Protein target profile

VK055_1548

3-phosphoshikimate 1-carboxyvinyltransferase

Genome: KpATCC43816 Gene: AIK80168.1 aroA 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt A0A0H3GV01

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Length 412

Pocket druggability 0.506

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 74 total records

Functional annotation 1 EC 7 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

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Central metabolic position More central than 99.5% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: 3.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 88.35 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 98.16 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 0.506

Structure 7TM4

Pocket Pocket 2

P2Rank 0.918

Structure 7TM6

Pocket Pocket 1

ColabFold model

FPocket 0.409 · Pocket 1

P2Rank 0.795 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 181 / 4744 genomes with a hit

Prevalence 3.8%

Cross-references

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

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction in Phenylalanine, tyrosine and tryptophan biosynthesis, no isoenzyme backup detected, more central than 99.5% of genes in this genome, no human homolog detected.

Relative network centrality 99.5% more central than 99.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MNLPGSKSVSNRALLLAALARGTTVLTNLLDSDDVRHMLNALSALGVQYTLSADRTRCEVTGNGGPLRSAAALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRQGGAQIDYLEQENYPPLRLRGGFQGGNVEVDGSVSSQFLTALLMTAPLAPQDTVIVIKGDLVSKPYIDITLHLMKTFGVEVDNQSYQRFVVRGKQQYQSPGDYLVEGDASSASYFLAAGAIKGGTVKVTGIGRNSVQGDIRFADVLEKMGATVTWGDDFIACTHGELKAVDMDMNHIPDAAMTIATAALFAQGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGEDYIRITPPAKLKYAEIGTYNDHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISTLA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

2.5.1.19

Gene Ontology (GO)

GO:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
GO:0009073 The chemical reactions and pathways resulting in the formation of aromatic amino acid family, amino acids with aromatic ring (phenylalanine, tyrosine, tryptophan).
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:0003866 Catalysis of the reaction: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0009423 The chemical reactions and pathways resulting in the formation of the unsymmetrical ether derived from phosphoenolpyruvate and 5-phosphoshikimic acid formed as an intermediate in the biosynthesis of aromatic amino acids and many other compounds.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
1	411	PIRSF	PIRSF000505	EPSPS
1	411	InterPro	IPR006264	3-phosphoshikimate 1-carboxyvinyltransferase
28	412	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
2	408	SUPERFAMILY	SSF55205	EPT/RTPC-like
2	408	InterPro	IPR013792	RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta
1	12	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
13	20	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	27	Phobius	SIGNAL_PEPTIDE	Signal peptide region
226	403	Gene3D	G3DSA:3.65.10.10	Enolpyruvate transferase domain
226	403	InterPro	IPR036968	Enolpyruvate transferase domain superfamily
75	89	ProSitePatterns	PS00104	EPSP synthase signature 1.
75	89	InterPro	IPR023193	3-phosphoshikimate 1-carboxyvinyltransferase, conserved site
5	208	FunFam	G3DSA:3.65.10.10:FF:000004	3-phosphoshikimate 1-carboxyvinyltransferase
2	407	PANTHER	PTHR21090	AROM/DEHYDROQUINATE SYNTHASE
2	408	CDD	cd01556	EPSP_synthase
2	408	InterPro	IPR006264	3-phosphoshikimate 1-carboxyvinyltransferase
21	27	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
2	408	NCBIfam	TIGR01356	3-phosphoshikimate 1-carboxyvinyltransferase
1	411	Hamap	MF_00210	3-phosphoshikimate 1-carboxyvinyltransferase [aroA].
5	208	Gene3D	G3DSA:3.65.10.10	Enolpyruvate transferase domain
5	208	InterPro	IPR036968	Enolpyruvate transferase domain superfamily
323	341	ProSitePatterns	PS00885	EPSP synthase signature 2.
323	341	InterPro	IPR023193	3-phosphoshikimate 1-carboxyvinyltransferase, conserved site
2	405	Pfam	PF00275	EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
2	405	InterPro	IPR001986	Enolpyruvate transferase domain
220	403	FunFam	G3DSA:3.65.10.10:FF:000003	3-phosphoshikimate 1-carboxyvinyltransferase

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 · P2Rank

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

Site 1 P2Rank #1

0.918

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Surrounding area

Site 2 P2Rank #2

0.228

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Surrounding area

Site 3 P2Rank #3

0.127

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Surrounding area

Site 4 P2Rank #4

0.078

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Surrounding area

Site 5 P2Rank #5

0.015

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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

0.795

Likely same site as FPocket 1 1.0 Å 20 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.134

