKADMVAHVFHSVAAKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRLVGETGRVMLADINDSMLKMGREKLRNIGIVGNVEYVQANAEALPFADNTFDCITISFGLRNVTDKEKALRSMYRVLKPGGRLLVLEFSKPILEPLSKAYDAYSFHILPKVGELVAKDGDSYRYLAESIRMHPDQETLKGMMQDAGFENVDYYNLTAGIVALHRGYKF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 6 GO

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
GO:0008425 Catalysis of the reaction: a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + S-adenosyl-L-homocysteine + H+.
GO:0043770 Catalysis of the reaction: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H+ + S-adenosyl-L-homocysteine. Reaction substrates can have varying polyprenyl side chain length.
GO:0009060 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which requires oxygen as the terminal electron acceptor.
GO:0009234 The chemical reactions and pathways resulting in the formation of any of the menaquinones. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones that have vitamin K activity and are known as vitamin K2.
GO:0032259 The process in which a methyl group is covalently attached to a molecule.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
36	51	ProSitePatterns	PS01183	ubiE/COQ5 methyltransferase family signature 1.
36	51	InterPro	IPR023576	UbiE/COQ5 methyltransferase, conserved site
27	233	PANTHER	PTHR43591	METHYLTRANSFERASE
25	250	NCBIfam	TIGR01934	ubiquinone/menaquinone biosynthesis methyltransferase
25	250	InterPro	IPR004033	UbiE/COQ5 methyltransferase
18	249	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
18	249	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
31	251	FunFam	G3DSA:3.40.50.150:FF:000014	Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE
16	250	Hamap	MF_01813	Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE [ubiE].
16	250	InterPro	IPR004033	UbiE/COQ5 methyltransferase
20	250	ProSiteProfiles	PS51608	UbiE family SAM-binding methyltransferase profile.
20	250	InterPro	IPR004033	UbiE/COQ5 methyltransferase
31	251	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
31	251	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
15	250	Pfam	PF01209	ubiE/COQ5 methyltransferase family
66	168	CDD	cd02440	AdoMet_MTases
158	172	ProSitePatterns	PS01184	ubiE/COQ5 methyltransferase family signature 2.
158	172	InterPro	IPR023576	UbiE/COQ5 methyltransferase, conserved site

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.988

Likely same site as P2Rank 1 4.9 Å 28 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #2

0.978

Show in viewer

Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.976

Likely same site as FPocket 1 4.9 Å 28 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.113

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:123-124

UniProt: Binding site:140-140

UniProt: Binding site:74-74

UniProt: Binding site:95-95

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.986

Likely same site as P2Rank 2 1.2 Å 25 shared residues 96% of smaller site

Show in viewer

Surrounding area

Site 2 FPocket #2

0.752

Likely same site as P2Rank 1 5.6 Å 15 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 3 FPocket #6

0.64

Likely same site as P2Rank 1 4.5 Å 14 shared residues 100% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.948

Likely same site as FPocket 6 4.5 Å 14 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.874

Likely same site as FPocket 1 1.2 Å 25 shared residues 96% of smaller site

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.15

Show in viewer

Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GLM9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01731	ColabFold	—	—	full sequence	—	Loaded

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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ARS PDB via homolog 74.9 Da · LogP -0.38 · TPSA 0.0 Open detail RCSB PDB

BY9 PDB via homolog Detail RCSB PDB

DTT PDB via homolog Detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

PA0 PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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
ARS RCSB PDB	4FSD	C0JV69	74.9 Da LogP -0.38 TPSA 0.0	✓ Ro5	✓ Clean	`[As]`
BY9 RCSB PDB	6UV6	Q0H2W9	487.5 Da LogP 1.29 TPSA 157.0	1 viol.	✓ Clean	`c1ccc2c(c1)c3c4c(c5c6ccccc6n(c5c3[nH]2)[C@H]7[C…`
DTT RCSB PDB	4RSR	C0JV69	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
MLI RCSB PDB	4PNE	Q9ALM7	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
PA0 RCSB PDB	4KW7	C0JV69	168.0 Da LogP 0.36 TPSA 17.1	✓ Ro5	✓ Clean	`c1ccc(cc1)[As]=O`
PC RCSB PDB	5WP4	Q9FR44	184.2 Da LogP -0.20 TPSA 66.8	✓ Ro5	✓ Clean	`C[N+](C)(C)CCOP(=O)(O)O`
RXO RCSB PDB	4RSR	C0JV69	215.0 Da LogP -0.44 TPSA 63.4	✓ Ro5	✓ Clean	`c1cc(c(cc1[AsH2])[N+](=O)[O-])O`
TEX RCSB PDB	5GM2	A0A077K7L1	437.6 Da LogP 4.85 TPSA 68.4	✓ Ro5	Alert	`CC(C)[C@H]1C(=O)N[C@@H](Cc2c[nH]c3c2c(ccc3[C@](…`

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).

