Protein target profile

KP13_00143

Alpha-xylosidase

Genome: KpKP13 Gene: AHE42063.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GXH3

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Length 772

Pocket druggability 0.212

Direct ligand evidence 0 62 total records

Functional annotation 1 EC 5 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

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

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.63. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 10 structural and 2 bioactivity records.

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 (%): 29.535 Lower values reduce human off-target concern.
Human E-value: 4.82e-41
Gut microbiome similarity: 5.9% 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: Unknown

Structure confidence

ColabFold pLDDT: 97.96 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 0.212

Structure A0A0H3GXH3

Pocket Pocket 19

P2Rank 0.634

Structure A0A0H3GXH3

Pocket Pocket 1

ColabFold model

FPocket 0.179 · Pocket 21

P2Rank 0.586 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 280 / 4744 genomes with a hit

Prevalence 5.9%

Cross-references

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

Sequence

UniProt A0A0H3GXH3

Chemistry

ChEMBL CHEMBL408500 ChEMBL CHEMBL179130

Sequence

Primary amino-acid sequence viewer.

MKISDGNWLIQPGLNLIQPVQVYEVEQQGNEMVVYAAPRDVRERAWQLDTPLFTLRFFSPQEGIIGVRMEHFQGALDNGPHYPLNVQKDVHVEIENTAGFAELKSGSLSVRVTKGEFWALDFLRDGLRITGSQLKNNGYVQDSKTQRNYMFERLDLGVGETVYGLGERFTALVRNGQTVETWNEDGGTSTEQSYKNIPFYLTNRGYGVLVNHPQRVSFEVGSEKVSKVQFSVEGEYLEYFVIDGPTPKAVLNRYTQFTGRPALPPAWSFGLWLTTSFTTNYDEATVNSFIDGMAERHLPLHVFHFDCFWMKAFQWCDFEWDPQTFPDPEGMIKRLKAKGLKVCVWINPYIGQRSPVFKELKEKGYLLKRPDGSLWQWDKWQPGLAIYDFTNPEACQWYADKLKGLVAMGVDCFKTDFGERIPTDVQWFDGSDPQKMHNHYAFIYNELVWKVLKETVGEQEAVLFARSASVGAQQFPVHWGGDCYANYESMAESLRGGLSIGMSGFGFWSHDIGGFENTAPAHVYKRWCAFGLLSSHSRLHGSKSYRVPWAYDDESCDVVRHFTQLKCRMMPYLYRQAALANECGTPMLRAMLLEFPDDPACDYLDRQYMLGDSVLVAPVFSEAGEVQFYLPEGRWTHLWHNDELPGSRWHKQHHDALSLPVYVRDNSLLALGNNDQKPDYAWHEGTAFQLFHLEDGREARCDVPAADGSTIFTLKARRQGNAIAVSGEGEARGWTLCLRNIPQVAGVQGGTQTGSEWGVVVSAEGNTLTITL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

3.2.1.177

Gene Ontology (GO)

GO:0030246 Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
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:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0061634 Catalysis of the hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
263	603	SUPERFAMILY	SSF51445	(Trans)glycosidases
263	603	InterPro	IPR017853	Glycoside hydrolase superfamily
259	569	CDD	cd06593	GH31_xylosidase_YicI
666	772	SUPERFAMILY	SSF117125	Putative glucosidase YicI, C-terminal domain
617	664	Gene3D	G3DSA:2.60.40.1180	-
617	664	InterPro	IPR013780	Glycosyl hydrolase, all-beta
240	668	Pfam	PF01055	Glycosyl hydrolases family 31
240	668	InterPro	IPR000322	Glycoside hydrolase family 31
1	247	SUPERFAMILY	SSF74650	Galactose mutarotase-like
1	247	InterPro	IPR011013	Galactose mutarotase-like domain superfamily
28	664	PANTHER	PTHR43053	GLYCOSIDASE FAMILY 31
665	772	Gene3D	G3DSA:2.60.40.1180	-
665	772	InterPro	IPR013780	Glycosyl hydrolase, all-beta
246	616	FunFam	G3DSA:3.20.20.80:FF:000053	Alpha-xylosidase YicI
1	245	Gene3D	G3DSA:2.60.40.1760	glycosyl hydrolase (family 31)
586	665	SUPERFAMILY	SSF51011	Glycosyl hydrolase domain
150	259	CDD	cd14752	GH31_N
159	218	Pfam	PF13802	Galactose mutarotase-like
159	218	InterPro	IPR025887	Glycoside hydrolase family 31, N-terminal domain
246	616	Gene3D	G3DSA:3.20.20.80	Glycosidases

