Protein target profile

KP13_00029

Glucosamine--fructose-6-phosphate aminotransferase isomerizing

Genome: KpKP13 Gene: glmS AHE47138.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H4X5

Export view

Length 609

Pocket druggability 0.989

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 10 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 0.71). 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 0.71. 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 (%): 40.93 Lower values reduce human off-target concern.
Human E-value: 4.81e-94
Gut microbiome similarity: 5.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.447 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: 94.29 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 0.989

Structure A0A0H3H4X5

Pocket Pocket 1

P2Rank 0.712

Structure A0A0H3H4X5

Pocket Pocket 1

ColabFold model

FPocket 0.962 · Pocket 1

P2Rank 0.759 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 277 / 4744 genomes with a hit

Prevalence 5.8%

Cross-references

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

Sequence

UniProt A0A0H3H4X5

Chemistry

ChEMBL CHEMBL1911372

Sequence

Primary amino-acid sequence viewer.

MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDSEGHMTRVRRLGKVQMLAQAVEEQPLHGGTGIAHTRWATHGEPSESNAHPHVSEHIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGTLREAVLRAIPQLRGAYGTVIMDTRDPGTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVVIFDKSGAEVKRQEIESNLQYDAGDKGIYRHYMQKEIFEQPNAIKNTLTGRISHGEVDLSELGPNANEMLAQVEHIQIVACGTSYNSGMVSRYWFEALAGVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLGSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLTVLLMLVAKLARLKGQDASIEHDIVHGLQALPNRIEQMLSQDKRIEQLAERFSDKHHALFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKSNIEEVRARGGELYVFADGEAGFNGSDNMHIIEMPHVEETIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

2.6.1.16

Gene Ontology (GO)

GO:1901135 The chemical reactions and pathways involving carbohydrate derivative.
GO:0097367 Binding to a carbohydrate derivative.
GO:0004360 Catalysis of the reaction: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate.
GO:1901137 The chemical reactions and pathways resulting in the formation of carbohydrate derivative.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046349 The chemical reactions and pathways resulting in the formation of any amino sugar, sugars containing an amino group in place of a hydroxyl group.
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:0006002 The chemical reactions and pathways involving fructose 6-phosphate, also known as F6P. The D-enantiomer is an important intermediate in glycolysis, gluconeogenesis, and fructose metabolism.
GO:0006487 A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of an asparagine residue.
GO:0006047 The chemical reactions and pathways involving UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
2	241	Gene3D	G3DSA:3.60.20.10	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
2	241	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
286	426	ProSiteProfiles	PS51464	SIS domain profile.
286	426	InterPro	IPR001347	SIS domain
2	609	NCBIfam	TIGR01135	glutamine--fructose-6-phosphate transaminase (isomerizing)
2	609	InterPro	IPR005855	Glucosamine-fructose-6-phosphate aminotransferase, isomerising
447	594	Gene3D	G3DSA:3.40.50.10490	-
2	232	SUPERFAMILY	SSF56235	N-terminal nucleophile aminohydrolases (Ntn hydrolases)
2	232	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
458	599	ProSiteProfiles	PS51464	SIS domain profile.
458	599	InterPro	IPR001347	SIS domain
453	607	CDD	cd05009	SIS_GlmS_GlmD_2
453	607	InterPro	IPR035490	GlmS/FrlB, SIS domain 2
451	594	FunFam	G3DSA:3.40.50.10490:FF:000002	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
1	609	Hamap	MF_00164	Glutamine--fructose-6-phosphate aminotransferase [isomerizing] [glmS].
1	609	InterPro	IPR005855	Glucosamine-fructose-6-phosphate aminotransferase, isomerising
289	418	Pfam	PF01380	SIS domain
289	418	InterPro	IPR001347	SIS domain
462	591	Pfam	PF01380	SIS domain
462	591	InterPro	IPR001347	SIS domain
248	608	Gene3D	G3DSA:3.40.50.10490	-
2	218	ProSiteProfiles	PS51278	Glutamine amidotransferase type 2 domain profile.
2	218	InterPro	IPR017932	Glutamine amidotransferase type 2 domain
2	240	FunFam	G3DSA:3.60.20.10:FF:000006	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
295	421	CDD	cd05008	SIS_GlmS_GlmD_1
295	421	InterPro	IPR035466	GlmS/AgaS, SIS domain 1
1	609	PANTHER	PTHR10937	GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING
66	174	Pfam	PF13522	Glutamine amidotransferase domain
245	609	SUPERFAMILY	SSF53697	SIS domain
245	609	InterPro	IPR046348	SIS domain superfamily
2	215	CDD	cd00714	GFAT
2	215	InterPro	IPR047084	Glucosamine-fructose-6-phosphate aminotransferase, isomerising, N-terminal domain
247	450	FunFam	G3DSA:3.40.50.10490:FF:000001	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

