KpATCC43816 Protein target profile

2-isopropylmalate synthase

Accession: VK055_2493

Gene: leuA AIK81090.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GJ80

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Length 523

Pocket druggability (P2Rank · AlphaFold DB model) 0.777

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 8 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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

Main supporting evidence

Central metabolic position More central than 96.1% of genes in this genome. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.78. Structure available AlphaFold DB model + ColabFold model 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 (%): 25.0 Lower values reduce human off-target concern.
Human E-value: 5.45e-07
Gut microbiome similarity: 7.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 66.996 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 88.55 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) 0.777

Structure A0A0H3GJ80

Pocket Pocket 1

Druggability (FPocket) 0.206

Structure A0A0H3GJ80

Pocket Pocket 38

ColabFold model

P2Rank 0.697 · Pocket 1

FPocket 0.285 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 344 / 4744 genomes with a hit

Prevalence 7.3%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 96.1% of genes in this genome.

Relative network centrality 96.1% more central than 96.1% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSQQVIIFDTTLRDGEQALQASLSVKEKLQIALALERMGVDVMEVGFPVSSPGDFESVQTIARTIKNSRVCALARCVEKDIDVAAESLKVAEAFRIHTFIATSPMHIATKLRSTLDEVIERAIYMVKRARNYTDDVEFSCEDAGRTPIADLARVVEAAINAGATTINIPDTVGYTMPFEYANIISGLYDRVPNIDKAIISVHTHDDLGIAVGNALAAVHAGARQVEGAMNGIGERAGNCALEEVIMAIKVRKDIMNVHTNINHHEIWRTSQTVSQICNMPIPANKAIVGTGAFAHSSGIHQDGVLKNRENYEIMTPESIGLNQVQLNLTSRSGRAAVKHRMEEMGYQESDYNLDHLYDAFLKLADKKGQVFDYDLEALAFINKQQEEPEHFRLDYFNVQSGSSDIATASIKLVCGDEIKTEAANGNGPVDAIYQAINRVTDYNIELVKYGLSAKGHGKDALGQVDIVVDYNGRRFHGVGLATDIVESSAKAMVHVLNNIWRAAEVEKELQRKAQNKENNKETV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.3.3.13

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:0003852 Catalysis of the reaction: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H+.
GO:0009098 The chemical reactions and pathways resulting in the formation of L-leucine, 2-amino-4-methylpentanoic acid.
GO:0019752 The chemical reactions and pathways involving carboxylic acids, any organic acid containing one or more carboxyl (COOH) groups or anions (COO-).
GO:0046912 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor), with the acyl group being converted into alkyl on transfer.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0003985 Catalysis of the reaction: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
GO:0030145 Binding to a manganese ion (Mn).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
502	523	Coils	Coil	Coil
280	392	Gene3D	G3DSA:1.10.238.260	-
4	273	Pfam	PF00682	HMGL-like
4	273	InterPro	IPR000891	Pyruvate carboxyltransferase
1	279	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	279	InterPro	IPR013785	Aldolase-type TIM barrel
394	500	FunFam	G3DSA:3.30.160.270:FF:000001	2-isopropylmalate synthase
1	290	SUPERFAMILY	SSF51569	Aldolase
2	509	Hamap	MF_01025	2-isopropylmalate synthase [leuA].
2	509	InterPro	IPR005671	2-isopropylmalate synthase, bacterial-type
1	279	FunFam	G3DSA:3.20.20.70:FF:000010	2-isopropylmalate synthase
12	28	ProSitePatterns	PS00815	Alpha-isopropylmalate and homocitrate synthases signature 1.
12	28	InterPro	IPR002034	Alpha-isopropylmalate/homocitrate synthase, conserved site
7	275	CDD	cd07940	DRE_TIM_IPMS
393	501	Gene3D	G3DSA:3.30.160.270	-
393	501	InterPro	IPR036230	2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain superfamily
3	501	PANTHER	PTHR10277	HOMOCITRATE SYNTHASE-RELATED
199	212	ProSitePatterns	PS00816	Alpha-isopropylmalate and homocitrate synthases signature 2.
199	212	InterPro	IPR002034	Alpha-isopropylmalate/homocitrate synthase, conserved site
280	393	FunFam	G3DSA:1.10.238.260:FF:000001	2-isopropylmalate synthase
391	499	SUPERFAMILY	SSF110921	2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain
391	499	InterPro	IPR036230	2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain superfamily
5	267	ProSiteProfiles	PS50991	Pyruvate carboxyltransferase domain.
5	267	InterPro	IPR000891	Pyruvate carboxyltransferase
369	499	Pfam	PF08502	LeuA allosteric (dimerisation) domain
369	499	InterPro	IPR013709	2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain
369	500	SMART	SM00917	LeuA_dimer_2
369	500	InterPro	IPR013709	2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain
4	497	NCBIfam	TIGR00973	2-isopropylmalate synthase
4	497	InterPro	IPR005671	2-isopropylmalate synthase, bacterial-type

