KpATCC43816 Protein target profile

2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylic-acid synthase

Accession: VK055_4853

Gene: AIK83380.1 menD 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GVP4

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Length 556

Pocket druggability (P2Rank · AlphaFold DB model) 0.619

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 6 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 chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.62, FPocket 0.73). Use the 3D pocket comparison to verify whether they identify the same site. Central metabolic position More central than 94.9% 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: 2.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 48.233 Higher values support similarity to known essential genes.
DEG E-value: 2.06e-180 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.82 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.619

Structure A0A0H3GVP4

Pocket Pocket 1

Druggability (FPocket) 0.729

Structure A0A0H3GVP4

Pocket Pocket 14

ColabFold model

P2Rank 0.643 · Pocket 1

FPocket 0.849 · Pocket 11

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 104 / 4744 genomes with a hit

Prevalence 2.2%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Ubiquinone and other terpenoid-quinone biosynthesis, no isoenzyme backup detected, more central than 94.9% of genes in this genome, no human homolog detected.

Relative network centrality 94.9% more central than 94.9% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSVSAFNRRWAAVILEALTRHGVQHICIAPGSRSTPLTLAAAENRAFIHHTHFDERGLGHLALGLAKASRQPVAVIVTSGTATANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPAQTISLPRPSQDIPARWLVSTIDQALGALHAGGVHINCPFAEPLYGDMDETGVEWQQQLGNWWQSDKPWLRQALQLESEKQRDWFFWRQKRGVVVAGRMSAAEGKKVAEWAQTLGWPLIGDVLSQTGQPLPCADLWLGNGKAVSELAQAQIVVQLGSSLTGKRVLQWQATCEPDEYWLVDNLPGRLDPAQHRGRRLLSSVERWLELHPAEKRQPWATVIPQLAGQAWQAAVASNEPFGEAQLAQRIRGYLPEQGQLFVGNSLVVRLIDALAQLPAGYPVYSNRGASGIDGLIATAAGVQRASARPTLAIVGDLSALYDLNSLALLRQASAPLVLIVVNNNGGQIFSMLPTPQDERRQFYLMPQDVDFSHAAAMFGLAYHRPDDWPSLDEALAGAWRRAGATVIELAVNETDGAQTLQQLLAQVSRL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Unknown

Enzyme Commission (EC)

2.2.1.9

Gene Ontology (GO)

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:0030976 Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
GO:0070204 Catalysis of the reaction: 2-oxoglutarate + H+ + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2.
GO:0009234 The chemical reactions and pathways resulting in the formation of any of the menaquinones. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones that have vitamin K activity and are known as vitamin K2.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0030145 Binding to a manganese ion (Mn).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
4	553	Hamap	MF_01659	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [menD].
4	553	InterPro	IPR004433	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
10	430	NCBIfam	TIGR00173	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
10	430	InterPro	IPR004433	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
1	196	FunFam	G3DSA:3.40.50.970:FF:000029	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
414	534	Pfam	PF02775	Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
414	534	InterPro	IPR011766	Thiamine pyrophosphate enzyme, TPP-binding
1	196	Gene3D	G3DSA:3.40.50.970	-
184	388	Pfam	PF16582	Middle domain of thiamine pyrophosphate
184	388	InterPro	IPR032264	Menaquinone biosynthesis protein MenD, middle domain
348	556	Gene3D	G3DSA:3.40.50.970	-
362	552	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
362	552	InterPro	IPR029061	Thiamin diphosphate-binding fold
5	550	PANTHER	PTHR42916	2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE
12	170	CDD	cd07037	TPP_PYR_MenD
11	130	Pfam	PF02776	Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
11	130	InterPro	IPR012001	Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
7	174	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
7	174	InterPro	IPR029061	Thiamin diphosphate-binding fold
367	538	CDD	cd02009	TPP_SHCHC_synthase
1	556	PIRSF	PIRSF004983	MenD
1	556	InterPro	IPR004433	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
212	337	Gene3D	G3DSA:3.40.50.1220	-

