Protein target profile

KP13_02775

Cystathionine beta-lyase metC

Genome: KpKP13 Gene: AHE42656.1 3D evidence: Experimental + ColabFold model UniProt A0A0H3GVN6

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Length 395

Pocket druggability 0.673

Direct ligand evidence 0 71 total records

Functional annotation 1 EC 9 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

Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.67. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.64. Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

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 (%): 31.902 Lower values reduce human off-target concern.
Human E-value: 4.89e-47
Gut microbiome similarity: 2.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 65.296 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: 97.13 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

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 0.673

Structure 8DUY

Pocket Pocket 2

P2Rank 0.637

Structure 8DUY

Pocket Pocket 1

ColabFold model

FPocket 0.197 · Pocket 16

P2Rank 0.526 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 132 / 4744 genomes with a hit

Prevalence 2.8%

Cross-references

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

Sequence

Primary amino-acid sequence viewer.

MADKHLDTALVNAGRSKKYTQGSVNSVIQRASSLVFDTVEAKKHATRNRANGELFYGRRGTLTHFSLQEAMCELEGGAGCALFPCGAAAVANTILAFVEQGDHVLMTNTAYEPSQDFCTKILAKLGVTTSWFDPLIGADIARLVRPETRVVFLESPGSITMEVHDVPAIVAAVRQVAPEAIIMIDNTWAAGILFKALDFGIDISIQAGTKYLIGHSDAMVGTAVANARCWPQLRENAYLMGQMLDADTAYMTSRGLRTLGVRLRQHHESSLRIAEWLAQHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLSKRLNDAELAEYLDNFSLFSMAYSWGGFESLILANQPEQIAHIRPDAEVDFSGTLIRLHIGLENVDDLQADLAAGFARIV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

4.4.1.13

Gene Ontology (GO)

GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
GO:0004121 OBSOLETE. Catalysis of the reaction: cystathionine + H2O = L-homocysteine + NH3 + pyruvate.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
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:0019346 The interconversion of homocysteine and cysteine via cystathionine. In contrast with enteric bacteria and mammals, Saccharomyces cerevisiae has two transsulfuration pathways employing two separate sets of enzymes.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0047804 Catalysis of the reaction: S-substituted L-cysteine + H2O = a thiol + NH4+ + pyruvate.
GO:0019450 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-cysteine into other compounds, including pyruvate.
GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
1	258	Gene3D	G3DSA:3.40.640.10	-
1	258	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
8	394	NCBIfam	TIGR01324	cystathionine beta-lyase
8	394	InterPro	IPR006233	Cystathionine beta-lyase, bacterial
202	216	ProSitePatterns	PS00868	Cys/Met metabolism enzymes pyridoxal-phosphate attachment site.
202	216	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
259	395	FunFam	G3DSA:3.90.1150.10:FF:000058	Cystathionine beta-lyase
1	258	FunFam	G3DSA:3.40.640.10:FF:000062	Cystathionine beta-lyase
24	393	SUPERFAMILY	SSF53383	PLP-dependent transferases
24	393	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
22	392	CDD	cd00614	CGS_like
22	392	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
1	395	PIRSF	PIRSF001434	CGS
1	395	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
3	394	PANTHER	PTHR43500	CYSTATHIONINE BETA-LYASE-RELATED
3	394	InterPro	IPR006233	Cystathionine beta-lyase, bacterial
7	391	Pfam	PF01053	Cys/Met metabolism PLP-dependent enzyme
7	391	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
259	395	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
259	395	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain

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

0.673

Likely same site as P2Rank 1 3.5 Å 14 shared residues 93% of smaller site

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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

0.637

Likely same site as FPocket 2 3.5 Å 14 shared residues 93% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.427

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Surrounding area

Site 3 P2Rank #3

0.112

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Surrounding area

Site 4 P2Rank #4

0.015

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Surrounding area

Site 5 P2Rank #5

0.015

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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

0.526

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Surrounding area

Site 2 P2Rank #2

0.365

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Surrounding area

Site 3 P2Rank #3

0.173

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Surrounding area

All structural evidence 1 experimental · 1 predicted

Structural evidence

1 + 1

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
PDB 8DUY	X-ray	1.90 Å	A,B,C,D	100.0% 1-395	PDBe RCSB PDBj File	Viewing
ColabFold KP13_02775	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.