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Surrounding area

Site 3 P2Rank #3

0.029

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Surrounding area

Site 4 P2Rank #4

0.006

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Surrounding area

Residue sets

UniProt: Active site:313-313 Proton acceptor

UniProt: Binding site:124-124

UniProt: Binding site:169-169

UniProt: Binding site:170-170

UniProt: Binding site:171-171

UniProt: Binding site:197-197

UniProt: Binding site:22-22

UniProt: Binding site:23-23

UniProt: Binding site:27-27

UniProt: Binding site:313-313

UniProt: Binding site:336-336

UniProt: Binding site:340-340

UniProt: Binding site:344-344

UniProt: Binding site:386-386

UniProt: Binding site:411-411

UniProt: Binding site:96-96

All structural evidence 3 experimental · 1 predicted

Structural evidence

3 + 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 7TM6	X-ray	1.26 Å	A,B	100.0% 1-412	PDBe RCSB PDBj File	Viewing
PDB 7TM5	X-ray	1.41 Å	A,B	100.0% 1-412	PDBe RCSB PDBj File	Loaded
PDB 7TM4	X-ray	1.70 Å	A	100.0% 1-412	PDBe RCSB PDBj File	Loaded
ColabFold VK055_1548	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.

74 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 24 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 14 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3DS PDB via homolog 172.1 Da · LogP -1.31 · TPSA 94.8 Open detail RCSB PDB

EPS PDB via homolog Detail RCSB PDB

GG9 PDB via homolog Detail RCSB PDB

GPF PDB via homolog Detail RCSB PDB

GPJ 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
3DS RCSB PDB	6HQV	G0S061	172.1 Da LogP -1.31 TPSA 94.8	✓ Ro5	✓ Clean	`C1[C@H]([C@@H](C(=O)C=C1C(=O)O)O)O`
EPS RCSB PDB	2O0Z	P9WPY5	324.2 Da LogP -0.78 TPSA 170.8	✓ Ro5	✓ Clean	`C=C(C(=O)O)O[C@@H]1CC(=C[C@H]([C@H]1O)OP(=O)(O)…`
GG9 RCSB PDB	2PQ9	P0A6D3	458.2 Da LogP -1.22 TPSA 237.6	1 viol.	✓ Clean	`C1[C@H]([C@@H]([C@@H](C=C1C(=O)O)OP(=O)(O)O)O)O…`
GPF RCSB PDB	3FJZ	P0A6D3	169.1 Da LogP -1.20 TPSA 106.9	✓ Ro5	✓ Clean	`C(C(=O)O)NCP(=O)(O)O`
GPJ RCSB PDB	3SLH	Q83E11	170.1 Da LogP -2.23 TPSA 111.4	✓ Ro5	✓ Clean	`C(C(=O)O)[NH2+]CP(=O)(O)O`
PEP RCSB PDB	2O0E	P9WPY5	168.0 Da LogP -0.31 TPSA 104.1	✓ Ro5	✓ Clean	`C=C(C(=O)O)OP(=O)(O)O`
RC1 RCSB PDB	1X8T	P0A6D3	406.2 Da LogP -1.40 TPSA 228.3	1 viol.	✓ Clean	`C[C@@](C(=O)O)(O[C@@H]1CC(=C[C@H]([C@H]1O)OP(=O…`
S3P RCSB PDB	1G6S	P0A6D3	254.1 Da LogP -1.40 TPSA 144.5	✓ Ro5	✓ Clean	`C1[C@H]([C@@H]([C@@H](C=C1C(=O)O)OP(=O)(O)O)O)O`
SKM RCSB PDB	2AA9	P0A6D3	174.2 Da LogP -1.52 TPSA 98.0	✓ Ro5	✓ Clean	`C1[C@H]([C@@H]([C@@H](C=C1C(=O)O)O)O)O`
SKP RCSB PDB	1Q36	P0A6D3	422.2 Da LogP -1.46 TPSA 237.6	1 viol.	✓ Clean	`C[C@](C(=O)O)(O[C@@H]1CC(=C[C@H]([C@H]1O)OP(=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
CHEMBL1627014 ChEMBL	P0A6D3	9.22 ~0.6 nM	462.1 Da LogP -5.85 TPSA 240.4	1 viol.	✓ Clean	`O=C([O-])C1=C[C@@H](OP(=O)(O)O)[C@@H](O)[C@H](O…`
CHEMBL1627015 ChEMBL	P0A6D3	8.40 ~4.0 nM	480.1 Da LogP -5.55 TPSA 240.4	1 viol.	✓ Clean	`O=C([O-])C1=C[C@@H](OP(=O)(O)O)[C@@H](O)[C@H](O…`
CHEMBL1627013 ChEMBL	P0A6D3	8.30 ~5.0 nM	428.2 Da LogP -5.73 TPSA 231.2	1 viol.	✓ Clean	`C[C@@](O[C@@H]1CC(C(=O)[O-])=C[C@@H](OP(=O)(O)O…`
CHEMBL1160691 ChEMBL	P0A6D3	7.84 ~14.5 nM	221.1 Da LogP -0.12 TPSA 130.8	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(O)P(=O)(O)O)c[nH]1`
SC1 ChEMBL	P0A6D3	7.82 ~15.1 nM	406.2 Da LogP -1.40 TPSA 228.3	1 viol.	✓ Clean	`C[C@](C(=O)O)(O[C@@H]1CC(=C[C@H]([C@H]1O)OP(=O)…`
CHEMBL1627010 ChEMBL	P0A6D3	7.50 ~31.6 nM	498.1 Da LogP -5.25 TPSA 240.4	1 viol.	✓ Clean	`O=C([O-])C1=C[C@@H](OP(=O)(O)O)[C@@H](O)[C@H](O…`
CHEMBL337302 ChEMBL	P0A6D3	7.00 ~100.0 nM	300.3 Da LogP 2.43 TPSA 96.2	✓ Ro5	Alert	`COc1ccc(/C=C2/Oc3c(ccc(O)c3O)C2=O)c(O)c1`
CHEMBL1627011 ChEMBL	P0A6D3	6.80 ~158.5 nM	394.1 Da LogP -4.51 TPSA 210.9	✓ Ro5	✓ Clean	`O=C([O-])c1cc(OC(C(=O)O)P(=O)(O)O)cc(OP(=O)(O)O…`
CHEMBL313253 ChEMBL	P0A6D3	6.80 ~158.5 nM	460.0 Da LogP -16.09 TPSA 219.4	✓ Ro5	✓ Clean	`O=C([O-])c1cc(OC(C(=O)[O-])P(=O)([O-])O)cc(OP(=…`
CHEMBL95406 ChEMBL	P0A6D3	6.30 ~501.2 nM	184.1 Da LogP -1.62 TPSA 124.1	✓ Ro5	✓ Clean	`NN(CC(=O)O)CP(=O)(O)O`
CHEMBL98868 ChEMBL	P0A6D3	6.28 ~524.8 nM	410.2 Da LogP -1.59 TPSA 256.4	1 viol.	✓ Clean	`O=C(O)c1cc(OC(C(=O)O)P(=O)(O)O)c(O)c(C(O)(C(=O)…`
CHEMBL334500 ChEMBL	P0A6D3	6.19 ~645.7 nM	325.4 Da LogP 3.56 TPSA 70.0	✓ Ro5	Alert	`CCN(CC)c1ccc(/C=C2/Oc3c(ccc(O)c3O)C2=O)cc1`
CHEMBL314675 ChEMBL	P0A6D3	6.11 ~776.2 nM	358.0 Da LogP -6.93 TPSA 176.5	✓ Ro5	✓ Clean	`O=C(O)c1cc(OP(=O)([O-])O)cc(OP(=O)([O-])O)c1.[N…`
CHEMBL33426 ChEMBL	P0A6D3	6.00 ~1.0 µM	390.1 Da LogP -13.07 TPSA 179.3	✓ Ro5	✓ Clean	`C=C(O[C@@H]1CC(C(=O)[O-])=C[C@@H](OP(=O)([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
ZINC3870237 ZINC	1.000	254.1 Da LogP -1.40 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(O)C1=C[C@@H](OP(=O)(O)O)[C@@H](O)[C@H](O)C1`
ZINC85783 ZINC	0.756	297.3 Da LogP 2.78 TPSA 70.0	✓ Ro5	Alert	`CN(C)c1ccc(/C=C2/Oc3c(ccc(O)c3O)C2=O)cc1`
ZINC62957630 ZINC	0.740	366.5 Da LogP 3.92 TPSA 53.0	✓ Ro5	Alert	`CCN(CC)c1ccc(/C=C2\Oc3c(ccc(O)c3CN(C)C)C2=O)cc1`
ZINC12875038 ZINC	0.667	312.3 Da LogP 3.33 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc(/C=C2\Oc3c(ccc(O)c3C)C2=O)c(OC)c1`
ZINC13487310 ZINC	0.652	272.2 Da LogP 2.85 TPSA 66.8	✓ Ro5	Alert	`O=C1/C(=C/c2ccc(F)cc2)Oc2c1ccc(O)c2O`
ZINC26461480 ZINC	0.635	312.3 Da LogP 3.33 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc(OC)c(/C=C2\Oc3c(ccc(O)c3C)C2=O)c1`
ZINC14725429 ZINC	0.630	286.2 Da LogP 2.13 TPSA 107.2	✓ Ro5	Alert	`O=C1/C(=C/c2ccc(O)c(O)c2)Oc2c1ccc(O)c2O`
ZINC32501378 ZINC	0.620	314.3 Da LogP 2.73 TPSA 85.2	✓ Ro5	Alert	`COc1ccc(/C=C2\Oc3c(ccc(O)c3O)C2=O)cc1OC`
ZINC11869336 ZINC	0.600	268.3 Da LogP 3.02 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc2c(c1)O/C(=C\c1ccccc1O)C2=O`
ZINC4521601 ZINC	0.600	205.0 Da LogP -1.15 TPSA 127.1	✓ Ro5	✓ Clean	`O=P(O)(O)CNCP(=O)(O)O`
ZINC13653683 ZINC	0.596	355.4 Da LogP 3.09 TPSA 68.2	✓ Ro5	Alert	`COc1ccc(/C=C2\Oc3c(ccc(O)c3CN(C)C)C2=O)c(OC)c1`
ZINC36065969 ZINC	0.596	355.4 Da LogP 3.09 TPSA 68.2	✓ Ro5	Alert	`COc1ccc(/C=C2/Oc3c(ccc(O)c3CN(C)C)C2=O)c(OC)c1`
ZINC12876227 ZINC	0.577	326.3 Da LogP 3.64 TPSA 54.0	✓ Ro5	✓ Clean	`COc1ccc(/C=C2\Oc3c(ccc(OC)c3C)C2=O)c(OC)c1`
ZINC20624751 ZINC	0.576	383.4 Da LogP 3.87 TPSA 68.2	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1ccc(OC)cc1OC)C2=O`
ZINC20624352 ZINC	0.574	337.4 Da LogP 4.16 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1ccc(C)cc1)C2=O`
ZINC36065975 ZINC	0.574	337.4 Da LogP 4.16 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C/c1ccc(C)cc1)C2=O`
ZINC72238401 ZINC	0.571	272.2 Da LogP 2.85 TPSA 66.8	✓ Ro5	Alert	`O=C1/C(=C/c2ccccc2F)Oc2c1ccc(O)c2O`
ZINC13653789 ZINC	0.569	355.4 Da LogP 3.09 TPSA 68.2	✓ Ro5	Alert	`COc1ccc(OC)c(/C=C2\Oc3c(ccc(O)c3CN(C)C)C2=O)c1`
ZINC12879577 ZINC	0.569	282.3 Da LogP 3.33 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(/C=C2\Oc3c(ccc(O)c3C)C2=O)cc1`
ZINC12419920 ZINC	0.566	298.3 Da LogP 3.03 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc(/C=C2\Oc3cc(O)ccc3C2=O)c(OC)c1`
ZINC2040417132 ZINC	0.566	298.3 Da LogP 3.03 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc(C=C2Oc3cc(O)ccc3C2=O)c(OC)c1`
ZINC491271 ZINC	0.566	298.3 Da LogP 3.03 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc(/C=C2/Oc3cc(O)ccc3C2=O)c(OC)c1`
ZINC20624374 ZINC	0.564	357.8 Da LogP 4.50 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1ccc(Cl)cc1)C2=O`
ZINC20624628 ZINC	0.564	341.4 Da LogP 3.99 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1ccc(F)cc1)C2=O`
ZINC20647292 ZINC	0.564	402.3 Da LogP 4.61 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1ccc(Br)cc1)C2=O`
ZINC36065977 ZINC	0.564	341.4 Da LogP 3.99 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C/c1ccc(F)cc1)C2=O`
ZINC36065978 ZINC	0.564	357.8 Da LogP 4.50 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C/c1ccc(Cl)cc1)C2=O`
ZINC8990603 ZINC	0.564	351.4 Da LogP 4.41 TPSA 49.8	✓ Ro5	Alert	`CCc1ccc(/C=C2\Oc3c(ccc(O)c3CN(CC)CC)C2=O)cc1`
ZINC26439487 ZINC	0.559	335.4 Da LogP 3.82 TPSA 60.7	✓ Ro5	✓ Clean	`COc1ccc2c(c1)c(/C=C1\Oc3c(ccc(O)c3C)C1=O)cn2C`
ZINC8765524 ZINC	0.559	335.4 Da LogP 3.82 TPSA 60.7	✓ Ro5	✓ Clean	`COc1ccc2c(c1)c(/C=C1/Oc3c(ccc(O)c3C)C1=O)cn2C`
ZINC20624791 ZINC	0.557	381.4 Da LogP 3.62 TPSA 68.2	✓ Ro5	Alert	`COc1ccc(/C=C2\Oc3c(ccc(O)c3CN3CCCC3)C2=O)c(OC)c1`
ZINC20646883 ZINC	0.557	411.5 Da LogP 4.65 TPSA 68.2	✓ Ro5	Alert	`CCCN(CCC)Cc1c(O)ccc2c1O/C(=C\c1ccc(OC)cc1OC)C2=O`
ZINC26439506 ZINC	0.557	349.4 Da LogP 4.30 TPSA 60.7	✓ Ro5	✓ Clean	`CCn1cc(/C=C2\Oc3c(ccc(O)c3C)C2=O)c2cc(OC)ccc21`
ZINC8764920 ZINC	0.557	349.4 Da LogP 4.30 TPSA 60.7	✓ Ro5	✓ Clean	`CCn1cc(/C=C2/Oc3c(ccc(O)c3C)C2=O)c2cc(OC)ccc21`
ZINC22625605 ZINC	0.556	323.4 Da LogP 3.85 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1ccccc1)C2=O`
ZINC26461486 ZINC	0.556	282.3 Da LogP 3.33 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cccc(/C=C2\Oc3c(ccc(O)c3C)C2=O)c1`
ZINC2048532699 ZINC	0.552	482.4 Da LogP 3.76 TPSA 205.0	✓ Ro5	✓ Clean	`O=C(O)c1cc(Oc2cc(C(=O)O)cc(C(=O)O)c2)cc(Oc2cc(C…`
ZINC299738170 ZINC	0.551	268.3 Da LogP 3.02 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1c(O)ccc2c1O/C(=C\c1ccc(O)cc1)C2=O`
ZINC20624578 ZINC	0.550	383.4 Da LogP 3.87 TPSA 68.2	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1cc(OC)ccc1OC)C2=O`
ZINC20517641 ZINC	0.548	443.5 Da LogP 3.12 TPSA 86.7	✓ Ro5	Alert	`COCCN(CCOC)Cc1c(O)ccc2c1O/C(=C\c1ccc(OC)cc1OC)C…`
ZINC20646869 ZINC	0.548	409.5 Da LogP 4.40 TPSA 68.2	✓ Ro5	Alert	`COc1ccc(/C=C2\Oc3c(ccc(O)c3CN3CCCCCC3)C2=O)c(OC…`
ZINC13811645 ZINC	0.545	323.4 Da LogP 3.63 TPSA 49.8	✓ Ro5	Alert	`CCc1ccc(/C=C2\Oc3c(ccc(O)c3CN(C)C)C2=O)cc1`
ZINC34481004 ZINC	0.545	202.2 Da LogP -1.04 TPSA 87.0	✓ Ro5	✓ Clean	`CCOC(=O)C1=C[C@@H](O)[C@@H](O)[C@H](O)C1`
ZINC20624349 ZINC	0.544	353.4 Da LogP 3.86 TPSA 59.0	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1ccc(OC)cc1)C2=O`
ZINC20663710 ZINC	0.544	365.5 Da LogP 4.97 TPSA 49.8	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C\c1ccc(C(C)C)cc1)C2=O`
ZINC36065989 ZINC	0.544	353.4 Da LogP 3.86 TPSA 59.0	✓ Ro5	Alert	`CCN(CC)Cc1c(O)ccc2c1O/C(=C/c1ccc(OC)cc1)C2=O`
ZINC22575532 ZINC	0.540	424.5 Da LogP 3.16 TPSA 71.5	✓ Ro5	Alert	`CCN1CCN(Cc2c(O)ccc3c2O/C(=C\c2ccc(OC)cc2OC)C3=O…`
ZINC22625745 ZINC	0.540	397.4 Da LogP 2.86 TPSA 77.5	✓ Ro5	Alert	`COc1ccc(/C=C2\Oc3c(ccc(O)c3CN3CCOCC3)C2=O)c(OC)…`
ZINC23078065 ZINC	0.540	410.5 Da LogP 2.77 TPSA 71.5	✓ Ro5	Alert	`COc1ccc(/C=C2\Oc3c(ccc(O)c3CN3CCN(C)CC3)C2=O)c(…`
ZINC72238404 ZINC	0.538	272.2 Da LogP 2.85 TPSA 66.8	✓ Ro5	Alert	`O=C1/C(=C/c2cccc(F)c2)Oc2c1ccc(O)c2O`

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.

VK055_1548

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

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Structure

Chemistry

Pathways

Metabolic context

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence