Protein target profile

KP13_03192

Periplasmic beta-glucosidase

Genome: KpKP13 Gene: bglX AHE43595.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GQV7

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Length 755

Pocket druggability 0.535

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 5 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

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: No hit
Gut microbiome similarity: 1.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: Periplasmic

Structure confidence

ColabFold pLDDT: 97.12 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 0.535

Structure A0A0H3GQV7

Pocket Pocket 2

P2Rank 0.677

Structure A0A0H3GQV7

Pocket Pocket 1

ColabFold model

FPocket 0.422 · Pocket 24

P2Rank 0.829 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 88 / 4744 genomes with a hit

Prevalence 1.9%

Cross-references

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

Sequence

UniProt A0A0H3GQV7

Chemistry

ChEMBL IFM

Sequence

Primary amino-acid sequence viewer.

MSLALQPALADELFGNHPLTPQARDAFVTDLLKKMTVDEKIGQLRLISVGPDNPKEAIREMIKNGQVGAIFNTVTRPDIRVMQDQVMQLSRLKIPLFFAYDVLHGQRTVFPISLGLASSFNLDAVKTVGRVSAYEAADDGLNMTWAPMVDVSRDPRWGRASEGFGEDTYLTTMMGQAMVESMQGKSPADRYSVMTSVKHFAAYGAVEGGKEYNTVDMSPQRLFNDYMPPYKAGLDAGSGAVMVALNSLNGTPATSDSWLLKDVLRDQWGFKGITVSDHGAIKELIKHGVASDPEDAVRVALKSGINMSMSDEYYSKYLPGLVKSGKVTMAELDDATRHVLNVKYDMGLFNDPYSHLGPKDSDPQDTNAESRLHRKEAREVARESLVLLKNRLDTLPLKKSGTIAVVGALADSKRDMMGSWSAAGVADQSVTVLTGIKEALGDNGKVIYAKGANVTDDKGIVDFLNLYENAVQVDPRSPQEMIDEAVAAAKQSDVVVAVVGEAQGMAHEASSRTDITLPQSQRNLIAALKATGKPLVLVLMNGRPLALVKEDQQADALLETWFAGTEGGHAIADVLFGDYNPSGKLPMSFPRSVGQIPTYYSHLNTGRPYNPEKPNKYTSRYFDEANGPLYPFGYGLSYTTFSVSDVNMSSATMPRDGSVTASVQVTNTGNREGATVIQLYLQDVTASMSRPVKMLRGFKKVTLKPGETQTVSFPIDVDALKFWNQQMKYVAEPGKFNVFIGVDSARVKQSEFELL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

3.2.1.21

Gene Ontology (GO)

GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0004553 Catalysis of the hydrolysis of any O-glycosyl bond.
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:0008422 Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
GO:0009251 The chemical reactions and pathways resulting in the breakdown of glucans, polysaccharides consisting only of glucose residues.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
22	638	PANTHER	PTHR30620	PERIPLASMIC BETA-GLUCOSIDASE-RELATED
23	384	SUPERFAMILY	SSF51445	(Trans)glycosidases
23	384	InterPro	IPR017853	Glycoside hydrolase superfamily
36	342	Pfam	PF00933	Glycosyl hydrolase family 3 N terminal domain
36	342	InterPro	IPR001764	Glycoside hydrolase, family 3, N-terminal
110	129	PRINTS	PR00133	Glycosyl hydrolase family 3 signature
110	129	InterPro	IPR001764	Glycoside hydrolase, family 3, N-terminal
156	172	PRINTS	PR00133	Glycosyl hydrolase family 3 signature
156	172	InterPro	IPR001764	Glycoside hydrolase, family 3, N-terminal
193	209	PRINTS	PR00133	Glycosyl hydrolase family 3 signature
193	209	InterPro	IPR001764	Glycoside hydrolase, family 3, N-terminal
263	281	PRINTS	PR00133	Glycosyl hydrolase family 3 signature
263	281	InterPro	IPR001764	Glycoside hydrolase, family 3, N-terminal
91	107	PRINTS	PR00133	Glycosyl hydrolase family 3 signature
91	107	InterPro	IPR001764	Glycoside hydrolase, family 3, N-terminal
263	280	ProSitePatterns	PS00775	Glycosyl hydrolases family 3 active site.
263	280	InterPro	IPR019800	Glycoside hydrolase, family 3, active site
20	362	FunFam	G3DSA:3.20.20.300:FF:000005	Periplasmic beta-glucosidase
675	744	SMART	SM01217	Fn3_like_2
675	744	InterPro	IPR026891	Fibronectin type III-like domain
371	638	FunFam	G3DSA:3.40.50.1700:FF:000004	Periplasmic beta-glucosidase
19	362	Gene3D	G3DSA:3.20.20.300	-
19	362	InterPro	IPR036962	Glycoside hydrolase, family 3, N-terminal domain superfamily
639	754	Gene3D	G3DSA:2.60.40.10	Immunoglobulins
639	754	InterPro	IPR013783	Immunoglobulin-like fold
371	638	Gene3D	G3DSA:3.40.50.1700	-
371	638	InterPro	IPR036881	Glycoside hydrolase family 3 C-terminal domain superfamily
385	638	Pfam	PF01915	Glycosyl hydrolase family 3 C-terminal domain
385	638	InterPro	IPR002772	Glycoside hydrolase family 3 C-terminal domain
676	743	Pfam	PF14310	Fibronectin type III-like domain
676	743	InterPro	IPR026891	Fibronectin type III-like domain
385	641	SUPERFAMILY	SSF52279	Beta-D-glucan exohydrolase, C-terminal domain
385	641	InterPro	IPR036881	Glycoside hydrolase family 3 C-terminal domain superfamily
640	755	FunFam	G3DSA:2.60.40.10:FF:000495	Periplasmic beta-glucosidase

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.

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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 #2

0.535

Likely same site as P2Rank 1 3.1 Å 16 shared residues 80% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #14

0.36

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Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.677

Likely same site as FPocket 2 3.1 Å 16 shared residues 80% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.548

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Surrounding area

Site 3 P2Rank #3

0.526

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Surrounding area

Site 4 P2Rank #4

0.224

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Surrounding area

Site 5 P2Rank #5

0.158

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Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.829

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Surrounding area

Site 2 P2Rank #2

0.775

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Surrounding area

Site 3 P2Rank #3

0.453

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Surrounding area

Site 4 P2Rank #4

0.286

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Surrounding area

Site 5 P2Rank #5

0.218

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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_A0A0H3GQV7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03192	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.

55 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

6BV PDB via homolog 358.4 Da · LogP -4.68 · TPSA 180.3 Open detail RCSB PDB

DTT PDB via homolog Detail RCSB PDB

LAM PDB via homolog Detail RCSB PDB

NOJ PDB via homolog Detail RCSB PDB

IFM ChEMBL via homolog · pchembl 8.15 (~7.1 nM) Detail ChEMBL

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
6BV RCSB PDB	6LC5	Q9XEI3	358.4 Da LogP -4.68 TPSA 180.3	2 viol.	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)S[C@H…`
DTT RCSB PDB	5Z87	A0A0H0XV02	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
LAM RCSB PDB	6JGN	Q9XEI3	641.6 Da LogP -4.86 TPSA 291.6	3 viol.	✓ Clean	`c1cc(ccc1[N+](=O)[O-])OC2C(C(C(C(O2)CO)O)O[C@H]…`
NOJ RCSB PDB	6R5N	Q9I311	163.2 Da LogP -2.97 TPSA 93.0	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]([C@@H]([C@H](N1)CO)O)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
IFM ChEMBL	P27034	8.15 ~7.1 nM	147.2 Da LogP -2.08 TPSA 72.7	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]([C@@H](CN1)O)O)CO`

