KpATCC43816 Protein target profile

isocitrate lyase

Accession: VK055_3078

Gene: aceA AIK81663.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GHC8

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Length 434

Pocket druggability (P2Rank · AlphaFold DB model) 0.638

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 66 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

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.64, FPocket 0.80). Use the 3D pocket comparison to verify whether they identify the same site. Central metabolic position More central than 95.0% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. 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 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: 4.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 67.824 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.28 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) 0.638

Structure A0A0H3GHC8

Pocket Pocket 1

Druggability (FPocket) 0.795

Structure A0A0H3GHC8

Pocket Pocket 9

ColabFold model

P2Rank 0.58 · Pocket 1

FPocket 0.811 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 203 / 4744 genomes with a hit

Prevalence 4.3%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 95.0% of genes in this genome, no human homolog detected.

Relative network centrality 95.0% more central than 95.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKTRTQQIEELNKEWTNPRWEGITRPYSAEEVVKLRGSVNPECTLAQLGAAKLWRLLHGEAKKGYVNSLGALTGGQALQQAKAGIEAIYLSGWQVAADANLASSMYPDQSLYPANSVPAVVDRINNTFRRADQIQWSAGIEPNDPRFIDYFLPIVADAEAGFGGVLNAFELMKSMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAIQKLVAARLAADVMGVPTLVIARTDADAADLITSDCDPYDREFITGDRTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSKPDLEQARRFAEAIHARFPGKLLAYNCSPSFNWKKNLDDKTIASFQQQLSDMGYKYQFITLAGIHSMWFNMFDLAHAYAQGEGMRHYVEKVQQPEFAAGPEGYTFVSHQQEVGTGYFDKVTTIIQGGTSSVTALTGSTEEEQF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

4.1.3.1

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:0019752 The chemical reactions and pathways involving carboxylic acids, any organic acid containing one or more carboxyl (COOH) groups or anions (COO-).
GO:0004451 Catalysis of the reaction: isocitrate = glyoxylate + succinate.
GO:0046872 Binding to a metal ion.
GO:0006097 A modification of the TCA cycle occurring in some plants and microorganisms, in which isocitrate is cleaved to glyoxylate and succinate. Glyoxylate can then react with acetyl-CoA to form malate.
GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
53	368	CDD	cd00377	ICL_PEPM
53	368	InterPro	IPR039556	ICL/PEPM domain
4	434	PANTHER	PTHR21631	ISOCITRATE LYASE/MALATE SYNTHASE
4	434	InterPro	IPR006254	Isocitrate lyase
1	434	PIRSF	PIRSF001362	ICL
1	434	InterPro	IPR006254	Isocitrate lyase
4	417	SUPERFAMILY	SSF51621	Phosphoenolpyruvate/pyruvate domain
4	417	InterPro	IPR015813	Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
1	434	FunFam	G3DSA:3.20.20.60:FF:000005	Isocitrate lyase
256	434	NCBIfam	TIGR01346	isocitrate lyase
256	434	InterPro	IPR006254	Isocitrate lyase
8	255	NCBIfam	TIGR01346	isocitrate lyase
8	255	InterPro	IPR006254	Isocitrate lyase
1	417	Gene3D	G3DSA:3.20.20.60	-
1	417	InterPro	IPR040442	Pyruvate kinase-like domain superfamily
193	198	ProSitePatterns	PS00161	Isocitrate lyase signature.
193	198	InterPro	IPR018523	Isocitrate lyase/phosphorylmutase, conserved site
8	255	Pfam	PF00463	Isocitrate lyase family
257	434	Pfam	PF00463	Isocitrate lyase family
257	434	InterPro	IPR006254	Isocitrate lyase

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

0.638

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Surrounding area

Pocket 2 P2Rank #2

0.103

Likely same site as FPocket 1 4.5 Å 10 shared residues 71% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.086

Likely same site as FPocket 3 1.7 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.062

Likely same site as FPocket 7 3.7 Å 8 shared residues 80% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.047

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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

0.795

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Surrounding area

Pocket 2 FPocket #7

0.682

Likely same site as P2Rank 4 3.7 Å 8 shared residues 80% of smaller site

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Surrounding area

Pocket 3 FPocket #3

0.254

Likely same site as P2Rank 3 1.7 Å 13 shared residues 100% of smaller site

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Surrounding area

Pocket 4 FPocket #1

0.216

Likely same site as P2Rank 2 4.5 Å 10 shared residues 71% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:200-200 Proton acceptor

UniProt: Binding site:162-162

UniProt: Binding site:201-202

UniProt: Binding site:237-237

UniProt: Binding site:322-326

UniProt: Binding site:356-356

UniProt: Binding site:96-98

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.58

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Surrounding area

Pocket 2 P2Rank #2

0.113

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Surrounding area

Pocket 3 P2Rank #3

0.094

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Surrounding area

Pocket 4 P2Rank #4

0.075

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Surrounding area

Pocket 5 P2Rank #5

0.072

Likely same site as FPocket 2 1.4 Å 9 shared residues 82% of smaller site

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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 #2

0.811 Unusual size

Likely same site as P2Rank 5 1.4 Å 9 shared residues 82% of smaller site

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Surrounding area

Pocket 2 FPocket #27

0.608 Unusual size

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Surrounding area

Residue sets

UniProt: Active site:200-200 Proton acceptor

UniProt: Binding site:162-162

UniProt: Binding site:201-202

UniProt: Binding site:237-237

UniProt: Binding site:322-326

UniProt: Binding site:356-356

UniProt: Binding site:96-98

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_A0A0H3GHC8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3078	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.

66 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 16 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 7 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3NP PDB via homolog 119.1 Da · LogP -0.26 · TPSA 80.4 Open detail RCSB PDB