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

0.989

Likely same site as P2Rank 2 4.4 Å 22 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #35

0.362

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.712

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.435

Likely same site as FPocket 1 4.4 Å 22 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.291

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.22

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.064

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:2-2 Nucleophile; for GATase activity

UniProt: Active site:604-604 For Fru-6P isomerization activity

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.759

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.334

Likely same site as FPocket 1 4.0 Å 14 shared residues 74% of smaller site

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.155

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.07

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.046

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_A0A0H3H4X5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00029	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 and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AGP PDB via homolog 261.2 Da · LogP -3.50 · TPSA 173.7 Open detail RCSB PDB

F6R PDB via homolog Detail RCSB PDB

G6Q PDB via homolog Detail RCSB PDB

HGA PDB via homolog Detail RCSB PDB

M6R 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
AGP RCSB PDB	1MOS	P17169	261.2 Da LogP -3.50 TPSA 173.7	1 viol.	✓ Clean	`C([C@@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)…`
F6R RCSB PDB	4AMV	P17169	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H](C(=O)CO)O)O)O)OP(=O)(O)O`
G6Q RCSB PDB	1JXA	P17169	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…`
HGA RCSB PDB	1XFG	P17169	162.1 Da LogP -1.32 TPSA 112.7	✓ Ro5	✓ Clean	`C(CC(=O)NO)[C@@H](C(=O)O)N`
M6R RCSB PDB	2PUV	P53704	261.2 Da LogP -3.50 TPSA 173.7	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)N…`
UD1 RCSB PDB	2PUT	P53704	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
UD2 RCSB PDB	6SVM	Q06210-2	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@H]([C@H](O[C@@H]1O[P@@](…`

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
CHEMBL1911372 ChEMBL	Q06210	6.82 ~151.4 nM	225.0 Da LogP -1.09 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CNC(=O)CBr)C(=O)O`

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`
ZINC100065511 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[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`
ZINC100085043 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[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…`
ZINC104869937 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(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`
ZINC13537943 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
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`
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…`
ZINC85994845 ZINC	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC5132038 ZINC	0.897	290.2 Da LogP -3.90 TPSA 185.0	1 viol.	✓ Clean	`O=C(CO)[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`
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`
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`
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`
ZINC1529626 ZINC	0.793	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1532567 ZINC	0.793	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532851 ZINC	0.793	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC30320708 ZINC	0.793	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[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`
ZINC12502210 ZINC	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@@H](O)COP(=O…`
ZINC12502212 ZINC	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC12502214 ZINC	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@@H](O)COP(=…`
ZINC12502216 ZINC	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@H](O)COP(=O…`
ZINC4523251 ZINC	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@@H](O)COP(…`
ZINC4523255 ZINC	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@H](O)COP(=…`
ZINC4523257 ZINC	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@@H](O)COP(=…`
ZINC4523259 ZINC	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@H](O)COP(=O…`
ZINC2516111 ZINC	0.724	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)CO`
ZINC2522704 ZINC	0.724	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC3869812 ZINC	0.724	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
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`
ZINC13518200 ZINC	0.688	276.2 Da LogP -2.32 TPSA 144.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)[C@H](S)COP(=O)(O)O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)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.