Protein target profile

VK055_3061

phosphoglucose isomerase family protein

Genome: KpATCC43816 Gene: AIK81646.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GGT9

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Length 549

Pocket druggability 0.764

Direct ligand evidence 0 61 total records

Functional annotation 1 EC 8 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 0.76, P2Rank 0.65). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.76. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.65. Structure available AlphaFold DB model + ColabFold model 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 (%): 70.241 Lower values reduce human off-target concern.
Human E-value: 0.0
Gut microbiome similarity: 17.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 96.175 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: 98.42 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 0.764

Structure A0A0H3GGT9

Pocket Pocket 2

P2Rank 0.648

Structure A0A0H3GGT9

Pocket Pocket 1

ColabFold model

FPocket 0.595 · Pocket 4

P2Rank 0.771 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 811 / 4744 genomes with a hit

Prevalence 17.1%

Cross-references

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

Sequence

UniProt A0A0H3GGT9

Chemistry

ChEMBL PAN ChEMBL CHEMBL4129274

Sequence

Primary amino-acid sequence viewer.

MKNINPTQTSAWQALQKHFDEMKDVTISELFAKDSDRFSKFSATFDDLMLVDFSKNRITEETLAKLQDLAKETDLAGAIKSMFSGEKINRTEDRAVLHVALRNRSNTPIVVDGKDVMPEVNAVLEKMKTFSEAIISGSWKGYTGKPITDVVNIGIGGSDLGPFMVTEALRPYKNHLNMHFVSNVDGTHIAEVLKNVNPETTLFLVASKTFTTQETMTNAHSARDWFLATAGDDKHVAKHFAALSTNAKAVGEFGIDTANMFEFWDWVGGRYSLWSAIGLSIILSVGFDNFVELLSGAHAMDKHFSTTPAEKNLPVLLALIGIWYNNFFGAETEAILPYDQYMHRFAAYFQQGNMESNGKYVDRNGHAVDYQTGPIIWGEPGTNGQHAFYQLIHQGTKMVPCDFIAPAITHNPLSDHHQKLLSNFFAQTEALAFGKSREVVEQEYRDQGKDPATLEHVVPFKVFEGNRPTNSILLREITPFSLGALIALYEHKIFTQGAILNIFTFDQWGVELGKQLANRILPELKDGSKVSSHDSSTNGLINRYKAWRA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

5.3.1.9

Gene Ontology (GO)

GO:0004347 Catalysis of the reaction: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate.
GO:0006094 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
GO:0097367 Binding to a carbohydrate derivative.
GO:1901135 The chemical reactions and pathways involving carbohydrate derivative.
GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0048029 Binding to a monosaccharide. Monosaccharides are the simplest carbohydrates; they are polyhydroxy aldehydes H[CH(OH)]nC(=O)H or polyhydroxy ketones H[CHOH]nC(=O)[CHOH]mH with three or more carbon atoms. They form the constitutional repeating units of oligo- and polysaccharides.
GO:0051156 The chemical reactions and pathways involving glucose 6-phosphate, a monophosphorylated derivative of glucose with the phosphate group attached to C-6.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

36 records

Show feature table

Start	End	DB	Term	Name
331	520	CDD	cd05016	SIS_PGI_2
331	520	InterPro	IPR035482	Phosphoglucose isomerase, SIS domain 2
9	547	ProSiteProfiles	PS51463	Glucose-6-phosphate isomerase family profile.
9	547	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
121	283	CDD	cd05015	SIS_PGI_1
121	283	InterPro	IPR035476	Phosphoglucose isomerase, SIS domain 1
52	541	Pfam	PF00342	Phosphoglucose isomerase
52	541	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
497	514	ProSitePatterns	PS00174	Phosphoglucose isomerase signature 2.
497	514	InterPro	IPR018189	Phosphoglucose isomerase, conserved site
507	549	Gene3D	G3DSA:1.10.1390.10	-
507	549	InterPro	IPR023096	Phosphoglucose isomerase, C-terminal
8	546	PANTHER	PTHR11469	GLUCOSE-6-PHOSPHATE ISOMERASE
8	546	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
98	291	Gene3D	G3DSA:3.40.50.10490	-
11	506	Gene3D	G3DSA:3.40.50.10490	-
507	549	FunFam	G3DSA:1.10.1390.10:FF:000001	Glucose-6-phosphate isomerase
338	359	PRINTS	PR00662	Glucose-6-phosphate isomerase signature
338	359	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
497	510	PRINTS	PR00662	Glucose-6-phosphate isomerase signature
497	510	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
483	497	PRINTS	PR00662	Glucose-6-phosphate isomerase signature
483	497	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
261	279	PRINTS	PR00662	Glucose-6-phosphate isomerase signature
261	279	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
150	169	PRINTS	PR00662	Glucose-6-phosphate isomerase signature
150	169	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
465	483	PRINTS	PR00662	Glucose-6-phosphate isomerase signature
465	483	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
46	524	Hamap	MF_00473	Glucose-6-phosphate isomerase [pgi].
46	524	InterPro	IPR001672	Phosphoglucose isomerase (PGI)
98	291	FunFam	G3DSA:3.40.50.10490:FF:000004	Glucose-6-phosphate isomerase
5	548	SUPERFAMILY	SSF53697	SIS domain
5	548	InterPro	IPR046348	SIS domain superfamily
265	278	ProSitePatterns	PS00765	Phosphoglucose isomerase signature 1.
265	278	InterPro	IPR018189	Phosphoglucose isomerase, 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.

