Protein target profile

KP13_00276

Cellulose synthase catalytic subunit

Genome: KpKP13 Gene: AHE42187.1 acsA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GX47

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Length 703

Pocket druggability 0.989

Direct ligand evidence 0 54 total records

Functional annotation 1 EC 7 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 1.00). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. 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 1.00. 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: No hit
Gut microbiome similarity: 1.1% 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: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 90.36 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 A0A0H3GX47

Pocket Pocket 29

P2Rank 0.999

Structure A0A0H3GX47

Pocket Pocket 1

ColabFold model

FPocket 0.991 · Pocket 43

P2Rank 0.999 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 51 / 4744 genomes with a hit

Prevalence 1.1%

Cross-references

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

Sequence

UniProt A0A0H3GX47

Sequence

Primary amino-acid sequence viewer.

MKKSLFWLLALVLSPVAVLVVITPMDSQKQYIFGLLSIGILFLMGFSKRRSVSVIMVVTSLLMSTRYMYFRLTQTLHFNSSIEAILGMGLFLAEVYIWVMLLLNYLQTVWPLKRGIVPLPDDMSKWPTVDIYIPSYNEPLEVVRDTVLAAQCIDYPKDKMKIYLLDDGKRSEFAVFAADVGVGYITRNDNKHAKAGNLNHALTLTQGELICVFDCDHVATRVFLQATVGGFLKDPMLALVQTPHYFYSPDPFERNLSVGRNIPNEGMLFYGPIQQGNDNWNATFFCGSCAVIRREALAQIGGFAVETVTEDAHTALKFQRLGWKSAFLDIPLAAGLATERLVVHVIQRTRWARGMTQIFRVDNPLFGRGLTFQQRLCYLSAMLYYQFALPRVVFVTAPLAYLLFNLNIIYSSASLIVSYALPHLFLAIYVGSRMNGRYRYSFWGEIYDIVLAFHLVLPTLVTMIFPKRGKFNVTDKGGLLDVGYFDFTVVRPHLVVACLLALGVVVGIVRAIGHDYFGSDPNVIALNVGWGIYSLIFLLAAIAVARETRQVRKTIRIDVDIPVVIHYASGIVSRSHTADLSMGGCRVVAPDNRHLEDDIEEIELILQSGAISIPAQLVTSDERFLRLKFDEDIPLSRRRELVRVVLARADAWINPPRPQDNPFRSFFTILRCVFELFWLTWKTRRSQRNRATVAKTAQEDGTL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

2.4.1.12

Gene Ontology (GO)

GO:0035438 Binding to cyclic-di-GMP, cyclic dimeric guanosine monophosphate.
GO:0030244 The chemical reactions and pathways resulting in the formation of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
GO:0016759 Catalysis of the reaction: nucleoside-disphosphate-glucose + ((1,4)-beta-D-glucosyl)(n) = nucleoside-disphosphate + ((1,4)-beta-D-glucosyl)(n+1).
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0016760 Catalysis of the reaction: UDP-glucose + ((1,4)-beta-D-glucosyl)(n) = UDP + ((1,4)-beta-D-glucosyl)(n+1).
GO:0006011 The chemical reactions and pathways involving UDP-alpha-D-glucose, a substance composed of alpha-D-glucose in glycosidic linkage with uridine diphosphate.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