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 #19

0.212

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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

0.634

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Surrounding area

Site 2 P2Rank #2

0.275

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Surrounding area

Site 3 P2Rank #3

0.193

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Surrounding area

Site 4 P2Rank #4

0.082

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Surrounding area

Site 5 P2Rank #5

0.073

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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

0.586

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Surrounding area

Site 2 P2Rank #2

0.167

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Surrounding area

Site 3 P2Rank #3

0.12

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Surrounding area

Site 4 P2Rank #4

0.09

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Surrounding area

Site 5 P2Rank #5

0.082

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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_A0A0H3GXH3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00143	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.

62 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5GF PDB via homolog 198.1 Da · LogP -2.92 · TPSA 110.4 Open detail RCSB PDB

66U PDB via homolog Detail RCSB PDB

66V PDB via homolog Detail RCSB PDB

93Z PDB via homolog Detail RCSB PDB

948 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
5GF RCSB PDB	4BA0	B3PEE6	198.1 Da LogP -2.92 TPSA 110.4	✓ Ro5	✓ Clean	`C([C@@]1([C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)F…`
66U RCSB PDB	5I24	B3PEE6	193.2 Da LogP -3.62 TPSA 127.2	1 viol.	✓ Clean	`C([C@H]1[C@@H]([C@H]([C@@H]([C@H]([C@@H]1O)O)O)…`
66V RCSB PDB	5I23	B3PEE6	347.4 Da LogP -1.10 TPSA 163.5	1 viol.	Alert	`C(CCCCN=[N+]=N)CCCN[C@H]1[C@@H]([C@H]([C@@H]([C…`
93Z RCSB PDB	5NPB	B3PEE6	274.2 Da LogP -3.76 TPSA 164.8	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@H](C([C@H]1OS(=O)(=O)O…`
948 RCSB PDB	5NPE	B3PEE6	175.2 Da LogP -2.97 TPSA 102.9	✓ Ro5	✓ Clean	`C([C@H]1[C@@H]2[C@@H](N2)[C@@H]([C@H]([C@@H]1O)…`
94B RCSB PDB	5NPD	B3PEE6	175.2 Da LogP -2.97 TPSA 102.9	✓ Ro5	✓ Clean	`C([C@H]1[C@H]2[C@H](N2)[C@@H]([C@H]([C@@H]1O)O)…`
94E RCSB PDB	5NPC	B3PEE6	256.2 Da LogP -3.28 TPSA 133.5	✓ Ro5	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@H]([C@@H]2[C@H]1OS(=O)…`
9VH RCSB PDB	6PNR	C4ZGB7	211.2 Da LogP -2.18 TPSA 106.9	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]([C@@H](CN1)O)O)CS(=O)(=O)O`
OXL RCSB PDB	5NPB	B3PEE6	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`
XTG RCSB PDB	2F2H	P31434	449.4 Da LogP -2.05 TPSA 192.2	2 viol.	✓ Clean	`c1cc(ccc1[N+](=O)[O-])O[C@H]2[C@@H]([C@H]([C@@H…`

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
CHEMBL408500 ChEMBL	Q653V4	7.28 ~52.5 nM	289.4 Da LogP 0.50 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCCCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
CHEMBL179130 ChEMBL	Q653V4	7.10 ~79.4 nM	163.2 Da LogP -2.97 TPSA 93.0	✓ Ro5	✓ Clean	`OC[C@@H]1NC[C@@H](O)[C@@H](O)[C@H]1O`