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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

0.764

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Surrounding area

Site 2 FPocket #1

0.38

Likely same site as P2Rank 3 2.8 Å 15 shared residues 100% of smaller site

Unusual size

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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

0.648

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Surrounding area

Site 2 P2Rank #2

0.268

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Surrounding area

Site 3 P2Rank #3

0.176

Likely same site as FPocket 1 2.8 Å 15 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.081

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Surrounding area

Site 5 P2Rank #5

0.066

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Surrounding area

Residue sets

UniProt: Active site:355-355 Proton donor

UniProt: Active site:386-386

UniProt: Active site:514-514

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.771

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Surrounding area

Site 2 P2Rank #2

0.189

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Surrounding area

Site 3 P2Rank #3

0.161

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Surrounding area

Site 4 P2Rank #4

0.141

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Surrounding area

Site 5 P2Rank #5

0.07

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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_A0A0H3GGT9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3061	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.

61 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

6PG PDB via homolog 276.1 Da · LogP -3.38 · TPSA 185.0 Open detail RCSB PDB

A5P PDB via homolog Detail RCSB PDB

DER PDB via homolog Detail RCSB PDB

E4P PDB via homolog Detail RCSB PDB

G6Q 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
6PG RCSB PDB	1DQR	Q9N1E2	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H]([C@H](C(=O)O)O)O)O)O)OP(=O…`
A5P RCSB PDB	2CXP	P06745	232.1 Da LogP -2.83 TPSA 147.7	1 viol.	✓ Clean	`C([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)O`
DER RCSB PDB	2CXO	P06745	216.1 Da LogP -2.10 TPSA 144.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](C(=O)O)O)O)OP(=O)(O)O`
E4P RCSB PDB	1U0G	P06745	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`C([C@H]([C@H](C=O)O)O)OP(=O)(O)O`
G6Q RCSB PDB	2O2C	P13377	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H]([C@H](C=O)O)O)O)O)OP(=O)(O…`
O1B RCSB PDB	6XUH	P06744	288.2 Da LogP -3.75 TPSA 182.6	1 viol.	✓ Clean	`C(CNC(=O)[C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)N`
PA5 RCSB PDB	1G98	Q9N1E2	246.1 Da LogP -2.74 TPSA 164.8	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H](C(=O)O)O)O)O)OP(=O)(O)O`
PG6 RCSB PDB	6XUI	P06744	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
S6P RCSB PDB	2CXQ	P06745	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`C([C@@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)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
PAN ChEMBL	Q9N1E2	7.00 ~100.0 nM	261.1 Da LogP -3.32 TPSA 176.8	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H](C(=O)NO)O)O)O)OP(=O)(O)O`
CHEMBL4129274 ChEMBL	P06744	—	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
ZINC100033330 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC100067275 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC100889630 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC104861723 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O…`
ZINC12503760 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC12503763 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC1692489 ZINC	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC19850142 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC2508229 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4530388 ZINC	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC4545927 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)COP(=O)(…`
ZINC4545928 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O)(O…`
ZINC4545929 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)COP(=O)(O…`
ZINC5701172 ZINC	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC12501558 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(…`
ZINC12501560 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O…`
ZINC12501562 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)…`
ZINC12501564 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(…`
ZINC1530556 ZINC	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532623 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(…`
ZINC2047359 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)COP(=O…`
ZINC22116391 ZINC	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC2545091 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O…`
ZINC3606137 ZINC	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3869426 ZINC	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC3869602 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)COP(=…`
ZINC3869603 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O…`
ZINC3869604 ZINC	0.889	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC8551307 ZINC	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC8551308 ZINC	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1532601 ZINC	0.750	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC32786787 ZINC	0.750	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC34764844 ZINC	0.733	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
ZINC100657408 ZINC	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC215934438 ZINC	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC255961849 ZINC	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC255961850 ZINC	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC5132021 ZINC	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC140264883 ZINC	0.688	223.3 Da LogP -0.43 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCON`
ZINC143705779 ZINC	0.688	443.5 Da LogP -0.34 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC71254558 ZINC	0.688	444.6 Da LogP 0.70 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC71254563 ZINC	0.688	488.6 Da LogP 0.71 TPSA 92.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC80685077 ZINC	0.688	427.5 Da LogP -0.28 TPSA 109.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC83253927 ZINC	0.688	400.5 Da LogP 0.68 TPSA 73.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90556279 ZINC	0.688	295.4 Da LogP -0.33 TPSA 81.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCN`
ZINC90556287 ZINC	0.688	268.4 Da LogP 0.63 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCS`

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.