No ChEMBL hits found through similar proteins.

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
ZINC2383097 ZINC	1.000	437.6 Da LogP 4.85 TPSA 68.4	✓ Ro5	Alert	`C=C[C@](C)(CCC=C(C)C)c1ccc2c3c(c[nH]c13)C[C@@H]…`
ZINC31333229 ZINC	1.000	437.6 Da LogP 4.85 TPSA 68.4	✓ Ro5	Alert	`C=C[C@@](C)(CCC=C(C)C)c1ccc2c3c(c[nH]c13)C[C@@H…`
ZINC3873176 ZINC	1.000	437.6 Da LogP 4.85 TPSA 68.4	✓ Ro5	Alert	`C=C[C@](C)(CCC=C(C)C)c1ccc2c3c(c[nH]c13)C[C@@H]…`
ZINC3873177 ZINC	1.000	437.6 Da LogP 4.85 TPSA 68.4	✓ Ro5	Alert	`C=C[C@](C)(CCC=C(C)C)c1ccc2c3c(c[nH]c13)C[C@H](…`
ZINC3873178 ZINC	1.000	437.6 Da LogP 4.85 TPSA 68.4	✓ Ro5	Alert	`C=C[C@](C)(CCC=C(C)C)c1ccc2c3c(c[nH]c13)C[C@H](…`
ZINC104949681 ZINC	0.787	453.6 Da LogP 3.82 TPSA 88.6	✓ Ro5	Alert	`C=C[C@](C)(CC[C@H](O)C(=C)C)c1ccc2c3c(c[nH]c13)…`
ZINC104949684 ZINC	0.787	453.6 Da LogP 3.82 TPSA 88.6	✓ Ro5	Alert	`C=C[C@](C)(CC[C@H](O)C(=C)C)c1ccc2c3c(c[nH]c13)…`
ZINC104949689 ZINC	0.787	453.6 Da LogP 3.82 TPSA 88.6	✓ Ro5	Alert	`C=C[C@](C)(CC[C@H](O)C(=C)C)c1ccc2c3c(c[nH]c13)…`
ZINC104949693 ZINC	0.787	453.6 Da LogP 3.82 TPSA 88.6	✓ Ro5	Alert	`C=C[C@](C)(CC[C@H](O)C(=C)C)c1ccc2c3c(c[nH]c13)…`
ZINC94568720 ZINC	0.655	265.0 Da LogP 1.90 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(I)ccc1O`
ZINC36377933 ZINC	0.600	218.0 Da LogP 2.06 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(Br)ccc1O`
ZINC167149949 ZINC	0.586	457.5 Da LogP 2.67 TPSA 119.7	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](n2c3ccccc3c3c4c(c5c6ccccc6[nH]c5…`
ZINC248002323 ZINC	0.586	457.5 Da LogP 2.67 TPSA 119.7	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](n2c3ccccc3c3c4c(c5c6ccccc6[nH]c5…`
ZINC248002325 ZINC	0.586	457.5 Da LogP 2.67 TPSA 119.7	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](n2c3ccccc3c3c4c(c5c6ccccc6[nH]c5…`
ZINC38658661 ZINC	0.586	457.5 Da LogP 2.67 TPSA 119.7	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](n2c3ccccc3c3c4c(c5c6ccccc6[nH]c…`
ZINC83923135 ZINC	0.586	457.5 Da LogP 2.67 TPSA 119.7	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](n2c3ccccc3c3c4c(c5c6ccccc6[nH]c5…`
ZINC1651546 ZINC	0.581	304.2 Da LogP 2.15 TPSA 143.8	✓ Ro5	✓ Clean	`O=C(c1ccc(O)c([N+](=O)[O-])c1)c1ccc(O)c([N+](=O…`
ZINC1672250 ZINC	0.581	340.3 Da LogP 1.75 TPSA 160.9	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(S(=O)(=O)c2ccc(O)c([N+](=O)[O-…`
ZINC1696886 ZINC	0.581	290.2 Da LogP 2.51 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(Cc2ccc(O)c([N+](=O)[O-])c2)ccc…`
ZINC95482938 ZINC	0.577	200.1 Da LogP 0.91 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(O)c([N+](=O)[O-])cc1O`
ZINC2517049 ZINC	0.569	301.4 Da LogP 1.66 TPSA 68.4	✓ Ro5	✓ Clean	`CC(C)[C@H]1C(=O)N[C@H](CO)Cc2c[nH]c3cccc(c23)N1C`
ZINC57363 ZINC	0.569	301.4 Da LogP 1.66 TPSA 68.4	✓ Ro5	✓ Clean	`CC(C)[C@@H]1C(=O)N[C@@H](CO)Cc2c[nH]c3cccc(c23)…`
ZINC1651909 ZINC	0.563	219.2 Da LogP 0.55 TPSA 117.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(S(=O)(=O)O)ccc1O`
ZINC24718402 ZINC	0.563	231.2 Da LogP 2.67 TPSA 83.6	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(-c2ccc(O)cc2)ccc1O`
ZINC4174041 ZINC	0.563	218.2 Da LogP -0.05 TPSA 123.5	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(O)c([N+](=O)[O-])c1`
ZINC1850960 ZINC	0.556	200.1 Da LogP 0.91 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc([N+](=O)[O-])c(O)cc1O`
ZINC113027531 ZINC	0.548	310.4 Da LogP 3.58 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCO[P@](=O)(O)OCC[N+](C)(C)C`
ZINC1560408744 ZINC	0.548	257.2 Da LogP -0.28 TPSA 96.2	✓ Ro5	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(O)OC[C](O)CO`
ZINC217410460 ZINC	0.548	338.4 Da LogP 4.36 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[P@@](=O)(O)OCC[N+](C)(C)C`
ZINC3649862 ZINC	0.548	296.4 Da LogP 3.19 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCO[P@](=O)(O)OCC[N+](C)(C)C`
ZINC43562168 ZINC	0.548	352.5 Da LogP 4.75 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[P@@](=O)(O)OCC[N+](C)(C)C`
ZINC58660415 ZINC	0.548	324.4 Da LogP 3.97 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCO[P@@](=O)(O)OCC[N+](C)(C)C`
ZINC125976582 ZINC	0.545	203.2 Da LogP 0.88 TPSA 100.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc([S@@](=O)O)ccc1O`
ZINC156016 ZINC	0.545	207.1 Da LogP 2.32 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(C(F)(F)F)ccc1O`
ZINC1577071 ZINC	0.545	318.3 Da LogP 3.24 TPSA 126.7	✓ Ro5	✓ Clean	`CC(C)(c1ccc(O)c([N+](=O)[O-])c1)c1ccc(O)c([N+](…`
ZINC343430 ZINC	0.545	217.2 Da LogP 0.70 TPSA 97.5	✓ Ro5	✓ Clean	`CS(=O)(=O)c1ccc(O)c([N+](=O)[O-])c1`
ZINC35575724 ZINC	0.545	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(-c2ccccc2)ccc1O`
ZINC1700830 ZINC	0.541	294.3 Da LogP -1.70 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]…`
ZINC4990785 ZINC	0.541	294.3 Da LogP -1.70 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2…`
ZINC4990786 ZINC	0.541	294.3 Da LogP -1.70 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4990788 ZINC	0.541	294.3 Da LogP -1.70 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H…`
ZINC96031232 ZINC	0.531	353.5 Da LogP 3.30 TPSA 81.8	✓ Ro5	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)OCCCCCCCCCCCN`
ZINC37246177 ZINC	0.529	371.1 Da LogP 4.11 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(C(=C(Cl)Cl)c2ccc(O)c([N+](=O)[…`
ZINC34240224 ZINC	0.519	200.1 Da LogP 0.91 TPSA 126.7	✓ Ro5	Alert	`O=[N+]([O-])c1cc(O)c(O)cc1[N+](=O)[O-]`
ZINC21303651 ZINC	0.516	234.0 Da LogP 1.77 TPSA 83.6	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(Br)c(O)cc1O`
ZINC1532714 ZINC	0.515	258.2 Da LogP -0.82 TPSA 96.2	✓ Ro5	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)OC[C@H](O)CO`
ZINC1842903 ZINC	0.515	258.2 Da LogP -0.82 TPSA 96.2	✓ Ro5	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(O)OC[C@@H](O)CO`
ZINC1507325 ZINC	0.514	271.2 Da LogP 1.59 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(S(=O)(=O)C(F)(F)F)ccc1O`
ZINC21985628 ZINC	0.514	426.2 Da LogP 4.32 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cc(C(c2ccc(O)c([N+](=O)[O-])c2)(C…`
ZINC2562578 ZINC	0.514	231.2 Da LogP 1.09 TPSA 97.5	✓ Ro5	✓ Clean	`CCS(=O)(=O)c1ccc(O)c([N+](=O)[O-])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.