71 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 21 records from similar proteins

Structural ligands 17 0 loaded crystals

Measured bioactivity 4 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2LM PDB via homolog 378.3 Da · LogP 1.48 · TPSA 149.5 Open detail RCSB PDB

3LM PDB via homolog Detail RCSB PDB

4LM PDB via homolog Detail RCSB PDB

AA5 PDB via homolog Detail RCSB PDB

BLP 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
2LM RCSB PDB	3AEL	Q86D28	378.3 Da LogP 1.48 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C(\CCSC)/C(=O)O)O`
3LM RCSB PDB	3AEO	Q86D28	378.3 Da LogP 1.13 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN/C(=C/CSC)/C(=O)O)O`
4LM RCSB PDB	3AEP	Q86D28	330.2 Da LogP 1.11 TPSA 149.5	✓ Ro5	✓ Clean	`C/C=C(\C(=O)O)/N=C/c1c(cnc(c1O)C)COP(=O)(O)O`
AA5 RCSB PDB	3AEJ	Q86D28	378.3 Da LogP 1.33 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C=N[C@@H](CCSC)C(=O)O)O`
BLP RCSB PDB	2GQN	P06721	469.3 Da LogP 0.16 TPSA 213.2	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNNC(=O)CNC(=O)c2ccccc…`
ECX RCSB PDB	3JW9	Q84AR1	149.2 Da LogP 0.15 TPSA 63.3	✓ Ro5	✓ Clean	`CCSC[C@@H](C(=O)O)N`
IN5 RCSB PDB	4ITX	P06721	356.2 Da LogP 0.32 TPSA 169.4	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](C)P(=O)(O)O)O`
LCS RCSB PDB	4OMA	Q84AR1	331.2 Da LogP -0.29 TPSA 150.6	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C/2\CONC2=O)O`
MEE RCSB PDB	3AEP	Q86D28	48.1 Da LogP 0.55 TPSA 0.0	✓ Ro5	✓ Clean	`CS`
MPJ RCSB PDB	3JWA	Q84AR1	169.2 Da LogP 0.49 TPSA 63.3	✓ Ro5	✓ Clean	`CSCC[C@H](N)[P@H](=O)O`
NLE RCSB PDB	5M3Z	A0A0A5P8W7	131.2 Da LogP 0.59 TPSA 63.3	✓ Ro5	✓ Clean	`CCCC[C@@H](C(=O)O)N`
P3F RCSB PDB	2FQ6	P06721	490.3 Da LogP 1.60 TPSA 170.4	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\NC(=O)CNC(=O)c2cc…`
PLG RCSB PDB	4HF8	Q84AR1	306.2 Da LogP -0.12 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNCC(=O)O)O`
PPG RCSB PDB	1CL2	P06721	389.3 Da LogP 0.22 TPSA 184.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C(\C=C\OCCN)/C(=O)…`
PPJ RCSB PDB	1E5E	A2FEV4	362.3 Da LogP 0.35 TPSA 169.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\[C@@H](C[C@H](C)O…`
PY6 RCSB PDB	5M3Z	A0A0A5P8W7	362.3 Da LogP 1.44 TPSA 149.2	✓ Ro5	✓ Clean	`CCCC[C@@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O`
PZP RCSB PDB	3MKJ	Q84AR1	246.2 Da LogP 0.70 TPSA 123.7	✓ Ro5	✓ Clean	`[H]/N=C/c1c(cnc(c1O)C)COP(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL219268 ChEMBL	P06721	7.10 ~79.4 nM	261.2 Da LogP 0.43 TPSA 84.2	✓ Ro5	✓ Clean	`NNC(=O)CNC(=O)c1ccccc1C(F)(F)F`
CHEMBL218090 ChEMBL	P06721	6.55 ~281.8 nM	285.2 Da LogP 3.67 TPSA 29.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)C(C(F)(F)F)C(F)(F)F`
CHEMBL220764 ChEMBL	P06721	6.28 ~524.8 nM	498.2 Da LogP 4.83 TPSA 145.2	✓ Ro5	✓ Clean	`O=C(OCc1ccccc1Br)c1cc([N+](=O)[O-])cc2c1-c1ccc(…`
CHEMBL221848 ChEMBL	P06721	6.19 ~645.7 nM	277.2 Da LogP -0.17 TPSA 93.4	✓ Ro5	✓ Clean	`COc1c(F)cc(C(=O)NCC(=O)NN)c(F)c1F`

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
ZINC2035155 ZINC	0.826	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](N)C(=O)O`
ZINC22148777 ZINC	0.703	247.2 Da LogP 1.52 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)c1ccccc1C(F)(F)F`
ZINC2590069 ZINC	0.694	322.3 Da LogP 4.28 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@H](Nc1ccccc1C)C(F)(F)F`
ZINC2590070 ZINC	0.694	322.3 Da LogP 4.28 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@@H](Nc1ccccc1C)C(F)(F)F`
ZINC1532514 ZINC	0.681	247.1 Da LogP 0.52 TPSA 117.0	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C=O)c1O`
ZINC3138368 ZINC	0.676	299.2 Da LogP 3.98 TPSA 29.1	✓ Ro5	✓ Clean	`Cc1cccc(C)c1NC(=O)C(C(F)(F)F)C(F)(F)F`
ZINC3188764 ZINC	0.676	339.2 Da LogP 4.38 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1C(F)(F)F)C(C(F)(F)F)C(F)(F)F`
ZINC2962475 ZINC	0.667	404.3 Da LogP 3.88 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)c1ccccc1C(F)(F)F)c1ccccc1C(F)(F)F`
ZINC2185058 ZINC	0.657	397.1 Da LogP 3.97 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1I)C(C(F)(F)F)C(F)(F)F`
ZINC3188827 ZINC	0.657	350.1 Da LogP 4.13 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1Br)C(C(F)(F)F)C(F)(F)F`
ZINC2114966 ZINC	0.643	332.2 Da LogP 0.99 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(/C=N/CCCC(=O)O)c1O`
ZINC19261983 ZINC	0.641	232.2 Da LogP 1.39 TPSA 55.1	✓ Ro5	✓ Clean	`NCCNC(=O)c1ccccc1C(F)(F)F`
ZINC5978748 ZINC	0.641	231.2 Da LogP 2.85 TPSA 29.1	✓ Ro5	✓ Clean	`CCCNC(=O)c1ccccc1C(F)(F)F`
ZINC1674993 ZINC	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSCCSCC[C@H](N)C(=O)O)C(=O)O`
ZINC1674994 ZINC	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSCCSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1674996 ZINC	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCSCCSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC100177544 ZINC	0.639	385.3 Da LogP 3.67 TPSA 145.2	✓ Ro5	✓ Clean	`CCCCOC(=O)c1cc([N+](=O)[O-])cc2c1-c1ccc([N+](=O…`
ZINC2317717 ZINC	0.639	315.2 Da LogP 3.06 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1NC(=O)C(C(F)(F)F)C(F)(F)F`
ZINC4837861 ZINC	0.632	343.3 Da LogP 2.50 TPSA 145.2	✓ Ro5	✓ Clean	`COC(=O)c1cc([N+](=O)[O-])cc2c1-c1ccc([N+](=O)[O…`
ZINC57160064 ZINC	0.632	271.2 Da LogP 3.00 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(NCC(F)(F)F)c1ccccc1C(F)(F)F`
ZINC103767685 ZINC	0.629	399.4 Da LogP 3.91 TPSA 145.2	✓ Ro5	✓ Clean	`CC(C)CCOC(=O)c1cc([N+](=O)[O-])cc2c1-c1ccc([N+]…`
ZINC25436796 ZINC	0.628	337.3 Da LogP 3.18 TPSA 55.4	✓ Ro5	✓ Clean	`O=C(CNC(=O)c1ccccc1C(F)(F)F)OCc1ccccc1`
ZINC9455654 ZINC	0.622	350.3 Da LogP 3.64 TPSA 58.2	✓ Ro5	✓ Clean	`CCc1ccccc1NC(=O)CNC(=O)c1ccccc1C(F)(F)F`
ZINC3150756 ZINC	0.622	321.2 Da LogP 4.52 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1cccc2ccccc12)C(C(F)(F)F)C(F)(F)F`
ZINC178267905 ZINC	0.619	343.4 Da LogP 2.89 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@@H](C)N1CCN([C@@H](C)C(F)(F)F…`
ZINC178267918 ZINC	0.619	343.4 Da LogP 2.89 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@H](C)N1CCN([C@@H](C)C(F)(F)F)…`
ZINC178267933 ZINC	0.619	343.4 Da LogP 2.89 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@@H](C)N1CCN([C@H](C)C(F)(F)F)…`
ZINC178267948 ZINC	0.619	343.4 Da LogP 2.89 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@H](C)N1CCN([C@H](C)C(F)(F)F)C…`
ZINC126350 ZINC	0.618	203.2 Da LogP 2.50 TPSA 29.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)C(F)(F)F`
ZINC2754661 ZINC	0.618	368.3 Da LogP 4.15 TPSA 58.2	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)C(F)(F)C(F)(F)C(=O)Nc1ccccc1C`
ZINC1529407 ZINC	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSC[C@@H](N)C(=O)O)C(=O)O`
ZINC1532680 ZINC	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSC[C@H](N)C(=O)O)C(=O)O`
ZINC1708207 ZINC	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCSC[C@H](N)C(=O)O)C(=O)O`
ZINC1708208 ZINC	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC28210975 ZINC	0.615	233.2 Da LogP 1.43 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(NCCO)c1ccccc1C(F)(F)F`
ZINC1605257 ZINC	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CCSC)C(=O)O`
ZINC1605258 ZINC	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](NC(=O)[C@H](N)CCSC)C(=O)O`
ZINC1605259 ZINC	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](CCSC)C(=O)O`
ZINC1605260 ZINC	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@H](CCSC)C(=O)O`
ZINC2384801 ZINC	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC242824 ZINC	0.613	240.3 Da LogP 3.95 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)Nc1ccccc1C`
ZINC4556875 ZINC	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC4556876 ZINC	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC4556877 ZINC	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC6218328 ZINC	0.611	294.3 Da LogP 4.66 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)Nc1ccccc1C(F)(F)F`
ZINC3339684 ZINC	0.609	350.3 Da LogP 3.69 TPSA 58.2	✓ Ro5	✓ Clean	`Cc1cccc(NC(=O)CNC(=O)c2ccccc2C(F)(F)F)c1C`
ZINC6993964 ZINC	0.609	376.3 Da LogP 3.49 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CNC(=O)c1ccccc1C(F)(F)F)Nc1ccc(F)c(F)c1F`
ZINC41636241 ZINC	0.600	227.2 Da LogP 2.07 TPSA 29.1	✓ Ro5	✓ Clean	`C#CCNC(=O)c1ccccc1C(F)(F)F`
ZINC450254 ZINC	0.600	279.3 Da LogP 3.64 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)c1ccccc1C(F)(F)F`
ZINC4761004 ZINC	0.600	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCC[C@H](N)C(=O)N[C@@H](C)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.