Protein target profile

VK055_0671

catalase/peroxidase HPI

Genome: KpATCC43816 Gene: katG AIK79294.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 4 reactions UniProt A0A0H3GQ65

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Length 725

Pocket druggability 0.988

Metabolic reactions 4

Chokepoint Yes

Direct ligand evidence 0 56 total records

Functional annotation 1 EC 8 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. Central metabolic position More central than 90.8% of genes in this genome. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Second pocket predictor agrees P2Rank predicted binding-site probability 0.98. 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: 2.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 82.759 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.22 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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 0.988

Structure A0A0H3GQ65

Pocket Pocket 2

P2Rank 0.985

Structure A0A0H3GQ65

Pocket Pocket 1

ColabFold model

FPocket 0.951 · Pocket 1

P2Rank 0.986 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 128 / 4744 genomes with a hit

Prevalence 2.7%

Cross-references

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

Sequence

UniProt A0A0H3GQ65

Pathways

BioCyc CATAL-RXN[CCO-CYTOSOL]-HYDROGEN-PEROXIDE//WATER/OXYGEN-MOLECULE.54. BioCyc CATAL-RXN[CCO-PERI-BAC]-HYDROGEN-PEROXIDE//WATER/OXYGEN-MOLECULE.55. BioCyc RXN66-1 KEGG R00602 BioCyc RXN-14189

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, more central than 90.8% of genes in this genome, no human homolog detected.

Relative network centrality 90.8% more central than 90.8% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSTSNDPSNNASAGKCPFHAETPKQSAGSGTANRDWWPNQLRVDLLNQHSNRSNPLGENFNYREEFKKLDYSALKADLRALLTDSQEWWPADWGSYIGLFIRMAWHGAGTYRTVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLYMLAGNVALENAGFRTFGFGAGREDVWEPDLDVDWGDEKEWLAHRHPESLAKQAIGATEMGLIYVNPEGPNASGEPLSAAAAIRATFGNMAMDDEEIVALIAGGHTLGKTHGAAETSHVGAEPEAAPLEAQGLGWHSSYGSGAGADAITSGLEVVWTQTPTQWSNYFFENLFKYEWVQTRSPAGAIQFEAKDAPEIIPDPFNPEKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKSRYLGPEVPKEDLIWQDPLPAATHQPSAEDIASLKSAIAGAGLSVSELVSVAWASASTFRGGDKRGGANGARLALAPQKDWPVNAIASRVLPTLQAIQRASGKASLADIIVLAGVVGVEQAAAAAGVSVNVPFTPGRVDALPEQTDVESFDLLQPLADGFRNYRRIEGGVSTETLLIDKAQQLTLTAPEMTVLVGGLRVLGANYDGSKHGVFTDRVGVLSNDFFVNLLDMATVWKAADDNAELFTGSDRKTGEAKYSATRVDLVFGSNSVLRALAEVYACADGQQKLVHDFVAAWTKVMNLDRFDL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1.11.1.21

Gene Ontology (GO)

GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
GO:0004096 Catalysis of the reaction: 2 H2O2 = O2 + 2 H2O.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0004601 Catalysis of the reaction: a reduced substrate + ROOH = an oxidized substrate + ROH + H2O.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046872 Binding to a metal ion.
GO:0070301 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
GO:0042744 The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

45 records

Show feature table

Start	End	DB	Term	Name
435	725	Gene3D	G3DSA:1.10.520.10	-
435	725	SUPERFAMILY	SSF48113	Heme-dependent peroxidases
435	725	InterPro	IPR010255	Haem peroxidase superfamily
1	33	MobiDBLite	mobidb-lite	consensus disorder prediction
32	430	Gene3D	G3DSA:1.10.520.10	-
436	722	CDD	cd08200	catalase_peroxidase_2
318	333	PRINTS	PR00458	Haem peroxidase superfamily signature
318	333	InterPro	IPR002016	Haem peroxidase
175	187	PRINTS	PR00458	Haem peroxidase superfamily signature
175	187	InterPro	IPR002016	Haem peroxidase
157	174	PRINTS	PR00458	Haem peroxidase superfamily signature
157	174	InterPro	IPR002016	Haem peroxidase
259	274	PRINTS	PR00458	Haem peroxidase superfamily signature
259	274	InterPro	IPR002016	Haem peroxidase
97	111	PRINTS	PR00458	Haem peroxidase superfamily signature
97	111	InterPro	IPR002016	Haem peroxidase
198	395	Gene3D	G3DSA:1.10.420.10	Peroxidase, domain 2
578	701	FunFam	G3DSA:1.10.420.10:FF:000004	Catalase-peroxidase
11	725	Hamap	MF_01961	Catalase-peroxidase [katG].
11	725	InterPro	IPR000763	Catalase-peroxidase haem
403	698	Pfam	PF00141	Peroxidase
403	698	InterPro	IPR002016	Haem peroxidase
83	396	Pfam	PF00141	Peroxidase
83	396	InterPro	IPR002016	Haem peroxidase
24	725	NCBIfam	TIGR00198	catalase/peroxidase HPI
24	725	InterPro	IPR000763	Catalase-peroxidase haem
33	221	FunFam	G3DSA:1.10.520.10:FF:000002	Catalase-peroxidase
29	429	SUPERFAMILY	SSF48113	Heme-dependent peroxidases
29	429	InterPro	IPR010255	Haem peroxidase superfamily
574	701	Gene3D	G3DSA:1.10.420.10	Peroxidase, domain 2
139	424	ProSiteProfiles	PS50873	Plant heme peroxidase family profile.
139	424	InterPro	IPR002016	Haem peroxidase
1	725	PANTHER	PTHR30555	HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE
1	725	InterPro	IPR000763	Catalase-peroxidase haem
479	505	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
479	505	InterPro	IPR000763	Catalase-peroxidase haem
59	72	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
59	72	InterPro	IPR000763	Catalase-peroxidase haem
267	290	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
267	290	InterPro	IPR000763	Catalase-peroxidase haem
74	99	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
74	99	InterPro	IPR000763	Catalase-peroxidase haem
33	55	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
33	55	InterPro	IPR000763	Catalase-peroxidase haem
198	395	FunFam	G3DSA:1.10.420.10:FF:000002	Catalase-peroxidase

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 · FPocket

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

Site 1 FPocket #2

0.988

Likely same site as P2Rank 1 1.1 Å 36 shared residues 92% of smaller site

Unusual size

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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

0.985

Likely same site as FPocket 2 1.1 Å 36 shared residues 92% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.272

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Surrounding area

Site 3 P2Rank #3

0.234

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Surrounding area

Site 4 P2Rank #4

0.214

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Surrounding area

Site 5 P2Rank #5

0.199

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Surrounding area

Residue sets

UniProt: Active site:106-106 Proton acceptor

UniProt: Binding site:267-267 axial binding residue

UniProt: Site:102-102 Transition state stabilizer

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.986

Likely same site as FPocket 1 0.6 Å 38 shared residues 95% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.282

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Surrounding area

Site 3 P2Rank #3

0.159

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Surrounding area

Site 4 P2Rank #4

0.125

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Surrounding area

Site 5 P2Rank #5

0.042

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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_A0A0H3GQ65	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0671	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

DDJ PDB via homolog 244.3 Da · LogP 2.54 · TPSA 70.5 Open detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

NIZ PDB via homolog Detail RCSB PDB

O PDB via homolog Detail RCSB PDB

OXY 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
DDJ RCSB PDB	3VLJ	O59651	244.3 Da LogP 2.54 TPSA 70.5	✓ Ro5	✓ Clean	`COc1cc(ccc1N)c2ccc(c(c2)OC)N`
FLC RCSB PDB	5JHX	A4QUT2	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
NIZ RCSB PDB	3WXO	Q31MN3	137.1 Da LogP -0.31 TPSA 68.0	✓ Ro5	✓ Clean	`c1cnccc1C(=O)NN`
O RCSB PDB	5SW6	Q3JNW6	18.0 Da LogP -0.82 TPSA 31.5	✓ Ro5	✓ Clean	`O`
OXY RCSB PDB	5KQ6	Q3JNW6	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`
SHA RCSB PDB	3VLL	O59651	153.1 Da LogP 0.51 TPSA 69.6	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)NO)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
ZINC56395 ZINC	1.000	244.3 Da LogP 2.54 TPSA 70.5	✓ Ro5	✓ Clean	`COc1cc(-c2ccc(N)c(OC)c2)ccc1N`
ZINC83315 ZINC	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC83317 ZINC	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC403598 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC403599 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC4899521 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC57505 ZINC	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC2566035 ZINC	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC6864822 ZINC	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC1690614 ZINC	0.743	233.2 Da LogP 1.50 TPSA 90.4	✓ Ro5	✓ Clean	`O=C(O)C(Cc1c[nH]c2ccccc12)C(=O)O`
ZINC39351856 ZINC	0.741	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC1637998 ZINC	0.732	261.3 Da LogP 0.24 TPSA 108.2	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)O`
ZINC2384992 ZINC	0.732	261.3 Da LogP 0.24 TPSA 108.2	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)O`
ZINC264238 ZINC	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC264242 ZINC	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC34781219 ZINC	0.718	218.3 Da LogP 1.21 TPSA 68.1	✓ Ro5	✓ Clean	`COC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC34781220 ZINC	0.718	218.3 Da LogP 1.21 TPSA 68.1	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC1557161 ZINC	0.714	390.4 Da LogP 2.33 TPSA 124.0	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](Cc1c[nH]…`
ZINC1557164 ZINC	0.714	390.4 Da LogP 2.33 TPSA 124.0	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](Cc1c[nH]c2…`
ZINC193616 ZINC	0.707	279.3 Da LogP 2.68 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)Nc1ccccc1`
ZINC2497690 ZINC	0.707	279.3 Da LogP 2.68 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)Nc1ccccc1`
ZINC874230 ZINC	0.707	231.3 Da LogP 1.17 TPSA 70.9	✓ Ro5	✓ Clean	`CCNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC874233 ZINC	0.707	231.3 Da LogP 1.17 TPSA 70.9	✓ Ro5	✓ Clean	`CCNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC39098 ZINC	0.703	205.2 Da LogP 1.16 TPSA 73.3	✓ Ro5	✓ Clean	`O=C(O)[C@@H](O)Cc1c[nH]c2ccccc12`
ZINC39099 ZINC	0.703	205.2 Da LogP 1.16 TPSA 73.3	✓ Ro5	✓ Clean	`O=C(O)[C@H](O)Cc1c[nH]c2ccccc12`
ZINC83138991 ZINC	0.703	268.1 Da LogP 2.56 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Br)Cc1c[nH]c2ccccc12`
ZINC34307123 ZINC	0.700	217.3 Da LogP 0.78 TPSA 70.9	✓ Ro5	✓ Clean	`CNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC34482181 ZINC	0.700	217.3 Da LogP 0.78 TPSA 70.9	✓ Ro5	✓ Clean	`CNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC52968847 ZINC	0.700	232.3 Da LogP 1.60 TPSA 68.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC53943847 ZINC	0.700	232.3 Da LogP 1.60 TPSA 68.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC1638007 ZINC	0.698	275.3 Da LogP 0.63 TPSA 108.2	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC2453187 ZINC	0.696	257.2 Da LogP 1.67 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(NC(=O)c1ccccc1O)c1ccccc1O`
ZINC4240327 ZINC	0.692	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)Cc1c[nH]c2ccccc12`
ZINC44544883 ZINC	0.692	218.3 Da LogP 1.37 TPSA 79.1	✓ Ro5	✓ Clean	`NC[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC44544886 ZINC	0.692	218.3 Da LogP 1.37 TPSA 79.1	✓ Ro5	✓ Clean	`NC[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC4521117 ZINC	0.692	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)Cc1c[nH]c2ccccc12`
ZINC2134508 ZINC	0.690	245.3 Da LogP 1.56 TPSA 70.9	✓ Ro5	✓ Clean	`CCCNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC2134510 ZINC	0.690	245.3 Da LogP 1.56 TPSA 70.9	✓ Ro5	✓ Clean	`CCCNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC2559489 ZINC	0.690	260.3 Da LogP -0.36 TPSA 114.0	✓ Ro5	✓ Clean	`NC(=O)CNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC32333 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC34319489 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC34319490 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC178387 ZINC	0.684	203.2 Da LogP 2.43 TPSA 53.1	✓ Ro5	✓ Clean	`C[C@H](Cc1c[nH]c2ccccc12)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.