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
ZINC14253608 ZINC	1.000	289.4 Da LogP 0.50 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCCCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
ZINC1552264 ZINC	1.000	289.4 Da LogP 0.50 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCCCCCCN1C[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1CO`
ZINC44351037 ZINC	1.000	331.5 Da LogP 1.67 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
ZINC3979739 ZINC	0.967	233.3 Da LogP -1.06 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@@H]1CO`
ZINC11681341 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@H](O)[C@@H](O)[C@@H](O)[C@@H]1CO`
ZINC13545227 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
ZINC13719785 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@H](O)[C@@H](O)[C@@H](O)[C@H]1CO`
ZINC1550969 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1CO`
ZINC2387141 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@H](O)[C@H](O)[C@@H](O)[C@@H]1CO`
ZINC36533584 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@H](O)[C@H](O)[C@H](O)[C@H]1CO`
ZINC3794711 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
ZINC3957104 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@@H]1CO`
ZINC71789999 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@H](O)[C@H](O)[C@@H](O)[C@H]1CO`
ZINC8627075 ZINC	0.871	219.3 Da LogP -1.45 TPSA 84.2	✓ Ro5	✓ Clean	`CCCCN1C[C@H](O)[C@H](O)[C@H](O)[C@@H]1CO`
ZINC3825455 ZINC	0.757	305.4 Da LogP -0.27 TPSA 93.4	✓ Ro5	✓ Clean	`CCCOCCCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
ZINC253683038 ZINC	0.750	205.3 Da LogP -1.84 TPSA 84.2	✓ Ro5	✓ Clean	`CCCN1C[C@H](O)[C@H](O)[C@@H](O)[C@@H]1CO`
ZINC253683042 ZINC	0.750	205.3 Da LogP -1.84 TPSA 84.2	✓ Ro5	✓ Clean	`CCCN1C[C@H](O)[C@H](O)[C@H](O)[C@H]1CO`
ZINC253683044 ZINC	0.750	205.3 Da LogP -1.84 TPSA 84.2	✓ Ro5	✓ Clean	`CCCN1C[C@H](O)[C@H](O)[C@@H](O)[C@H]1CO`
ZINC34383558 ZINC	0.750	205.3 Da LogP -1.84 TPSA 84.2	✓ Ro5	✓ Clean	`CCCN1C[C@H](O)[C@H](O)[C@H](O)[C@@H]1CO`
ZINC137899614 ZINC	0.722	319.4 Da LogP 0.12 TPSA 93.4	✓ Ro5	✓ Clean	`COCCCCCCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
ZINC44960154 ZINC	0.714	346.5 Da LogP 0.61 TPSA 110.2	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@@H]…`
ZINC44960155 ZINC	0.714	346.5 Da LogP 0.61 TPSA 110.2	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCN1C[C@@H](O)[C@@H](O)[C@H](O)[C@@H…`
ZINC44960156 ZINC	0.714	346.5 Da LogP 0.61 TPSA 110.2	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1…`
ZINC44960157 ZINC	0.714	346.5 Da LogP 0.61 TPSA 110.2	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCN1C[C@@H](O)[C@@H](O)[C@H](O)[C@H]…`
ZINC95553643 ZINC	0.692	333.5 Da LogP 0.25 TPSA 104.4	✓ Ro5	✓ Clean	`CCC(O)(CC)CCCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC22054059 ZINC	0.676	277.3 Da LogP -1.61 TPSA 121.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCN1C[C@H](O)[C@H](O)[C@H](O)[C@H]1CO`
ZINC5157115 ZINC	0.676	277.3 Da LogP -1.61 TPSA 121.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
ZINC6562433 ZINC	0.676	277.3 Da LogP -1.61 TPSA 121.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCN1C[C@H](O)[C@H](O)[C@H](O)[C@@H]1CO`
ZINC6562434 ZINC	0.676	277.3 Da LogP -1.61 TPSA 121.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@@H]1CO`
ZINC1070097 ZINC	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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	0.647	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…`
ZINC141935332 ZINC	0.636	207.2 Da LogP -3.26 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN1C[C@H](O)[C@H](O)[C@@H](O)[C@H]1CO`
ZINC4097426 ZINC	0.636	207.2 Da LogP -3.26 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN1C[C@H](O)[C@@H](O)[C@H](O)[C@H]1CO`
ZINC897171 ZINC	0.636	207.2 Da LogP -3.26 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN1C[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1CO`

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.