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

0.777

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Surrounding area

Pocket 2 P2Rank #2

0.266

Likely same site as FPocket 38 3.7 Å 15 shared residues 88% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.103

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Surrounding area

Pocket 4 P2Rank #4

0.087

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Surrounding area

Pocket 5 P2Rank #5

0.064

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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 #38

0.206 Unusual size

Likely same site as P2Rank 2 3.7 Å 15 shared residues 88% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:14-14

UniProt: Binding site:202-202

UniProt: Binding site:204-204

UniProt: Binding site:238-238

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.697

Likely same site as FPocket 3 1.1 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.24

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Surrounding area

Pocket 3 P2Rank #3

0.149

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Surrounding area

Pocket 4 P2Rank #4

0.075

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Surrounding area

Pocket 5 P2Rank #5

0.062

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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_A0A0H3GJ80	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2493	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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 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

HCA PDB via homolog Detail RCSB PDB

KIV PDB via homolog Detail RCSB PDB

KMT PDB via homolog Detail RCSB PDB

MLI 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	2ZTJ	O87198	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
HCA RCSB PDB	2ZTK	O87198	206.1 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`C(C[C@@](CC(=O)O)(C(=O)O)O)C(=O)O`
KIV RCSB PDB	4OV4	B0SN40	116.1 Da LogP 0.30 TPSA 54.4	✓ Ro5	✓ Clean	`CC(C)C(=O)C(=O)O`
KMT RCSB PDB	6E1J	C5J4P1	148.2 Da LogP 0.39 TPSA 54.4	✓ Ro5	✓ Clean	`CSCCC(=O)C(=O)O`
MLI RCSB PDB	3BLE	Q8F3Q1	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
PYR RCSB PDB	3BLF	Q8F3Q1	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
VPM RCSB PDB	4OV9	B0SN40	176.2 Da LogP -0.07 TPSA 94.8	✓ Ro5	✓ Clean	`CC(C)[C@@](CC(=O)O)(C(=O)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).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC2572371 ZINC	0.680	206.1 Da LogP -1.00 TPSA 132.1	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)[C@@](O)(CC(=O)O)C(=O)O`
ZINC2572383 ZINC	0.680	206.1 Da LogP -1.00 TPSA 132.1	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@@](O)(CC(=O)O)C(=O)O`
ZINC3869734 ZINC	0.680	206.1 Da LogP -1.00 TPSA 132.1	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@](O)(CC(=O)O)C(=O)O`
ZINC901307 ZINC	0.680	206.1 Da LogP -1.00 TPSA 132.1	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)[C@](O)(CC(=O)O)C(=O)O`
ZINC2384798 ZINC	0.607	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC146315135 ZINC	0.593	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.593	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC2391059 ZINC	0.586	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@H](C(=O)O)[C@@H](C)CC`
ZINC40472549 ZINC	0.586	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@@H](C(=O)O)[C@@H](C)…`
ZINC40490721 ZINC	0.586	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](NC(=O)[C@@H](N)[C@H](C)CC)C(=O…`
ZINC5909388 ZINC	0.586	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](NC(=O)[C@@H](N)[C@H](C)CC)C(=O)O`
ZINC1726452 ZINC	0.571	220.2 Da LogP -0.61 TPSA 132.1	✓ Ro5	✓ Clean	`CC[C@@H](C(=O)O)[C@@](O)(CC(=O)O)C(=O)O`
ZINC1726453 ZINC	0.571	220.2 Da LogP -0.61 TPSA 132.1	✓ Ro5	✓ Clean	`CC[C@H](C(=O)O)[C@@](O)(CC(=O)O)C(=O)O`
ZINC1726454 ZINC	0.571	220.2 Da LogP -0.61 TPSA 132.1	✓ Ro5	✓ Clean	`CC[C@@H](C(=O)O)[C@](O)(CC(=O)O)C(=O)O`
ZINC1726455 ZINC	0.571	220.2 Da LogP -0.61 TPSA 132.1	✓ Ro5	✓ Clean	`CC[C@H](C(=O)O)[C@](O)(CC(=O)O)C(=O)O`
ZINC4899467 ZINC	0.567	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC5662848 ZINC	0.567	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC5662849 ZINC	0.567	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC5662850 ZINC	0.567	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC3634656 ZINC	0.556	210.1 Da LogP -1.30 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)C[C@](O)(C(=O)O)[C@H](F)C(=O)O`
ZINC3634658 ZINC	0.556	210.1 Da LogP -1.30 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)C[C@@](O)(C(=O)O)[C@H](F)C(=O)O`
ZINC3634659 ZINC	0.556	210.1 Da LogP -1.30 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)C[C@](O)(C(=O)O)[C@@H](F)C(=O)O`
ZINC3634661 ZINC	0.556	210.1 Da LogP -1.30 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)C[C@@](O)(C(=O)O)[C@@H](F)C(=O)O`
ZINC255963942 ZINC	0.548	357.5 Da LogP 1.51 TPSA 121.5	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@H](C(=O)N[C@H](C(=O)…`
ZINC255963943 ZINC	0.548	357.5 Da LogP 1.51 TPSA 121.5	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@H](C(=O)N[C@H](C(=O)…`
ZINC2560984 ZINC	0.548	246.3 Da LogP -0.60 TPSA 129.7	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)N[C@@H](CC(=O)O)C(=O)O`
ZINC2575119 ZINC	0.548	218.3 Da LogP -1.08 TPSA 112.7	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@@H](CO)C(=O)O`
ZINC39831468 ZINC	0.548	357.5 Da LogP 1.51 TPSA 121.5	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@H](C(=O)N[C@H](C(=O)…`
ZINC4762961 ZINC	0.548	357.5 Da LogP 1.51 TPSA 121.5	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@H](C(=O)N[C@H](C(=O)…`
ZINC13529436 ZINC	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N1CCCCCC1`
ZINC1726446 ZINC	0.533	234.2 Da LogP -0.22 TPSA 132.1	✓ Ro5	✓ Clean	`CCC[C@@H](C(=O)O)[C@@](O)(CC(=O)O)C(=O)O`
ZINC1726447 ZINC	0.533	234.2 Da LogP -0.22 TPSA 132.1	✓ Ro5	✓ Clean	`CCC[C@H](C(=O)O)[C@@](O)(CC(=O)O)C(=O)O`
ZINC1726448 ZINC	0.533	234.2 Da LogP -0.22 TPSA 132.1	✓ Ro5	✓ Clean	`CCC[C@@H](C(=O)O)[C@](O)(CC(=O)O)C(=O)O`
ZINC1726449 ZINC	0.533	234.2 Da LogP -0.22 TPSA 132.1	✓ Ro5	✓ Clean	`CCC[C@H](C(=O)O)[C@](O)(CC(=O)O)C(=O)O`
ZINC19502834 ZINC	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)N1CCCCCC1`
ZINC19502836 ZINC	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](N)C(=O)N1CCCCCC1`
ZINC19502838 ZINC	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@H](N)C(=O)N1CCCCCC1`
ZINC13508097 ZINC	0.531	234.3 Da LogP -0.14 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@@H](CS)C(=O)O`
ZINC2556613 ZINC	0.531	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)O`
ZINC11959312 ZINC	0.516	213.3 Da LogP 0.13 TPSA 49.6	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@H](N)C(=O)N1CCN(C)CC1`
ZINC11959315 ZINC	0.516	213.3 Da LogP 0.13 TPSA 49.6	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N1CCN(C)CC1`
ZINC19504598 ZINC	0.516	213.3 Da LogP 0.13 TPSA 49.6	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)N1CCN(C)CC1`
ZINC19504599 ZINC	0.516	213.3 Da LogP 0.13 TPSA 49.6	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](N)C(=O)N1CCN(C)CC1`
ZINC2390958 ZINC	0.516	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](NC(=O)[C@@H](N)C(C)C)C(=O)O`
ZINC40472548 ZINC	0.516	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@@H](NC(=O)[C@@H](N)C(C)C)C(=O)O`
ZINC8577168 ZINC	0.516	230.3 Da LogP 0.59 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](NC(=O)[C@@H](N)C(C)C)C(=O)O`
ZINC2522618 ZINC	0.515	245.3 Da LogP -1.20 TPSA 135.5	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)O`
ZINC3593496 ZINC	0.500	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.500	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC8577157 ZINC	0.500	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](NC(=O)[C@H](C)N)C(=O)O`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.

Cross-references

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

Sequence

UniProt A0A0H3GJ80

Pathways

KEGG R01213 BioCyc 2-ISOPROPYLMALATESYN-RXN