Protein target profile

VK055_2542

citrate-sodium symporter

Genome: KpATCC43816 Gene: AIK81139.1 citS 3D evidence: Experimental + ColabFold model UniProt P31602

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Length 446

Pocket druggability 0.987

Direct ligand evidence 2 52 total records

Functional annotation 0 EC 8 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Direct ligand evidence 2 direct ligand records. Strong known ligand: co-crystal structure 2 PDB record(s) show a ligand actually co-crystallized with this exact protein - real experimental evidence, not a computational prediction. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. 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: 0.7% 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: 90.9 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

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 0.987

Structure 9LSJ

Pocket Pocket 3

P2Rank 0.743

Structure 9LSK

Pocket Pocket 1

ColabFold model

FPocket 0.357 · Pocket 4

P2Rank 0.626 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 35 / 4744 genomes with a hit

Prevalence 0.7%

Cross-references

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

Sequence

UniProt P31602

Structure

PDB 5XAS PDB 5XAR PDB 5XAT PDB 5X9R PDB 9LSH PDB 9LSI PDB 9LSJ PDB 9LSK

Sequence

Primary amino-acid sequence viewer.

MTNMSQAPATEKKGVSDLLGFKIFGMPLPLYAFALITLLLSHFYNALPTDIVGGFAIMFIIGAIFGEIGKRLPIFNKYIGGAPVMIFLVAAYFVYAGIFTQKEIDAISNVMDKSNFLNLFIAVLITGAILSVNRRLLLKSLLGYIPTILMGIVGASIFGIAIGLVFGIPVDRIMMLYVLPIMGGGNGAGAVPLSEIYHSVTGRSREEYYSTAIAILTIANIFAIVFAAVLDIIGKKHTWLSGEGELVRKASFKVEEDEKAGQITHRETAVGLVLSTTCFLLAYVVAKKILPSIGGVAIHYFAWMVLIVAALNASGLCSPEIKAGAKRLSDFFSKQLLWVLMVGVGVCYTDLQEIINAITFANVVIAAIIVIGAVLGAAIGGWLMGFFPIESAITAGLCMANRGGSGDLEVLSACNRMNLISYAQISSRLGGGIVLVIASIVFGMMI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

GO:0008514 OBSOLETE. Enables the transfer of organic anions from one side of a membrane to the other. Organic anions are atoms or small molecules with a negative charge which contain carbon in covalent linkage.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0015711 The directed movement of organic anions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Organic anions are atoms or small molecules with a negative charge which contain carbon in covalent linkage.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0046872 Binding to a metal ion.
GO:0015293 Enables the active transport of a solute across a membrane by a mechanism whereby two or more species are transported together in the same direction in a tightly coupled process not directly linked to a form of energy other than chemiosmotic energy.
GO:0006101 The chemical reactions and pathways involving citrate, 2-hydroxy-1,2,3-propanetricarboxylate. Citrate is widely distributed in nature and is an important intermediate in the TCA cycle and the glyoxylate cycle.
GO:0006814 The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

45 records

Show feature table

Start	End	DB	Term	Name
425	444	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
446	446	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
176	198	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
385	424	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
269	286	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
144	168	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
336	358	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
114	132	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
208	230	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
46	66	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
23	440	Pfam	PF03390	2-hydroxycarboxylate transporter family
23	440	InterPro	IPR004679	2-hydroxycarboxylate transporter
3	446	PIRSF	PIRSF005348	YxkH
3	446	InterPro	IPR004679	2-hydroxycarboxylate transporter
174	196	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
96	114	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
352	362	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
78	95	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
133	143	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
18	441	NCBIfam	TIGR00783	citrate:cation symporter
18	441	InterPro	IPR018025	2-hydroxycarboxylate transporter, proteobacteria/firmicutes
115	132	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
23	45	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
79	101	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
208	230	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
2	445	PANTHER	PTHR40033	NA(+)-MALATE SYMPORTER
2	445	InterPro	IPR004679	2-hydroxycarboxylate transporter
197	207	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
296	315	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
363	384	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
52	69	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
312	330	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
425	445	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
67	77	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
231	267	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
21	40	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
293	311	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
363	385	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
268	286	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
41	45	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
287	292	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1	20	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
147	169	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
169	173	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
331	351	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.