GLV PDB via homolog Detail RCSB PDB

ICT PDB via homolog Detail RCSB PDB

MLA PDB via homolog Detail RCSB PDB

OXD 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
3NP RCSB PDB	6C4A	P9WKK7	119.1 Da LogP -0.26 TPSA 80.4	✓ Ro5	✓ Clean	`C(C[N+](=O)[O-])C(=O)O`
GLV RCSB PDB	1F8I	P9WKK7	74.0 Da LogP -0.73 TPSA 54.4	✓ Ro5	✓ Clean	`C(=O)C(=O)O`
ICT RCSB PDB	6LRT	A9WDE7	192.1 Da LogP -1.39 TPSA 132.1	✓ Ro5	✓ Clean	`C([C@@H]([C@H](C(=O)O)O)C(=O)O)C(=O)O`
MLA RCSB PDB	3OQ8	Q2YQA0	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
OXD RCSB PDB	6VB9	P9WKK7	90.0 Da LogP -0.84 TPSA 74.6	✓ Ro5	✓ Clean	`C(=O)(C(=O)O)O`
PYR RCSB PDB	1IGW	P0A9G6	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
SIN RCSB PDB	1F8I	P9WKK7	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)O`
U9S RCSB PDB	6WSI	P9WKK7	132.1 Da LogP -1.08 TPSA 87.1	✓ Ro5	✓ Clean	`[C@@H]1([C@H](O1)C(=O)O)C(=O)O`
VGX RCSB PDB	5DQL	P9WKK7	118.1 Da LogP -0.98 TPSA 74.6	✓ Ro5	✓ Clean	`C(CO)C(=O)C(=O)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
CHEMBL1818383 ChEMBL	P9WKK7	7.00 ~100.0 nM	490.5 Da LogP 2.27 TPSA 135.2	✓ Ro5	✓ Clean	`COc1c(N2C(C)CN(C(=O)CC[N+](=O)[O-])CC2C)c(F)cc2…`
CHEMBL1818381 ChEMBL	P9WKK7	6.92 ~120.2 nM	432.4 Da LogP 1.49 TPSA 126.0	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2cc(N3CCN(C(=O)CC[N+](=O)[O-]…`
CHEMBL1818380 ChEMBL	P9WKK7	6.70 ~199.5 nM	420.4 Da LogP 1.17 TPSA 126.0	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)CC[N+](=…`
BPV ChEMBL	P9WKK6	—	167.0 Da LogP 0.03 TPSA 54.4	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)Br`
CHEMBL1497581 ChEMBL	P9WKK6	—	328.3 Da LogP 3.64 TPSA 89.9	✓ Ro5	✓ Clean	`CCOC(=O)c1ccc(CC(=O)c2oc3cc(O)ccc3c2C)o1`
CHEMBL4293898 ChEMBL	P9WKK6	—	340.3 Da LogP 3.45 TPSA 97.0	✓ Ro5	✓ Clean	`CCOC(=O)c1cc2cc(CC(=O)c3ccc(O)cc3O)ccc2o1`
ITN ChEMBL	P9WKK6	—	130.1 Da LogP 0.10 TPSA 74.6	✓ Ro5	✓ Clean	`C=C(CC(=O)O)C(=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
ZINC407263 ZINC	1.000	328.3 Da LogP 3.64 TPSA 89.9	✓ Ro5	✓ Clean	`CCOC(=O)c1ccc(CC(=O)c2oc3cc(O)ccc3c2C)o1`
ZINC519239 ZINC	1.000	340.3 Da LogP 3.45 TPSA 97.0	✓ Ro5	✓ Clean	`CCOC(=O)c1cc2cc(CC(=O)c3ccc(O)cc3O)ccc2o1`
ZINC2130430 ZINC	0.820	354.4 Da LogP 3.75 TPSA 86.0	✓ Ro5	✓ Clean	`CCOC(=O)c1cc2cc(CC(=O)c3ccc(OC)cc3O)ccc2o1`
ZINC3186991 ZINC	0.820	368.4 Da LogP 4.14 TPSA 86.0	✓ Ro5	✓ Clean	`CCOC(=O)c1cc2cc(CC(=O)c3ccc(OCC)cc3O)ccc2o1`
ZINC2325812886 ZINC	0.807	389.4 Da LogP 2.31 TPSA 82.8	✓ Ro5	✓ Clean	`CCCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3CC)C…`
ZINC4869572 ZINC	0.767	403.5 Da LogP 2.70 TPSA 82.8	✓ Ro5	✓ Clean	`CCCCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3CC)…`
ZINC2592080 ZINC	0.759	375.4 Da LogP 1.92 TPSA 82.8	✓ Ro5	✓ Clean	`CCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3CC)CC1`
ZINC4869545 ZINC	0.754	417.5 Da LogP 3.09 TPSA 82.8	✓ Ro5	✓ Clean	`CCCCCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3CC…`
ZINC9847172 ZINC	0.746	451.5 Da LogP 3.14 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)CCc4cccc…`
ZINC38140892 ZINC	0.742	445.5 Da LogP 3.87 TPSA 82.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3…`
ZINC38140894 ZINC	0.742	459.6 Da LogP 4.26 TPSA 82.8	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn…`
ZINC38140899 ZINC	0.742	473.6 Da LogP 4.65 TPSA 82.8	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)c…`
ZINC4082786 ZINC	0.742	431.5 Da LogP 3.48 TPSA 82.8	✓ Ro5	✓ Clean	`CCCCCCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C…`
ZINC9469693 ZINC	0.742	421.5 Da LogP 2.26 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)CCSC)CC3…`
ZINC9783296 ZINC	0.727	481.5 Da LogP 3.59 TPSA 82.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2cc(N3CCN(C(=O)CCc4ccccc4F)CC…`
ZINC3887391 ZINC	0.724	361.4 Da LogP 1.53 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(C)=O)CC3)cc…`
ZINC13178736 ZINC	0.712	468.4 Da LogP 2.73 TPSA 126.0	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)c4ccccc4…`
