KpATCC43816 Protein target profile

cystathionine beta-lyase

Accession: VK055_0773

Gene: metC AIK79396.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 28 reactions UniProt A0A0C7KER1

Export view

Length 401

Pocket druggability (P2Rank · AlphaFold DB model) 0.856

Metabolic reactions 28

Chokepoint No

Direct ligand evidence 0 68 total records

Functional annotation 1 EC 7 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

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

Main supporting evidence

Central metabolic position More central than 91.3% of genes in this genome. Second pocket predictor agrees P2Rank predicted binding-site probability 0.86. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 12 structural and 6 bioactivity records.

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 (%): 34.897 Lower values reduce human off-target concern.
Human E-value: 2.13e-51
Gut microbiome similarity: 0.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 43.236 Higher values support similarity to known essential genes.
DEG E-value: 3.41e-109 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.2 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) 0.856

Structure A0A0C7KER1

Pocket Pocket 1

Druggability (FPocket) 0.535

Structure A0A0C7KER1

Pocket Pocket 21

ColabFold model

P2Rank 0.889 · Pocket 1

FPocket 0.618 · Pocket 7

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 4 / 4744 genomes with a hit

Prevalence 0.1%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 91.3% of genes in this genome.

Relative network centrality 91.3% more central than 91.3% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTNHSFDNQMSPETYLCHGPFDPEVFGGVVNPPVYHASTVIFKNCKELNERHQALFEDAEDEVMYYGRFGTPITFAVQKALAELEGGYRSLLLPTGLAACTSALLALVKSGDHILVSSSVYGPTRGFVNNVLAKMGVSATFFDPTIGDGIGQLFQENTTVVFTESPGSQTFDIQDIPAITRVAHAHNAKVIIDNTWATPLFFKPFEHGVDVSVHAATKYIVGHSDAQMGLITTNKETWLAIRRFIYLFGLHAAPDDVYLAQRGLRTMSLRLGRHQDSALKIAKWFEEREEVEQVLHPALPSCPGHEIWKRDFTGSSGLFSVVLKPHYSKESVEKFIDSLQYFGIGFSWGGFESLAIPFNPRKDRPEYHWPYEGHSFRLQIGLEDPVDLVRDLDQALRHLKG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

4.4.1.8

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: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: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:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
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.

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	400	PIRSF	PIRSF001434	CGS
1	400	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
32	397	SUPERFAMILY	SSF53383	PLP-dependent transferases
32	397	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
21	396	Pfam	PF01053	Cys/Met metabolism PLP-dependent enzyme
21	396	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
210	224	ProSitePatterns	PS00868	Cys/Met metabolism enzymes pyridoxal-phosphate attachment site.
210	224	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
28	397	CDD	cd00614	CGS_like
28	397	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
10	266	FunFam	G3DSA:3.40.640.10:FF:000046	Cystathionine gamma-lyase
8	265	Gene3D	G3DSA:3.40.640.10	-
8	265	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
42	62	Coils	Coil	Coil
266	398	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
266	398	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
9	399	PANTHER	PTHR43500	CYSTATHIONINE BETA-LYASE-RELATED
9	399	InterPro	IPR006233	Cystathionine beta-lyase, bacterial
14	396	NCBIfam	TIGR01324	cystathionine beta-lyase
14	396	InterPro	IPR006233	Cystathionine beta-lyase, bacterial

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.856

Likely same site as FPocket 21 1.8 Å 22 shared residues 96% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.037

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.036

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.028

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.017

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #21

0.535 Unusual size

Likely same site as P2Rank 1 1.8 Å 22 shared residues 96% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.889

Likely same site as FPocket 7 0.8 Å 25 shared residues 93% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.01

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.005

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #7

0.618 Unusual size

Likely same site as P2Rank 1 0.8 Å 25 shared residues 93% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #6

0.366

Show in viewer

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_A0A0C7KER1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0773	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.