68 records

Show feature table

Start	End	DB	Term	Name
1	19	SignalP_EUK	SignalP-TM	SignalP-TM
81	106	PRINTS	PR01439	Cellulose synthase subunit A signature
81	106	InterPro	IPR003919	Cellulose synthase, subunit A
447	466	PRINTS	PR01439	Cellulose synthase subunit A signature
447	466	InterPro	IPR003919	Cellulose synthase, subunit A
378	404	PRINTS	PR01439	Cellulose synthase subunit A signature
378	404	InterPro	IPR003919	Cellulose synthase, subunit A
523	544	PRINTS	PR01439	Cellulose synthase subunit A signature
523	544	InterPro	IPR003919	Cellulose synthase, subunit A
217	241	PRINTS	PR01439	Cellulose synthase subunit A signature
217	241	InterPro	IPR003919	Cellulose synthase, subunit A
136	155	PRINTS	PR01439	Cellulose synthase subunit A signature
136	155	InterPro	IPR003919	Cellulose synthase, subunit A
53	73	PRINTS	PR01439	Cellulose synthase subunit A signature
53	73	InterPro	IPR003919	Cellulose synthase, subunit A
407	426	PRINTS	PR01439	Cellulose synthase subunit A signature
407	426	InterPro	IPR003919	Cellulose synthase, subunit A
487	511	PRINTS	PR01439	Cellulose synthase subunit A signature
487	511	InterPro	IPR003919	Cellulose synthase, subunit A
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
48	53	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
107	382	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
431	441	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
127	359	CDD	cd06421	CESA_CelA_like
108	405	SUPERFAMILY	SSF53448	Nucleotide-diphospho-sugar transferases
108	405	InterPro	IPR029044	Nucleotide-diphospho-sugar transferases
383	402	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
408	430	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
2	675	NCBIfam	TIGR03030	UDP-forming cellulose synthase catalytic subunit
2	675	InterPro	IPR003919	Cellulose synthase, subunit A
442	465	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
117	337	Gene3D	G3DSA:3.90.550.10	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
117	337	InterPro	IPR029044	Nucleotide-diphospho-sugar transferases
5	25	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
73	83	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
52	69	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
302	433	Pfam	PF03552	Cellulose synthase
302	433	InterPro	IPR005150	Cellulose synthase
547	652	Gene3D	G3DSA:2.40.10.220	predicted glycosyltransferase like domains
84	106	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
682	703	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
84	106	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
552	631	SUPERFAMILY	SSF141371	PilZ domain-like
54	72	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
443	465	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
21	29	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
524	545	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
523	545	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
5	13	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
403	407	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
408	430	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
30	47	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
30	47	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
513	523	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
546	662	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
663	681	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
494	512	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
130	300	Pfam	PF00535	Glycosyl transferase family 2
130	300	InterPro	IPR001173	Glycosyltransferase 2-like
489	511	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	13	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
466	493	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
14	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
382	404	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
550	645	Pfam	PF07238	PilZ domain
550	645	InterPro	IPR009875	PilZ domain
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
57	547	PANTHER	PTHR43867	CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]

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 #29

0.989

Unusual size

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Surrounding area

Site 2 FPocket #54

0.979

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

0.999

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Surrounding area

Site 2 P2Rank #2

0.297

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Surrounding area

Site 3 P2Rank #3

0.188

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Surrounding area

Site 4 P2Rank #4

0.108

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Surrounding area

Site 5 P2Rank #5

0.096

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #43

0.991

Unusual size

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Surrounding area

Site 2 FPocket #8

0.964

Unusual size

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Surrounding area

Site 3 FPocket #36

0.428

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Surrounding area

Site 4 FPocket #44

0.228

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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

0.999

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Surrounding area

Site 2 P2Rank #2

0.495

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Surrounding area

Site 3 P2Rank #3

0.347

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Surrounding area

Site 4 P2Rank #4

0.078

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Surrounding area

Site 5 P2Rank #5

0.045

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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_A0A0H3GX47	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00276	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