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

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.619

Likely same site as FPocket 3 1.6 Å 17 shared residues 85% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.517

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Surrounding area

Pocket 3 P2Rank #3

0.057

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Surrounding area

Pocket 4 P2Rank #4

0.047

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Surrounding area

Pocket 5 P2Rank #5

0.012

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #14

0.729

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Surrounding area

Pocket 2 FPocket #3

0.637

Likely same site as P2Rank 1 1.6 Å 17 shared residues 85% of smaller site

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Surrounding area

Pocket 3 FPocket #15

0.421

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Surrounding area

Pocket 4 FPocket #27

0.362

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.643

Likely same site as FPocket 4 1.0 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.59

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Surrounding area

Pocket 3 P2Rank #3

0.037

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Surrounding area

Pocket 4 P2Rank #4

0.014

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Surrounding area

Pocket 5 P2Rank #5

0.011

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #11

0.849

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Surrounding area

Pocket 2 FPocket #14

0.431

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Surrounding area

Pocket 3 FPocket #4

0.297

Likely same site as P2Rank 1 1.0 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 4 FPocket #37

0.25

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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_A0A0H3GVP4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4853	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 6 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AKG PDB via homolog 146.1 Da · LogP -0.50 · TPSA 91.7 Open detail RCSB PDB

DNA PDB via homolog Detail RCSB PDB

ISC PDB via homolog Detail RCSB PDB

TD5 PDB via homolog Detail RCSB PDB

TD6 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
AKG RCSB PDB	3HWW	P17109	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
DNA RCSB PDB	6O0J	P9WK11	204.2 Da LogP 1.95 TPSA 77.8	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(cc(c2O)C(=O)O)O`
ISC RCSB PDB	5ESO	P9WK11	226.2 Da LogP -0.09 TPSA 104.1	✓ Ro5	✓ Clean	`C=C(C(=O)O)O[C@H]1C=CC=C([C@@H]1O)C(=O)O`
TD5 RCSB PDB	5EJM	P17109	527.4 Da LogP 0.74 TPSA 226.5	2 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@@H](CCC(=O)O)O)CC…`
TD6 RCSB PDB	5EJ4	P17109	527.4 Da LogP 0.74 TPSA 226.5	2 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@H](CCC(=O)O)O)CCO…`
TOI RCSB PDB	5ESU	P9WK11	753.6 Da LogP -0.04 TPSA 331.3	3 viol.	✓ Clean	`[H]/N=C/1\C(=CNC(=N1)C)C[n+]2c(c(sc2[C@](CCC(=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
1CS ChEMBL	J7HAW4	8.15 ~7.1 nM	357.8 Da LogP 1.35 TPSA 123.2	✓ Ro5	✓ Clean	`Cc1nc(nc(n1)OC)NC(=O)NS(=O)(=O)c2ccccc2Cl`
CHEMBL401913 ChEMBL	J7HAW4	7.64 ~22.9 nM	350.4 Da LogP 1.30 TPSA 138.3	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)O)n1`