68 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 18 records from similar proteins

Structural ligands 12 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

BLP PDB via homolog 469.3 Da · LogP 0.16 · TPSA 213.2 Open detail RCSB PDB

ECX PDB via homolog Detail RCSB PDB

IN5 PDB via homolog Detail RCSB PDB

LCS PDB via homolog Detail RCSB PDB

MPJ 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
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`
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`
CHEMBL4795578 ChEMBL	Q8VCN5	—	113.1 Da LogP -0.58 TPSA 63.3	✓ Ro5	✓ Clean	`C#CCC(N)C(=O)O`
QU4 ChEMBL	Q8VCN5	—	422.3 Da LogP 2.45 TPSA 169.4	✓ Ro5	✓ Clean	`c1cc(c(cc1C(=C2C=CC(=O)C(=C2)C(=O)O)c3ccc(c(c3)…`

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
ZINC3833863 ZINC	1.000	422.3 Da LogP 2.45 TPSA 169.4	✓ Ro5	✓ Clean	`O=C(O)C1=CC(=C(c2ccc(O)c(C(=O)O)c2)c2ccc(O)c(C(…`
ZINC2035155 ZINC	0.826	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](N)C(=O)O`
ZINC1532514 ZINC	0.756	247.1 Da LogP 0.52 TPSA 117.0	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C=O)c1O`
ZINC2054344316 ZINC	0.756	300.3 Da LogP 2.01 TPSA 111.9	✓ Ro5	✓ Clean	`CC(=C1C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1`
ZINC28092924 ZINC	0.756	300.3 Da LogP 2.01 TPSA 111.9	✓ Ro5	✓ Clean	`C/C(=C1/C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1`
ZINC36748824 ZINC	0.756	300.3 Da LogP 2.01 TPSA 111.9	✓ Ro5	✓ Clean	`C/C(=C1\C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1`
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`
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`
ZINC1532708 ZINC	0.674	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
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`
ZINC1532705 ZINC	0.652	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC64708385 ZINC	0.644	467.4 Da LogP 0.44 TPSA 214.5	1 viol.	✓ Clean	`NOC(=O)C1=CC(=C(c2ccc(O)c(C(=O)ON)c2)c2ccc(O)c(…`
ZINC1656021 ZINC	0.643	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C)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`
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`
ZINC27644247 ZINC	0.633	230.3 Da LogP 0.09 TPSA 111.2	✓ Ro5	✓ Clean	`CCCCNC(=N)NCCC[C@H](N)C(=O)O`
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`
ZINC28210975 ZINC	0.615	233.2 Da LogP 1.43 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(NCCO)c1ccccc1C(F)(F)F`
ZINC217503161 ZINC	0.613	230.3 Da LogP 0.88 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCC(=O)NCCCC[C@H](N)C(=O)O`
ZINC242824 ZINC	0.613	240.3 Da LogP 3.95 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)Nc1ccccc1C`
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`
ZINC1872765 ZINC	0.595	336.2 Da LogP 4.22 TPSA 42.0	✓ Ro5	✓ Clean	`Cc1ccc2c(NC(=O)C(C(F)(F)F)C(F)(F)F)cccc2n1`
ZINC1075373 ZINC	0.591	356.7 Da LogP 3.73 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CNC(=O)c1ccccc1Cl)Nc1ccccc1C(F)(F)F`
ZINC2884493 ZINC	0.591	336.3 Da LogP 3.38 TPSA 58.2	✓ Ro5	✓ Clean	`Cc1ccccc1C(=O)NCC(=O)Nc1ccccc1C(F)(F)F`
ZINC4820780 ZINC	0.591	340.3 Da LogP 3.21 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CNC(=O)c1ccccc1F)Nc1ccccc1C(F)(F)F`
ZINC2975508 ZINC	0.590	286.2 Da LogP 3.07 TPSA 42.0	✓ Ro5	✓ Clean	`Cc1cccnc1NC(=O)C(C(F)(F)F)C(F)(F)F`
ZINC3844326 ZINC	0.590	316.2 Da LogP 3.27 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1[N+](=O)[O-])C(C(F)(F)F)C(F)(F)F`

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.

cystathionine beta-lyase

Target candidate with partial support; inspect missing evidence before prioritizing.

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