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 #1

0.922

Likely same site as P2Rank 5 0.9 Å 19 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #9

0.517

Likely same site as P2Rank 3 1.7 Å 10 shared residues 100% of smaller site

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Surrounding area

Site 3 FPocket #6

0.509

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Surrounding area

Site 4 FPocket #12

0.438

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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

0.968

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Surrounding area

Site 2 P2Rank #2

0.737

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Surrounding area

Site 3 P2Rank #3

0.585

Likely same site as FPocket 9 1.7 Å 10 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.537

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Surrounding area

Site 5 P2Rank #5

0.427

Likely same site as FPocket 1 0.9 Å 19 shared residues 100% of smaller site

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #4

0.357

Unusual size

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Surrounding area

Site 2 FPocket #24

0.337

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Surrounding area

Site 3 FPocket #17

0.204

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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

0.626

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Surrounding area

Site 2 P2Rank #2

0.237

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Surrounding area

Site 3 P2Rank #3

0.194

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Surrounding area

Site 4 P2Rank #4

0.112

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Surrounding area

Site 5 P2Rank #5

0.11

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Surrounding area

Residue sets

UniProt: Binding site:181-181

UniProt: Binding site:183-183

UniProt: Binding site:186-186

UniProt: Binding site:187-187

UniProt: Binding site:399-399

UniProt: Binding site:401-401

UniProt: Binding site:402-402

UniProt: Binding site:404-404

UniProt: Binding site:405-405

UniProt: Binding site:428-428

All structural evidence 8 experimental · 1 predicted

Structural evidence

8 + 1

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
PDB 5XAS	X-ray	3.47 Å	A,B	97.3% 13-446	PDBe RCSB PDBj File	Viewing
PDB 5XAR	X-ray	3.62 Å	A,B,C,D	97.3% 13-446	PDBe RCSB PDBj File	Loaded
PDB 5XAT	X-ray	3.76 Å	A,B,C,D	97.3% 13-446	PDBe RCSB PDBj File	Loaded
PDB 5X9R	X-ray	3.98 Å	A,B	97.3% 13-446	PDBe RCSB PDBj File	Loaded
PDB 9LSH	X-ray	—	A	—	PDBe RCSB PDBj File	Loaded
PDB 9LSI	X-ray	—	A	—	PDBe RCSB PDBj File	Loaded
PDB 9LSJ	X-ray	—	A	—	PDBe RCSB PDBj File	Loaded
PDB 9LSK	X-ray	—	A	—	PDBe RCSB PDBj File	Loaded
ColabFold VK055_2542	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 2 same-protein records

Transferred evidence 0 records from similar proteins

Structural ligands 2 2 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

BOG PDB co-crystal 292.4 Da · LogP 0.16 · TPSA 99.4 Open detail RCSB PDB

FLC PDB co-crystal Detail RCSB PDB

ZINC100034925 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC100050848 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC100056252 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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
BOG RCSB PDB	5XAR 3.62 Å Open crystal	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)CO)…`
FLC RCSB PDB	5X9R 3.98 Å Open crystal	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`

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.

No PDB ligands found through similar proteins.

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
ZINC100034925 ZINC	1.000	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC100050848 ZINC	1.000	376.5 Da LogP 2.50 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](…`
ZINC100056252 ZINC	1.000	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[…`
ZINC100622854 ZINC	1.000	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O…`
ZINC100622858 ZINC	1.000	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O…`
ZINC100622862 ZINC	1.000	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC100623033 ZINC	1.000	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)…`
ZINC100623036 ZINC	1.000	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O…`
ZINC100623039 ZINC	1.000	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)…`
ZINC100623040 ZINC	1.000	334.5 Da LogP 1.33 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O…`
ZINC105807070 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H…`
ZINC106384623 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC118906329 ZINC	1.000	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[…`
ZINC118906375 ZINC	1.000	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H]1O`
ZINC118911494 ZINC	1.000	278.3 Da LogP -0.23 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H…`
ZINC118911500 ZINC	1.000	278.3 Da LogP -0.23 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H]…`
ZINC118911909 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@…`
ZINC140958235 ZINC	1.000	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)…`
ZINC140974145 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@…`
ZINC141152247 ZINC	1.000	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H]…`
ZINC141261234 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C…`
ZINC141262250 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@…`
ZINC14880349 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)[…`
ZINC14880350 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)[C…`
ZINC15609263 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC1849674 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@@H](CO)[C@H](O)[C@@H](O)[C@@…`
ZINC2046837 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@H]1O[C@@H](CO)[C@H](O)[C@@H](O)[C@…`
ZINC248251557 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@@H](CO)[C@H](O)[C@@H](O)[C…`
ZINC40165555 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H…`
ZINC4521560 ZINC	1.000	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O`
ZINC48016017 ZINC	1.000	278.3 Da LogP -0.23 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]…`
ZINC49878458 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)[…`
ZINC53683291 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]…`
ZINC5820343 ZINC	1.000	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O`
ZINC58538417 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C…`
ZINC58563863 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]…`
ZINC59206904 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@…`
ZINC66122924 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H…`
ZINC71788562 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC71788563 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC71788565 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C…`
ZINC71788566 ZINC	1.000	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C…`
ZINC85478989 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC85590873 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)[…`
ZINC85590876 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)…`
ZINC85590883 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)[…`
ZINC85590888 ZINC	1.000	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)…`
ZINC85605815 ZINC	1.000	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[…`
ZINC94437834 ZINC	1.000	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O`
ZINC95713698 ZINC	1.000	348.5 Da LogP 1.72 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](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.