KpATCC43816 Protein target profile

3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase

Accession: VK055_2778

Gene: iolD AIK81367.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GLT3

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Length 646

Pocket druggability (P2Rank · AlphaFold DB model) 0.838

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 77 total records

Functional annotation 0 EC 5 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. Central metabolic position More central than 91.1% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. 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: Hit
Human identity (%): 31.818 Lower values reduce human off-target concern.
Human E-value: 1.05e-07
Gut microbiome similarity: 5.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 26.976 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 97.3 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) 0.838

Structure A0A0H3GLT3

Pocket Pocket 1

Druggability (FPocket) 0.87

Structure A0A0H3GLT3

Pocket Pocket 9

ColabFold model

P2Rank 0.839 · Pocket 1

FPocket 0.992 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 241 / 4744 genomes with a hit

Prevalence 5.1%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a consuming chokepoint reaction in Inositol phosphate metabolism, no isoenzyme backup detected, more central than 91.1% of genes in this genome.

Relative network centrality 91.1% more central than 91.1% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MGKLRLTTAQALVKFLDNQYLEVDGVELKFVKGIFAIFGHGNVLGLGQALEQDSGDMRVYQGRNEQGMAHAATGFARQALRRQIIACTSSIGPGAANMITAAGTASANRIPLLLLPGDVFATRQPDPVLQQIEQSYDLSISTNDAFRAVSKYWDRITRPEQLMSACINAMRVLTDPAETGAVTLCLPQDVQGEAWDYPESFFARRVHRLDRRPASAAQLADAVAAIKGSRKPLIVCGGGVKYSGAGEALSRFAERYGVPFAETQAGKGTVVSSHPLNVGGVGETGCLAANLLAKEADLVIGVGTRFSDFTTASKWIFQHPEVRFLNINVSNFDAWKLDGIAMLADAREAMTALDAALADSGWQAGWGAQIESVQSRQLKETQRVYQAVWQEKSFVPEIDDHLDRESVYREFRQITDSTLTQSSVLGVLNETLPAEAVIVAAAGSLPGDLQRVWRNRAENTYHVEYGYSCMGYEVNAALGVKLAQPQSEVYSLVGDGSFMMLHSELVTSLQERAKINVVLFDNMANGCINNLQMEHGMDSFGTEFRYRQPETGQLQGGLVPVDFATIAAGYGCKTWRVTTLDELRHALDAARRETVSTLIDIKVLPKTMVHKYGSWWNVGVAQTALSERIRKVAQMINEKRAQARDY

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0016823 Catalysis of the hydrolysis of any carbon-carbon bond in a ketonic substance, a substance containing a keto (C=O) group.
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:0019310 The chemical reactions and pathways resulting in the breakdown of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
GO:0000287 Binding to a magnesium (Mg) ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
185	367	SUPERFAMILY	SSF52467	DHS-like NAD/FAD-binding domain
185	367	InterPro	IPR029035	DHS-like NAD/FAD-binding domain superfamily
419	630	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
419	630	InterPro	IPR029061	Thiamin diphosphate-binding fold
214	393	Gene3D	G3DSA:3.40.50.1220	-
409	641	Gene3D	G3DSA:3.40.50.970	-
478	497	ProSitePatterns	PS00187	Thiamine pyrophosphate enzymes signature.
478	497	InterPro	IPR000399	TPP-binding enzyme, conserved site
3	208	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
3	208	InterPro	IPR029061	Thiamin diphosphate-binding fold
442	601	Pfam	PF02775	Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
442	601	InterPro	IPR011766	Thiamine pyrophosphate enzyme, TPP-binding
5	644	NCBIfam	TIGR04377	3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (decyclizing)
5	644	InterPro	IPR030817	3,5/4-Trihydroxycyclohexa-1,2-dione hydrolase
220	353	Pfam	PF00205	Thiamine pyrophosphate enzyme, central domain
220	353	InterPro	IPR012000	Thiamine pyrophosphate enzyme, central domain
10	188	CDD	cd07035	TPP_PYR_POX_like
7	196	Pfam	PF02776	Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
7	196	InterPro	IPR012001	Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
421	624	CDD	cd02003	TPP_IolD
5	608	PANTHER	PTHR18968	THIAMINE PYROPHOSPHATE ENZYMES
5	608	InterPro	IPR045229	Thiamine pyrophosphate enzyme
3	209	Gene3D	G3DSA:3.40.50.970	-

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

0.838

Likely same site as FPocket 9 4.4 Å 23 shared residues 92% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.798