C2E PDB via homolog 690.4 Da · LogP -3.05 · TPSA 349.6 Open detail RCSB PDB

GDD PDB via homolog Detail RCSB PDB

LDA PDB via homolog Detail RCSB PDB

PLC PDB via homolog Detail RCSB PDB

ZINC12501894 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
C2E RCSB PDB	5EJZ	Q3J125	690.4 Da LogP -3.05 TPSA 349.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@H]4[C@H](O3)CO[P@@](=O…`
GDD RCSB PDB	6YV9	A3MTD6	605.3 Da LogP -4.63 TPSA 331.7	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
LDA RCSB PDB	4HG6	Q3J125	229.4 Da LogP 4.48 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)[O-]`
PLC RCSB PDB	5EJZ	Q3J125	622.8 Da LogP 8.12 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](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
ZINC12501894 ZINC	1.000	345.2 Da LogP -1.52 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H]3CO[P@](=O)(O)O[C@@H]…`
ZINC13544781 ZINC	1.000	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	1.000	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC1849937 ZINC	1.000	201.4 Da LogP 3.70 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)[O-]`
ZINC2008702 ZINC	1.000	243.4 Da LogP 4.87 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC[N+](C)(C)[O-]`
ZINC2039372 ZINC	1.000	229.4 Da LogP 4.48 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)[O-]`
ZINC2516963 ZINC	1.000	215.4 Da LogP 4.09 TPSA 23.1	✓ Ro5	✓ Clean	`CCCCCCCCCCC[N+](C)(C)[O-]`
ZINC33494013 ZINC	1.000	345.2 Da LogP -1.52 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H]3CO[P@](=O)(O)O[C@@H]…`
ZINC4095501 ZINC	1.000	345.2 Da LogP -1.52 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H]3CO[P@](=O)(O)O[C@H]3…`
ZINC88465990 ZINC	1.000	345.2 Da LogP -1.52 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H]3CO[P@@](=O)(O)O[C@H]…`
ZINC13543439 ZINC	0.977	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441 ZINC	0.977	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC33822387 ZINC	0.911	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC33822389 ZINC	0.911	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)…`
ZINC12834352 ZINC	0.826	398.4 Da LogP 1.88 TPSA 108.4	✓ Ro5	✓ Clean	`CCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)OC…`
ZINC12834353 ZINC	0.826	398.4 Da LogP 1.88 TPSA 108.4	✓ Ro5	✓ Clean	`CCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)OC(…`
ZINC102190506 ZINC	0.771	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	0.771	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC34541308 ZINC	0.761	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC102189757 ZINC	0.755	454.6 Da LogP 4.04 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OCC[N+…`
ZINC13544128 ZINC	0.755	370.4 Da LogP 1.70 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCC[N+](C)(C…`
ZINC14880038 ZINC	0.755	440.5 Da LogP 3.65 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCC[N+]…`
ZINC14880039 ZINC	0.755	440.5 Da LogP 3.65 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OCC[N+]…`
ZINC15297567 ZINC	0.755	468.6 Da LogP 4.43 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCC[…`
ZINC32789157 ZINC	0.755	412.5 Da LogP 2.87 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCC[N+](C…`
ZINC32789161 ZINC	0.755	412.5 Da LogP 2.87 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCC[N+](C)…`
ZINC32822149 ZINC	0.755	468.6 Da LogP 4.43 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCC[N+…`
ZINC32822162 ZINC	0.755	482.6 Da LogP 4.82 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCC…`
ZINC32822163 ZINC	0.755	482.6 Da LogP 4.82 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCC[N…`
ZINC44305349 ZINC	0.755	454.6 Da LogP 4.04 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCC[N…`
ZINC44405718 ZINC	0.755	398.5 Da LogP 2.48 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCC[N+](C…`
ZINC44405722 ZINC	0.755	426.5 Da LogP 3.26 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCC[N+]…`
ZINC85576534 ZINC	0.755	384.4 Da LogP 2.09 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCC[N+](C)…`
ZINC27416437 ZINC	0.750	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.750	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC13507210 ZINC	0.735	356.4 Da LogP 1.31 TPSA 102.3	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCC[N+](C)(C)C`
ZINC13508374 ZINC	0.708	370.4 Da LogP 1.10 TPSA 108.4	✓ Ro5	✓ Clean	`CCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)OC(=…`
ZINC28711394 ZINC	0.706	415.3 Da LogP -0.17 TPSA 180.9	1 viol.	✓ Clean	`CCCC(=O)O[C@@H]1[C@@H]2O[P@](=O)(O)OC[C@H]2O[C@…`
ZINC13515981 ZINC	0.701	415.3 Da LogP -0.37 TPSA 177.9	✓ Ro5	✓ Clean	`CCCC(=O)Nc1nc2c(ncn2[C@@H]2O[C@@H]3CO[P@](=O)(O…`
ZINC25757995 ZINC	0.689	346.2 Da LogP -1.81 TPSA 168.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)c2ncn([C@H]3O[C@H]4CO[P@](=O)(O)O[…`
ZINC25757999 ZINC	0.689	346.2 Da LogP -1.81 TPSA 168.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)c2ncn([C@H]3O[C@H]4CO[P@@](=O)(O)O…`
ZINC4095873 ZINC	0.689	329.2 Da LogP -0.49 TPSA 154.6	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@@H]3O[P@@](=O)(O)OC[C@H]3…`
ZINC102191119 ZINC	0.686	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551 ZINC	0.686	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC2390993 ZINC	0.683	424.1 Da LogP -0.76 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(nc(Br)n2[C@H]2O[C@@H]3CO[P@@](=O)(O)O[C…`
ZINC34046802 ZINC	0.683	424.1 Da LogP -0.76 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(nc(Br)n2[C@@H]2O[C@H]3CO[P@@](=O)(O)O[C…`
ZINC3871269 ZINC	0.683	424.1 Da LogP -0.76 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(nc(Br)n2[C@@H]2O[C@@H]3CO[P@@](=O)(O)O[…`
ZINC3871271 ZINC	0.683	424.1 Da LogP -0.76 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(nc(Br)n2[C@@H]2O[C@@H]3CO[P@@](=O)(O)O[…`
ZINC4475080 ZINC	0.683	424.1 Da LogP -0.76 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(nc(Br)n2[C@@H]2O[C@@H]3CO[P@@](=O)(O)O[…`
ZINC4654944 ZINC	0.683	424.1 Da LogP -0.76 TPSA 174.8	✓ Ro5	✓ Clean	`Nc1nc2c(nc(Br)n2[C@@H]2O[C@@H]3CO[P@@](=O)(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.