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
ZINC1854808 ZINC	1.000	350.4 Da LogP 1.30 TPSA 138.3	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)O)n1`
ZINC409255 ZINC	1.000	204.2 Da LogP 1.95 TPSA 77.8	✓ Ro5	✓ Clean	`O=C(O)c1cc(O)c2ccccc2c1O`
ZINC186159 ZINC	0.792	337.4 Da LogP 1.01 TPSA 123.2	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC1565922 ZINC	0.769	430.4 Da LogP 3.87 TPSA 149.2	✓ Ro5	Alert	`O=C(O)c1cc(C(=O)C(=O)c2cc(C(=O)O)c(O)c3ccccc23)…`
ZINC22016278 ZINC	0.765	461.1 Da LogP 2.87 TPSA 123.2	✓ Ro5	✓ Clean	`COc1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(C(Cl)(Cl)C…`
ZINC2521491 ZINC	0.765	373.8 Da LogP 1.06 TPSA 143.4	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)c2cc(O)ccc2Cl)n1`
ZINC103209083 ZINC	0.761	336.3 Da LogP 0.99 TPSA 138.3	✓ Ro5	✓ Clean	`Cc1ccnc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)O)n1`
ZINC3176576 ZINC	0.744	320.4 Da LogP 1.91 TPSA 101.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC300799 ZINC	0.711	340.8 Da LogP 2.26 TPSA 101.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)n1`
ZINC18193628 ZINC	0.692	370.8 Da LogP 1.41 TPSA 117.2	✓ Ro5	✓ Clean	`Cc1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(N(C)C)n1`
ZINC1703286 ZINC	0.690	202.2 Da LogP 2.45 TPSA 57.5	✓ Ro5	✓ Clean	`CC(=O)c1cc(O)c2ccccc2c1O`
ZINC394847 ZINC	0.688	267.3 Da LogP 0.89 TPSA 117.7	✓ Ro5	✓ Clean	`NS(=O)(=O)c1cc(C(=O)O)c(O)c2ccccc12`
ZINC22204870 ZINC	0.684	409.8 Da LogP 2.30 TPSA 136.3	✓ Ro5	✓ Clean	`COc1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(-c2ccco2)n1`
ZINC104199149 ZINC	0.667	444.4 Da LogP 4.26 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)CC(=O)c2cc(C(=O)O)c(O)c3ccccc23…`
ZINC1565924 ZINC	0.667	230.2 Da LogP 2.45 TPSA 74.6	✓ Ro5	✓ Clean	`CC(=O)c1cc(C(=O)O)c(O)c2ccccc12`
ZINC235999 ZINC	0.667	267.1 Da LogP 3.01 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)c1cc(Br)c2ccccc2c1O`
ZINC38337775 ZINC	0.667	264.3 Da LogP 3.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)c1cc(-c2ccccc2)c2ccccc2c1O`
ZINC4014517 ZINC	0.667	222.6 Da LogP 2.90 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)c1cc(Cl)c2ccccc2c1O`
ZINC59687703 ZINC	0.667	206.2 Da LogP 2.38 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)c1cc(F)c2ccccc2c1O`
ZINC3149462 ZINC	0.660	371.8 Da LogP 1.38 TPSA 114.4	✓ Ro5	✓ Clean	`COc1nc(C)nc(N(C)C(=O)NS(=O)(=O)c2ccccc2Cl)n1`
ZINC902231 ZINC	0.660	357.8 Da LogP 1.56 TPSA 126.7	✓ Ro5	✓ Clean	`COc1nc(C)nc(N/C(O)=N\S(=O)(=O)c2ccccc2Cl)n1`
ZINC1226893 ZINC	0.655	440.7 Da LogP 2.53 TPSA 123.2	✓ Ro5	✓ Clean	`COc1nc(NC(=O)NS(=O)(=O)c2ccccc2C)nc(C(Cl)(Cl)Cl…`
ZINC2149641 ZINC	0.636	280.3 Da LogP 3.47 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(Oc1ccccc1)c1cc(O)c2ccccc2c1O`
ZINC3848736 ZINC	0.633	340.8 Da LogP 2.26 TPSA 101.0	✓ Ro5	✓ Clean	`Cc1cc(Cl)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC3639593 ZINC	0.627	365.4 Da LogP 0.79 TPSA 140.2	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc1nc(C)nc(C)n1`
ZINC13335462 ZINC	0.625	218.2 Da LogP 2.04 TPSA 66.8	✓ Ro5	✓ Clean	`COC(=O)c1cc(O)c2ccccc2c1O`
ZINC22016266 ZINC	0.614	484.7 Da LogP 2.00 TPSA 149.5	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc1nc(OC)nc(C(Cl)…`