ZINC1089984 ZINC	0.705	407.5 Da LogP 2.51 TPSA 65.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2cc(N3CCN(C(=S)S)CC3)c(F)cc2c…`
ZINC1775971059 ZINC	0.703	398.4 Da LogP 1.74 TPSA 106.6	✓ Ro5	✓ Clean	`N#CCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C2C…`
ZINC9550326 ZINC	0.701	485.9 Da LogP 3.79 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)CCc4cccc…`
ZINC3886912 ZINC	0.700	373.4 Da LogP 1.84 TPSA 82.8	✓ Ro5	✓ Clean	`CC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C2CC2)…`
ZINC1775971134 ZINC	0.698	386.4 Da LogP 1.42 TPSA 106.6	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)CC#N)CC3…`
ZINC503731 ZINC	0.694	290.3 Da LogP 2.29 TPSA 97.0	✓ Ro5	✓ Clean	`CCOC(=O)c1ccc(CC(=O)c2ccc(O)cc2O)o1`
ZINC95626838 ZINC	0.689	206.2 Da LogP 2.32 TPSA 59.7	✓ Ro5	✓ Clean	`CCOC(=O)c1cc2cc(O)ccc2o1`
ZINC12405021 ZINC	0.688	248.1 Da LogP -1.68 TPSA 158.4	✓ Ro5	✓ Clean	`O=C(O)[C@H]1[C@H](C(=O)O)[C@H](C(=O)O)O[C@H]1C(…`
ZINC2318885 ZINC	0.688	437.5 Da LogP 2.75 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)Cc4ccccc…`
ZINC2563982 ZINC	0.688	248.1 Da LogP -1.68 TPSA 158.4	✓ Ro5	✓ Clean	`O=C(O)[C@H]1O[C@H](C(=O)O)[C@@H](C(=O)O)[C@@H]1…`
ZINC3861122 ZINC	0.688	248.1 Da LogP -1.68 TPSA 158.4	✓ Ro5	✓ Clean	`O=C(O)[C@H]1O[C@@H](C(=O)O)[C@@H](C(=O)O)[C@H]1…`
ZINC3861123 ZINC	0.688	248.1 Da LogP -1.68 TPSA 158.4	✓ Ro5	✓ Clean	`O=C(O)[C@H]1O[C@@H](C(=O)O)[C@@H](C(=O)O)[C@@H]…`
ZINC3861124 ZINC	0.688	248.1 Da LogP -1.68 TPSA 158.4	✓ Ro5	✓ Clean	`O=C(O)[C@H]1O[C@@H](C(=O)O)[C@H](C(=O)O)[C@H]1C…`
ZINC3861125 ZINC	0.688	248.1 Da LogP -1.68 TPSA 158.4	✓ Ro5	✓ Clean	`O=C(O)[C@H]1O[C@@H](C(=O)O)[C@H](C(=O)O)[C@@H]1…`
ZINC8818330 ZINC	0.687	485.6 Da LogP 4.81 TPSA 82.8	✓ Ro5	✓ Clean	`C=CCCCCCCCCC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O…`
ZINC9550294 ZINC	0.687	483.6 Da LogP 3.69 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)CCSc4ccc…`
ZINC9550329 ZINC	0.686	493.5 Da LogP 3.46 TPSA 92.1	✓ Ro5	✓ Clean	`COc1ccc(CCC(=O)N2CCN(c3cc4c(cc3F)c(=O)c(C(=O)O)…`
ZINC2099820 ZINC	0.685	354.4 Da LogP 3.75 TPSA 97.0	✓ Ro5	✓ Clean	`CCOC(=O)c1oc2ccc(CC(=O)c3ccc(O)cc3O)cc2c1C`
ZINC1577652 ZINC	0.684	234.2 Da LogP -0.66 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](C(=O)O)[C@@H](CC(=O)O)C(=O)O`
ZINC16672028 ZINC	0.684	304.3 Da LogP 2.46 TPSA 62.5	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCCC3)cc21`
ZINC1428791 ZINC	0.683	423.4 Da LogP 2.82 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)c4ccccc4…`
ZINC13178742 ZINC	0.681	468.4 Da LogP 2.73 TPSA 126.0	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)c4cccc([…`
ZINC1894 ZINC	0.678	333.4 Da LogP 1.61 TPSA 65.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C)CC3)cc21`
ZINC26740199 ZINC	0.678	335.3 Da LogP 1.37 TPSA 86.0	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(O)CC3)cc21`
ZINC22511298 ZINC	0.677	391.4 Da LogP 2.14 TPSA 92.1	✓ Ro5	✓ Clean	`CCOC(=O)N1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3CC)C…`
ZINC3996579 ZINC	0.677	378.4 Da LogP 1.22 TPSA 91.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(N)=S)CC3)cc…`
ZINC597112 ZINC	0.677	359.4 Da LogP 2.32 TPSA 65.8	✓ Ro5	✓ Clean	`CCN1CCN(c2cc3c(cc2F)c(=O)c(C(=O)O)cn3C2CC2)CC1`
ZINC794056 ZINC	0.677	389.4 Da LogP 2.16 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)C(C)C)CC…`
ZINC9469690 ZINC	0.676	497.6 Da LogP 4.00 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)CCSc4ccc…`
ZINC16677382 ZINC	0.672	318.3 Da LogP 2.85 TPSA 62.5	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCCCC3)cc21`
ZINC2479098 ZINC	0.672	441.4 Da LogP 2.96 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)c4ccc(F)…`
ZINC686337 ZINC	0.672	441.4 Da LogP 2.96 TPSA 82.8	✓ Ro5	✓ Clean	`CCn1cc(C(=O)O)c(=O)c2cc(F)c(N3CCN(C(=O)c4ccccc4…`
ZINC9723042 ZINC	0.672	483.9 Da LogP 3.72 TPSA 82.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2cc(N3CCN(C(=O)Cc4ccccc4Cl)CC…`

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.

isocitrate lyase

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