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
ZINC22065001 ZINC	0.782	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@@H](O)[C@…`
ZINC77311812 ZINC	0.782	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@@H](O)[C@…`
ZINC77311821 ZINC	0.782	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O)[C…`
ZINC13531965 ZINC	0.714	358.4 Da LogP -4.68 TPSA 180.3	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](S[C@@H]2O[C@H](CO)[C@H](O)[C@H]…`
ZINC248005832 ZINC	0.714	358.4 Da LogP -4.68 TPSA 180.3	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](S[C@@H]2O[C@H](CO)[C@H](O)[C@H]…`
ZINC248005837 ZINC	0.714	358.4 Da LogP -4.68 TPSA 180.3	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](S[C@@H]2O[C@H](CO)[C@H](O)[C@H]…`
ZINC248005841 ZINC	0.714	358.4 Da LogP -4.68 TPSA 180.3	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](S[C@@H]2O[C@H](CO)[C@H](O)[C@H]…`
ZINC26184038 ZINC	0.714	358.4 Da LogP -4.68 TPSA 180.3	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](S[C@H]2O[C@H](CO)[C@H](O)[C@H](…`
ZINC5273968 ZINC	0.714	358.4 Da LogP -4.68 TPSA 180.3	2 viol.	✓ Clean	`OC[C@@H]1O[C@H](S[C@@H]2O[C@H](CO)[C@H](O)[C@H]…`
ZINC1857777631 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@H](O[C@@H…`
ZINC1857777632 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@H](O[C@@H…`
ZINC1857777633 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@H](O[C@@H…`
ZINC1857777634 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@H](O[C@@H…`
ZINC1857789176 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O[C@@…`
ZINC1857789177 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O[C@H…`
ZINC1911531502 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O[C@H…`
ZINC238809660 ZINC	0.690	949.8 Da LogP -9.93 TPSA 459.1	3 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O[C@…`
ZINC238809661 ZINC	0.690	949.8 Da LogP -9.93 TPSA 459.1	3 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O[C@…`
ZINC253497560 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O[C@@…`
ZINC253497561 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O[C@@…`
ZINC253497562 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O[C@@…`
ZINC253497563 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O[C@@…`
ZINC27647331 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O[C@…`
ZINC4282193 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@@H](O[C@H…`
ZINC44021709 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O[C@…`
ZINC76945115 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O[C@@…`
ZINC85603684 ZINC	0.690	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O[C@…`
ZINC22064965 ZINC	0.672	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@@H](O)[C@…`
ZINC87528054 ZINC	0.672	463.4 Da LogP -3.40 TPSA 221.7	2 viol.	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O)[C…`
ZINC1070097 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@@H](CO)[C@@H](O)[…`
ZINC12359987 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@H](O)[C@…`
ZINC12359988 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@H](O)[C@@…`
ZINC134307 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O)[C@…`
ZINC134310 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@@H](O)[C…`
ZINC134325 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@@H](CO)[C@H](O)[C…`
ZINC156947 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@@H](CO)[C@@H](O)[…`
ZINC2539731 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@H](O)[C@…`
ZINC3956718 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@H](O)[C@…`
ZINC4028812 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O)[C…`
ZINC4282153 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@@H](O)[C@…`
ZINC4282228 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@@H](O)[C@…`
ZINC4282287 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@H](O)[C@H…`
ZINC44963928 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@H](O)[C@H…`
ZINC4521725 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@@H](CO)[C@@H](O)[C…`
ZINC5227213 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@@H](CO)[C@@H](O)[…`
ZINC5227791 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@H]2O[C@H](CO)[C@H](O)[C@@…`
ZINC5842327 ZINC	0.655	301.3 Da LogP -1.23 TPSA 142.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@@H](O)[C…`
ZINC13550858 ZINC	0.636	271.2 Da LogP -0.59 TPSA 122.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@H](O)[C@…`
ZINC242464073 ZINC	0.636	271.2 Da LogP -0.59 TPSA 122.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@H](CO)[C@H](O)[C@…`
ZINC6093332 ZINC	0.636	271.2 Da LogP -0.59 TPSA 122.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O[C@@H]2O[C@@H](CO)[C@H](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.