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Surrounding area

Pocket 3 P2Rank #3

0.639

Likely same site as FPocket 9 5.6 Å 18 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.14

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Surrounding area

Pocket 5 P2Rank #5

0.096

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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 #9

0.87 Unusual size

Likely same site as P2Rank 1 4.4 Å 23 shared residues 92% of smaller site

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Surrounding area

Pocket 2 FPocket #2

0.676

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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

0.839

Likely same site as FPocket 27 4.1 Å 22 shared residues 88% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.794

Likely same site as FPocket 1 1.0 Å 24 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.752

Likely same site as FPocket 27 6.6 Å 17 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.17

Likely same site as FPocket 3 1.7 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.0

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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 #1

0.992 Unusual size

Likely same site as P2Rank 2 1.0 Å 24 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #27

0.794 Unusual size

Likely same site as P2Rank 1 4.1 Å 22 shared residues 88% of smaller site

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Surrounding area

Pocket 3 FPocket #3

0.406

Likely same site as P2Rank 4 1.7 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 4 FPocket #32

0.317

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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_A0A0H3GLT3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2778	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.

77 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 27 records from similar proteins

Structural ligands 19 0 loaded crystals

Measured bioactivity 8 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1MM PDB via homolog 381.4 Da · LogP 0.49 · TPSA 149.5 Open detail RCSB PDB

AUJ PDB via homolog Detail RCSB PDB

AYD PDB via homolog Detail RCSB PDB

CIE PDB via homolog Detail RCSB PDB

CO2 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
1MM RCSB PDB	1T9D	P07342	381.4 Da LogP 0.49 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1nc(nc(n1)OC)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC`
AUJ RCSB PDB	5WKC	P07342	—	—	—	`Cc1ncc(c(n1)N)C[N]2=C(SC(=C2C)CCOP(=O)(O)OP(=O)…`
AYD RCSB PDB	1N0H	P07342	382.3 Da LogP 0.98 TPSA 177.1	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN/C(=C/CCO[P@@](=O)(O)OP(=O)(O)O…`
CIE RCSB PDB	1N0H	P07342	414.8 Da LogP 1.83 TPSA 136.6	✓ Ro5	✓ Clean	`CCOC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc2nc(cc(n2)Cl)OC`
CO2 RCSB PDB	6BD3	P07342	44.0 Da LogP -0.58 TPSA 34.1	✓ Ro5	✓ Clean	`C(=O)=O`
DTT RCSB PDB	1N0H	P07342	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
F50 RCSB PDB	5WKC	P07342	76.1 Da LogP 0.02 TPSA 46.5	✓ Ro5	✓ Clean	`CC(=O)OO`
HTL RCSB PDB	6BD3	P07342	467.4 Da LogP 1.04 TPSA 186.0	✓ Ro5	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)C(=O)C)CCO[P@@](=O)(…`
NSP RCSB PDB	1T9B	P07342	138.2 Da LogP -0.17 TPSA 77.8	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN`
OXY RCSB PDB	5IMS	P07342	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`
P22 RCSB PDB	1T9B	P07342	206.0 Da LogP 0.23 TPSA 113.3	✓ Ro5	✓ Clean	`CCO[P@](=O)(O)OP(=O)(O)O`
P23 RCSB PDB	1T9A	P07342	220.1 Da LogP 0.62 TPSA 113.3	✓ Ro5	✓ Clean	`CCCO[P@@](=O)(O)OP(=O)(O)O`
P25 RCSB PDB	1T9B	P07342	248.1 Da LogP 1.40 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCO[P@@](=O)(O)OP(=O)(O)O`
PXD RCSB PDB	5WKC	P07342	483.4 Da LogP 2.61 TPSA 116.9	✓ Ro5	✓ Clean	`COc1cnc(n2c1nc(n2)NS(=O)(=O)c3c(cccc3OCC(F)F)C(…`
PYD RCSB PDB	1T9D	P07342	123.2 Da LogP 0.68 TPSA 51.8	✓ Ro5	✓ Clean	`Cc1cnc(nc1N)C`
PYR RCSB PDB	6BD9	P07342	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
TP9 RCSB PDB	5WKC	P07342	412.3 Da LogP -0.03 TPSA 182.8	1 viol.	✓ Clean	`Cc1ncc(c(n1)N)CN/C(=C(/CCO[P@](=O)([O-])O[P@@](…`
YF3 RCSB PDB	1T9A	P07342	212.3 Da LogP 0.78 TPSA 63.8	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CNC(C)CS`
YF4 RCSB PDB	1T9A	P07342	180.3 Da LogP 0.82 TPSA 55.0	✓ Ro5	✓ Clean	`CCN(C)Cc1cnc(nc1N)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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
60G ChEMBL	P07342	8.36 ~4.4 nM	410.4 Da LogP 0.93 TPSA 145.8	✓ Ro5	✓ Clean	`COc1cc(nc(n1)NC(=O)NS(=O)(=O)Cc2ccccc2C(=O)OC)OC`
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`
1CS ChEMBL	A7XBP7	7.52 ~30.2 nM	357.8 Da LogP 1.35 TPSA 123.2	✓ Ro5	✓ Clean	`Cc1nc(nc(n1)OC)NC(=O)NS(=O)(=O)c2ccccc2Cl`
CHEMBL2313155 ChEMBL	P07342	7.50 ~31.6 nM	414.4 Da LogP -0.09 TPSA 163.6	1 viol.	✓ Clean	`CCOC(=O)c1cnn(C)c1S(=O)(=O)NC(=O)Nc1nc(OC)cc(OC…`
1SM ChEMBL	P07342	7.29 ~51.3 nM	364.4 Da LogP 1.39 TPSA 127.3	✓ Ro5	✓ Clean	`Cc1cc(nc(n1)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)C`
CHEMBL2313153 ChEMBL	P07342	7.19 ~64.6 nM	398.4 Da LogP 1.34 TPSA 138.0	✓ Ro5	✓ Clean	`CCOc1ccccc1OS(=O)(=O)NC(=O)Nc1nc(OC)cc(OC)n1`
CHEMBL1885280 ChEMBL	P07342	6.46 ~346.7 nM	410.4 Da LogP 0.61 TPSA 161.5	✓ Ro5	✓ Clean	`CCOc1nc(NC)nc(NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)n1`
1TB ChEMBL	P07342	6.40 ~398.1 nM	395.4 Da LogP 0.51 TPSA 140.7	✓ Ro5	✓ Clean	`Cc1nc(nc(n1)OC)N(C)C(=O)NS(=O)(=O)c2ccccc2C(=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
ZINC13827750 ZINC	1.000	483.4 Da LogP 2.61 TPSA 116.9	✓ Ro5	✓ Clean	`COc1cnc(OC)n2nc(NS(=O)(=O)c3c(OCC(F)F)cccc3C(F)…`
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`
ZINC103194086 ZINC	0.845	433.4 Da LogP 1.97 TPSA 116.9	✓ Ro5	✓ Clean	`COc1cccc(C(F)(F)F)c1S(=O)(=O)Nc1nc2c(OC)cnc(OC)…`
ZINC5463312 ZINC	0.800	234.1 Da LogP 1.28 TPSA 102.3	✓ Ro5	✓ Clean	`CCO[P@](=O)(O)O[P@](=O)(O)OCC`
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`
ZINC38334558 ZINC	0.770	421.3 Da LogP 2.10 TPSA 107.7	✓ Ro5	✓ Clean	`COc1cnc(OC)n2nc(NS(=O)(=O)c3c(F)cccc3C(F)(F)F)n…`
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`
ZINC2522710 ZINC	0.760	238.3 Da LogP 3.50 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCOP(=O)(O)OCCCCC`
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`
ZINC1673633 ZINC	0.667	266.3 Da LogP 4.02 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOP(=O)(O)O`
ZINC1849859 ZINC	0.667	238.3 Da LogP 3.24 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCOP(=O)(O)O`
ZINC2038200 ZINC	0.667	210.2 Da LogP 2.46 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCOP(=O)(O)O`
ZINC8215517 ZINC	0.656	425.3 Da LogP 0.84 TPSA 169.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…`
ZINC1577196 ZINC	0.654	210.2 Da LogP 2.72 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCOP(=O)(O)OCCCC`
ZINC13544772 ZINC	0.652	234.1 Da LogP 1.28 TPSA 102.3	✓ Ro5	✓ Clean	`CCOP(=O)(OCC)OP(=O)(O)O`
ZINC103195583 ZINC	0.645	404.2 Da LogP 2.25 TPSA 107.7	✓ Ro5	✓ Clean	`COc1cnc(OC)n2nc(NS(=O)(=O)c3c(Cl)cccc3Cl)nc12`
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`
ZINC2579357 ZINC	0.630	248.1 Da LogP 1.26 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)CCO[P@](=O)(O)OP(=O)(O)O`
ZINC3639593 ZINC	0.625	365.4 Da LogP 0.79 TPSA 140.2	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc1nc(C)nc(C)n1`
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`
ZINC8215654 ZINC	0.607	246.1 Da LogP 1.18 TPSA 113.3	✓ Ro5	✓ Clean	`C=C(C)CCO[P@@](=O)(O)OP(=O)(O)O`
ZINC45921737 ZINC	0.600	235.0 Da LogP 0.97 TPSA 51.8	✓ Ro5	✓ Clean	`Cc1ncc(I)c(N)n1`
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…`
ZINC13540298 ZINC	0.588	440.3 Da LogP 0.72 TPSA 187.1	✓ Ro5	✓ Clean	`Cc1ncc(Cn2c(C)c(CCO[P@@](=O)(O)OP(=O)(O)O)sc2=O…`
ZINC113027531 ZINC	0.576	310.4 Da LogP 3.58 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCO[P@](=O)(O)OCC[N+](C)(C)C`
ZINC1644960 ZINC	0.576	203.2 Da LogP -0.24 TPSA 106.2	✓ Ro5	✓ Clean	`Cc1ncc(CS(=O)(=O)O)c(N)n1`
ZINC217410460 ZINC	0.576	338.4 Da LogP 4.36 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[P@@](=O)(O)OCC[N+](C)(C)C`
ZINC3649862 ZINC	0.576	296.4 Da LogP 3.19 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCO[P@](=O)(O)OCC[N+](C)(C)C`
ZINC43562168 ZINC	0.576	352.5 Da LogP 4.75 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[P@@](=O)(O)OCC[N+](C)(C)C`
ZINC58660415 ZINC	0.576	324.4 Da LogP 3.97 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCO[P@@](=O)(O)OCC[N+](C)(C)C`
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`
ZINC15020471 ZINC	0.565	232.1 Da LogP 1.39 TPSA 93.1	✓ Ro5	✓ Clean	`CCO[P@@](=O)(O)C[P@](=O)(O)OCC`
ZINC87489300 ZINC	0.561	319.3 Da LogP -0.56 TPSA 116.6	✓ Ro5	✓ Clean	`CCOC(=O)CNS(=O)(=O)c1c(C(=O)OCC)cnn1C`
ZINC1532839 ZINC	0.561	345.3 Da LogP 0.72 TPSA 122.4	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCOP(=O)(O)O)c2C)c(N)n1`
ZINC1061537 ZINC	0.559	247.3 Da LogP 1.76 TPSA 77.6	✓ Ro5	✓ Clean	`Cc1cnc(SCc2cnc(C)nc2N)nc1`
ZINC3878521 ZINC	0.559	201.3 Da LogP 0.70 TPSA 55.7	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2ccccc2)c(N)n1`
ZINC6745052 ZINC	0.558	243.2 Da LogP 0.21 TPSA 100.5	✓ Ro5	✓ Clean	`CC(=O)NS(=O)(=O)c1ccccc1C(=O)O`
ZINC6827739 ZINC	0.550	258.0 Da LogP -0.69 TPSA 170.8	✓ Ro5	✓ Clean	`O=P(O)(O)OP(=O)(O)OP(=O)(O)O`
ZINC754110 ZINC	0.549	397.5 Da LogP 3.24 TPSA 113.1	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)Nc2ccc(-c3ccccc3)cc2…`
ZINC14985466 ZINC	0.547	233.2 Da LogP -0.76 TPSA 104.3	✓ Ro5	✓ Clean	`CCOC(=O)c1cnn(C)c1S(N)(=O)=O`
ZINC754132 ZINC	0.547	411.5 Da LogP 3.17 TPSA 104.3	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)NS(=O)(=O)N(Cc2ccccc2)c2ccccc2…`
ZINC455281 ZINC	0.545	242.3 Da LogP 2.74 TPSA 66.9	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NC(=O)Nc2ccccc2)n1`
ZINC251478 ZINC	0.543	215.3 Da LogP 1.01 TPSA 55.7	✓ Ro5	✓ Clean	`Cc1cc[n+](Cc2cnc(C)nc2N)cc1`
ZINC619990 ZINC	0.543	261.4 Da LogP 2.07 TPSA 77.6	✓ Ro5	✓ Clean	`Cc1cc(C)nc(SCc2cnc(C)nc2N)n1`
ZINC6614885 ZINC	0.543	231.3 Da LogP 2.66 TPSA 51.8	✓ Ro5	✓ Clean	`Cc1ncc(CSc2ccccc2)c(N)n1`

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.

3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase

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

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