ZINC22016269 ZINC	0.614	395.4 Da LogP 0.88 TPSA 149.5	✓ Ro5	✓ Clean	`CCOc1nc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)n1`
ZINC2275141 ZINC	0.610	421.9 Da LogP 2.15 TPSA 131.8	✓ Ro5	✓ Clean	`Cc1cc(C)n(-c2nc(C)nc(NC(=O)NS(=O)(=O)c3ccccc3Cl…`
ZINC3848734 ZINC	0.608	336.4 Da LogP 1.61 TPSA 110.3	✓ Ro5	✓ Clean	`COc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C)n1`
ZINC22016313 ZINC	0.607	351.4 Da LogP 1.26 TPSA 123.2	✓ Ro5	✓ Clean	`CCc1nc(NC(=O)NS(=O)(=O)c2ccccc2C)nc(OC)n1`
ZINC22016655 ZINC	0.607	408.2 Da LogP 1.37 TPSA 148.1	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)Nc2nc(Cl)ccc2Cl)n1`
ZINC35874338 ZINC	0.603	493.2 Da LogP 1.00 TPSA 160.5	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)c2cc(I)ccc2C(=O)O)n1`
ZINC1074291 ZINC	0.593	433.9 Da LogP 3.10 TPSA 123.2	✓ Ro5	✓ Clean	`CCOc1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(-c2ccccc2…`
ZINC221542346 ZINC	0.593	450.5 Da LogP 1.52 TPSA 145.8	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC[C@@H…`
ZINC221542395 ZINC	0.593	450.5 Da LogP 1.52 TPSA 145.8	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC[C@H]…`
ZINC221542457 ZINC	0.593	450.5 Da LogP 1.52 TPSA 145.8	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC[C@@H…`
ZINC221542513 ZINC	0.593	450.5 Da LogP 1.52 TPSA 145.8	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC[C@H]…`
ZINC754111 ZINC	0.592	425.5 Da LogP 3.16 TPSA 104.3	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)N(Cc2ccccc2)Cc2ccccc…`
ZINC8215517 ZINC	0.592	425.3 Da LogP 0.84 TPSA 169.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…`
ZINC15218722 ZINC	0.589	421.3 Da LogP 2.02 TPSA 136.1	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)NS(=O)(=O)c2c(Cl)nc(C)c(Cl)c2…`
ZINC2243725 ZINC	0.589	413.4 Da LogP 0.42 TPSA 150.9	✓ Ro5	✓ Clean	`COCCOc1ccccc1S(=O)(=O)NC(=O)Nc1nc(OC)nc(OC)n1`
ZINC2831367 ZINC	0.583	423.5 Da LogP 1.66 TPSA 149.5	✓ Ro5	✓ Clean	`CCCCOc1nc(C)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)…`
ZINC1611750 ZINC	0.581	204.2 Da LogP 1.95 TPSA 77.8	✓ Ro5	Alert	`O=C(O)c1cc2ccccc2c(O)c1O`
ZINC13335464 ZINC	0.571	232.2 Da LogP 2.43 TPSA 66.8	✓ Ro5	✓ Clean	`CCOC(=O)c1cc(O)c2ccccc2c1O`
ZINC336013 ZINC	0.571	246.2 Da LogP 2.17 TPSA 83.8	✓ Ro5	✓ Clean	`CC(=O)Oc1cc(C(=O)O)c(O)c2ccccc12`
ZINC13130640 ZINC	0.569	395.4 Da LogP 0.74 TPSA 149.5	✓ Ro5	✓ Clean	`CCc1nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)nc(OC)n1`
ZINC388870 ZINC	0.566	328.2 Da LogP 3.14 TPSA 89.0	✓ Ro5	✓ Clean	`COc1nc(C)nc(NC(=O)Nc2ccc(Cl)c(Cl)c2)n1`
ZINC2831368 ZINC	0.565	461.9 Da LogP 3.88 TPSA 123.2	✓ Ro5	✓ Clean	`CCCCOc1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(-c2cccc…`
ZINC1182224 ZINC	0.563	467.9 Da LogP 2.80 TPSA 138.8	✓ Ro5	✓ Clean	`CN(C)c1nc(NC(=O)NS(=O)(=O)c2ccccc2Cl)nc(ON=C2CC…`

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.

Cross-references

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

2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylic-acid synthase

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

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways