Protein target profile

VK055_2391

MTA/SAH nucleosidase

Genome: KpATCC43816 Gene: AIK80988.1 mtnN 3D evidence: Experimental + ColabFold model Metabolism 2 reactions UniProt A6T4W3

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Length 232

Pocket druggability 0.374

Metabolic reactions 2

Chokepoint Yes

Direct ligand evidence 1 95 total records

Functional annotation 0 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

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Direct ligand evidence 1 direct ligand records. Strong known ligand: co-crystal structure 1 PDB record(s) show a ligand actually co-crystallized with this exact protein - real experimental evidence, not a computational prediction. Review the complete evidence below

Risks to review

Microbiome similarity 195 of 4744 screened genomes (4.1%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.37. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.36.

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: 4.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 90.517 Higher values support similarity to known essential genes.
DEG E-value: 2.31e-148 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.71 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 0.374

Structure 4G89

Pocket Pocket 2

P2Rank 0.357

Structure 4G89

Pocket Pocket 1

ColabFold model

FPocket 0.818 · Pocket 1

P2Rank 0.459 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 195 / 4744 genomes with a hit

Prevalence 4.1%

Cross-references

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

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Cysteine and methionine metabolism, no isoenzyme backup detected, more central than 92.8% of genes in this genome, no human homolog detected.

Relative network centrality 92.8% more central than 92.8% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKIGIIGAMEEEVTLLRDKIENRQTITIGGSEIYTGQLHGVDVALLKSGIGKVAAAMGATLLLERCQPDVIINTGSAGGLASTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADEKLVAAAESCIKALDLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFKVPFVVVRAISDVADQQSHLSFEEFLAVAARQSTLMVENLVQNLARG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

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:0019509 OBSOLETE. The generation of L-methionine (2-amino-4-(methylthio)butanoic acid) from methylthioadenosine.
GO:0009164 The chemical reactions and pathways resulting in the breakdown of any one of a family of organic molecules consisting of a purine or pyrimidine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
GO:0008930 Catalysis of the reaction: methylthioadenosine + H2O = adenine + 5-methylthio-D-ribose.
GO:0008782 Catalysis of the reaction: S-adenosyl-L-homocysteine + H2O = adenine + S-D-ribosyl-L-homocysteine.
GO:0009116 The chemical reactions and pathways involving a nucleoside, a nucleobase linked to either beta-D-ribofuranose (a ribonucleoside) or 2-deoxy-beta-D-ribofuranose, (a deoxyribonucleoside), e.g. adenosine, guanosine, inosine, cytidine, uridine and deoxyadenosine, deoxyguanosine, deoxycytidine and thymidine (= deoxythymidine).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

12 records

Show feature table

Start	End	DB	Term	Name
2	229	PANTHER	PTHR46832	5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE
1	230	FunFam	G3DSA:3.40.50.1580:FF:000001	MTA/SAH nucleosidase family protein
2	229	NCBIfam	TIGR01704	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
2	229	InterPro	IPR010049	MTA/SAH nucleosidase
2	229	Hamap	MF_01684	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase [mtnN].
3	225	CDD	cd09008	MTAN
1	232	Gene3D	G3DSA:3.40.50.1580	Nucleoside phosphorylase domain
1	232	InterPro	IPR035994	Nucleoside phosphorylase superfamily
2	225	Pfam	PF01048	Phosphorylase superfamily
2	225	InterPro	IPR000845	Nucleoside phosphorylase domain
1	229	SUPERFAMILY	SSF53167	Purine and uridine phosphorylases
1	229	InterPro	IPR035994	Nucleoside phosphorylase superfamily

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

0.374

Unusual size

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Surrounding area

Site 2 FPocket #14

0.293

Show in viewer

Surrounding area

Site 3 FPocket #10

0.248

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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

0.357

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:12-12 Proton acceptor

UniProt: Active site:197-197 Proton donor

UniProt: Binding site:152-152

UniProt: Binding site:173-174

UniProt: Binding site:78-78

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 4G89	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
ColabFold VK055_2391	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.

95 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 1 same-protein records

Transferred evidence 44 records from similar proteins

Structural ligands 11 1 loaded crystals

Measured bioactivity 34 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ADE PDB co-crystal 135.1 Da · LogP -0.06 · TPSA 80.5 Open detail RCSB PDB

4CT PDB via homolog Detail RCSB PDB

4F0 PDB via homolog Detail RCSB PDB

9DA PDB via homolog Detail RCSB PDB

BIG 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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ADE RCSB PDB	4G89 Open crystal	135.1 Da LogP -0.06 TPSA 80.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(ncn2)N`

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
4CT RCSB PDB	3O4V	P0AF12	389.9 Da LogP 2.78 TPSA 91.1	✓ Ro5	✓ Clean	`c1cc(ccc1SC[C@H]2C[N@](C[C@@H]2O)Cc3c[nH]c4c3nc…`
4F0 RCSB PDB	4YML	P0AF12	293.4 Da LogP 0.70 TPSA 91.1	✓ Ro5	✓ Clean	`CSC[C@@H]1CN(C[C@H]1O)Cc2c[nH]c3c2ncnc3N`
9DA RCSB PDB	5UE1	Q5E2X3	134.1 Da LogP 0.54 TPSA 67.6	✓ Ro5	✓ Clean	`c1c[nH]c2c1ncnc2N`
BIG RCSB PDB	4WKC	A7ZHQ1	335.5 Da LogP 1.87 TPSA 91.1	✓ Ro5	✓ Clean	`CCCCSC[C@H]1C[N@](C[C@@H]1O)Cc2c[nH]c3c2ncnc3N`
DF9 RCSB PDB	3DF9	P0AF14	369.5 Da LogP 2.27 TPSA 91.1	✓ Ro5	✓ Clean	`c1ccc(cc1)CSC[C@H]2CN(C[C@@H]2O)Cc3c[nH]c4c3ncn…`
FMC RCSB PDB	1NC3	P0AF12	267.2 Da LogP -1.91 TPSA 150.4	✓ Ro5	✓ Clean	`c1nc2c(c(n1)N)[nH]nc2[C@H]3[C@@H]([C@@H]([C@H](…`
MTA RCSB PDB	1Z5O	P0AF12	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)…`
MTH RCSB PDB	1NC1	P0AF12	296.4 Da LogP -0.00 TPSA 106.4	✓ Ro5	✓ Clean	`CSC[C@@H]1[C@H]([C@H]([C@@H](O1)n2ccc3c2ncnc3N)…`
MTM RCSB PDB	1Y6R	P0AF12	297.4 Da LogP -0.67 TPSA 118.7	1 viol.	✓ Clean	`CSC[C@@H]1[C@H]([C@H]([C@@H](N1)c2c[nH]c3c2N=CN…`
PE5 RCSB PDB	1Z5P	P0AF12	398.5 Da LogP 0.13 TPSA 94.1	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCOCCO`

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
TDI ChEMBL	P0AF14	10.32 ~0.0 nM	293.4 Da LogP 0.70 TPSA 91.1	✓ Ro5	✓ Clean	`CSC[C@H]1C[N@](C[C@@H]1O)Cc2c[nH]c3c2ncnc3N`
CHEMBL1242854 ChEMBL	Q9KPI8	10.15 ~0.1 nM	307.4 Da LogP 1.09 TPSA 91.1	✓ Ro5	✓ Clean	`CCSC[C@H]1CN(Cc2c[nH]c3c(N)ncnc23)C[C@@H]1O`
CHEMBL405371 ChEMBL	P0AF14	9.35 ~0.4 nM	263.4 Da LogP 1.33 TPSA 70.8	✓ Ro5	✓ Clean	`CSCC1CN(Cc2c[nH]c3c(N)ncnc23)C1`
CHEMBL407216 ChEMBL	P0AF14	9.08 ~0.8 nM	293.4 Da LogP 0.70 TPSA 91.1	✓ Ro5	✓ Clean	`CSCC1(CO)CN(Cc2c[nH]c3c(N)ncnc23)C1`
CHEMBL1242855 ChEMBL	Q9KPI8	8.80 ~1.6 nM	309.4 Da LogP 0.03 TPSA 120.1	✓ Ro5	✓ Clean	`CCSC[C@H]1N[C@@H](c2c[nH]c3c(N)ncnc23)[C@H](O)[…`
CHEMBL154234 ChEMBL	P0AF14	8.80 ~1.6 nM	523.9 Da LogP 7.06 TPSA 86.9	2 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3ccc(Cl)c(Cl)c3)…`
CHEMBL207655 ChEMBL	P0AF14	8.77 ~1.7 nM	382.4 Da LogP -1.19 TPSA 183.4	1 viol.	✓ Clean	`Nc1ncnc2c([C@@H]3N[C@H](CSCCC(N)C(=O)O)[C@@H](O…`
CHEMBL1241493 ChEMBL	Q9KPI8	8.68 ~2.1 nM	371.5 Da LogP 1.21 TPSA 120.1	✓ Ro5	✓ Clean	`Nc1ncnc2c([C@@H]3N[C@H](CSCc4ccccc4)[C@@H](O)[C…`
CHEMBL1241494 ChEMBL	Q9KPI8	8.66 ~2.2 nM	391.9 Da LogP 1.72 TPSA 120.1	✓ Ro5	✓ Clean	`Nc1ncnc2c([C@@H]3N[C@H](CSc4ccc(Cl)cc4)[C@@H](O…`
CHEMBL349317 ChEMBL	P0AF14	8.47 ~3.4 nM	507.4 Da LogP 6.54 TPSA 86.9	2 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3ccc(F)c(Cl)c3)c…`
CHEMBL154218 ChEMBL	P0AF14	8.41 ~3.9 nM	503.5 Da LogP 6.71 TPSA 86.9	2 viol.	✓ Clean	`Cc1cc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4n[nH]c(C…`
CHEMBL345254 ChEMBL	P0AF14	8.09 ~8.1 nM	491.0 Da LogP 6.03 TPSA 86.9	1 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3ccc(F)c(F)c3)c2…`
CHEMBL1195586 ChEMBL	Q9KPI8	8.00 ~10.0 nM	295.4 Da LogP -0.36 TPSA 120.1	✓ Ro5	✓ Clean	`CSC[C@H]1N[C@@H](c2c[nH]c3c(N)ncnc23)[C@H](O)[C…`
CHEMBL156794 ChEMBL	P0AF14	7.97 ~10.7 nM	506.0 Da LogP 6.30 TPSA 99.8	2 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3cnc4ccccc4c3)c2…`
CHEMBL349792 ChEMBL	P0AF14	7.96 ~11.0 nM	523.0 Da LogP 6.77 TPSA 86.9	2 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3cccc(C(F)(F)F)c…`
CHEMBL156734 ChEMBL	P0AF14	7.90 ~12.6 nM	489.4 Da LogP 6.41 TPSA 86.9	1 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3ccc(Cl)cc3)c2)c…`
CHEMBL421824 ChEMBL	P0AF14	7.89 ~12.9 nM	523.0 Da LogP 6.77 TPSA 86.9	2 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3ccc(C(F)(F)F)cc…`
CHEMBL154219 ChEMBL	P0AF14	7.84 ~14.5 nM	487.0 Da LogP 6.20 TPSA 86.9	1 viol.	✓ Clean	`Cc1cc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4n[nH]c(C…`
CHEMBL153941 ChEMBL	P0AF14	7.77 ~17.0 nM	501.1 Da LogP 6.47 TPSA 86.9	2 viol.	✓ Clean	`CSc1cccc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4[nH]n…`
CHEMBL157262 ChEMBL	P0AF14	7.70 ~20.0 nM	502.6 Da LogP 6.43 TPSA 86.9	2 viol.	✓ Clean	`Cc1n[nH]c2c(NCC(C)C)cc(NS(=O)(=O)c3cccc(-c4cccc…`
CHEMBL152127 ChEMBL	P0AF14	7.60 ~25.1 nM	499.0 Da LogP 5.29 TPSA 107.1	1 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3cccc(CCO)c3)c2)…`
CHEMBL346924 ChEMBL	P0AF14	7.54 ~28.8 nM	470.0 Da LogP 5.46 TPSA 99.8	1 viol.	✓ Clean	`Cc1cc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4n[nH]c(C…`
CHEMBL153876 ChEMBL	P0AF14	7.44 ~36.3 nM	471.0 Da LogP 4.85 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1nccc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4n[nH]c…`
CHEMBL154684 ChEMBL	P0AF14	7.44 ~36.3 nM	469.0 Da LogP 6.06 TPSA 86.9	1 viol.	✓ Clean	`Cc1cccc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4n[nH]c…`
CHEMBL154614 ChEMBL	P0AF14	7.28 ~52.5 nM	456.0 Da LogP 5.15 TPSA 99.8	1 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3ccncc3)c2)cc2c(…`
CHEMBL157317 ChEMBL	P0AF14	7.03 ~93.3 nM	455.0 Da LogP 5.75 TPSA 86.9	1 viol.	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2cccc(-c3ccccc3)c2)cc2c(…`
CHEMBL347675 ChEMBL	P0AF14	7.00 ~100.0 nM	448.6 Da LogP 5.72 TPSA 86.9	1 viol.	✓ Clean	`Cc1cccc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4[nH]nc…`
CHEMBL347181 ChEMBL	P0AF14	6.90 ~125.9 nM	462.6 Da LogP 5.97 TPSA 86.9	1 viol.	✓ Clean	`CCc1cccc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4[nH]n…`
CHEMBL153820 ChEMBL	P0AF14	6.72 ~190.5 nM	450.6 Da LogP 4.51 TPSA 112.7	✓ Ro5	✓ Clean	`Cc1nccc(-c2cccc(S(=O)(=O)Nc3cc(NCC(C)C)c4[nH]nc…`
CHEMBL157223 ChEMBL	P0AF14	6.62 ~239.9 nM	435.6 Da LogP 4.80 TPSA 99.8	✓ Ro5	✓ Clean	`Cc1n[nH]c2c(NCC(C)C)cc(NS(=O)(=O)c3cccc(-c4ccnc…`
CHEMBL153309 ChEMBL	P0AF14	6.30 ~501.2 nM	434.6 Da LogP 5.41 TPSA 86.9	1 viol.	✓ Clean	`Cc1n[nH]c2c(NCC(C)C)cc(NS(=O)(=O)c3cccc(-c4cccc…`
CHEMBL154601 ChEMBL	P0AF14	6.30 ~501.2 nM	411.3 Da LogP 4.49 TPSA 86.9	✓ Ro5	✓ Clean	`O=S(=O)(Nc1cc(NCC2CC2)c2[nH]nc(Cl)c2c1)c1ccc(Cl…`
CHEMBL349108 ChEMBL	P0AF14	6.12 ~758.6 nM	413.3 Da LogP 4.74 TPSA 86.9	✓ Ro5	✓ Clean	`CC(C)CNc1cc(NS(=O)(=O)c2ccc(Cl)cc2)cc2c(Cl)[nH]…`
CHEMBL152983 ChEMBL	P0AF14	6.00 ~1.0 µM	366.4 Da LogP 3.58 TPSA 78.1	✓ Ro5	✓ Clean	`CN(C)c1cccc2c(S(=O)(=O)Nc3ccc4c[nH]nc4c3)cccc12`

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
ZINC5650743 ZINC	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC8577182 ZINC	0.773	268.2 Da LogP -1.79 TPSA 144.6	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](c2n[nH]c3c(O)ncnc23)[C@H](O)[C@…`
ZINC253500647 ZINC	0.766	298.3 Da LogP -0.49 TPSA 113.5	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(O)ncnc32)[C@H](O)[C@H]…`
ZINC4972228 ZINC	0.761	310.3 Da LogP -1.30 TPSA 124.4	✓ Ro5	✓ Clean	`C[N+](C)(C)c1ncnc2c([C@H]3O[C@@H](CO)[C@@H](O)[…`
ZINC11686540 ZINC	0.759	293.4 Da LogP 0.70 TPSA 91.1	✓ Ro5	✓ Clean	`CSC[C@H]1CN(Cc2c[nH]c3c(N)ncnc23)C[C@@H]1O`
ZINC5139067 ZINC	0.756	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CS)[C@@H](O)[C@H]1O`
ZINC14766197 ZINC	0.745	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC201682330 ZINC	0.745	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)…`
ZINC248157271 ZINC	0.745	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)…`
ZINC2516140 ZINC	0.745	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O…`
ZINC5138266 ZINC	0.745	339.4 Da LogP 0.42 TPSA 119.3	✓ Ro5	✓ Clean	`CC(C)CSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)…`
ZINC26735509 ZINC	0.745	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC3832269 ZINC	0.745	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC3873955 ZINC	0.745	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3873956 ZINC	0.745	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3873957 ZINC	0.745	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC3873958 ZINC	0.745	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC5161656 ZINC	0.745	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC5162989 ZINC	0.745	266.3 Da LogP -1.38 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1ccn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC8628081 ZINC	0.745	282.3 Da LogP -2.21 TPSA 162.4	1 viol.	✓ Clean	`NNc1ncnc2c([C@H]3O[C@@H](CO)[C@@H](O)[C@H]3O)n[…`
ZINC8628082 ZINC	0.745	282.3 Da LogP -2.21 TPSA 162.4	1 viol.	✓ Clean	`NNc1ncnc2c([C@@H]3O[C@@H](CO)[C@@H](O)[C@H]3O)n…`
ZINC2047403 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC2047673 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC2169830 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC3201876 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC3201878 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC3814316 ZINC	0.739	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]…`
ZINC3830178 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3830179 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3978047 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC3978048 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC3978049 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC4048240 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC4773848 ZINC	0.739	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]…`
ZINC4773849 ZINC	0.739	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H…`
ZINC4773850 ZINC	0.739	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H…`
ZINC4773851 ZINC	0.739	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@…`
ZINC77981211 ZINC	0.739	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]…`
ZINC82228511 ZINC	0.739	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]1O`
ZINC8580514 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC895113 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC896706 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC970363 ZINC	0.739	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC1081541 ZINC	0.723	285.7 Da LogP -0.73 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CCl)[C@@H](O)[C@@H]…`
ZINC4188112 ZINC	0.723	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC5941240 ZINC	0.723	269.2 Da LogP -1.00 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CF)[C@@H](O)[C@H]1O`
ZINC8638190 ZINC	0.723	283.2 Da LogP -1.69 TPSA 156.6	1 viol.	✓ Clean	`OC[C@@H]1O[C@H](c2n[nH]c3c(NO)ncnc23)[C@H](O)[C…`
ZINC8638192 ZINC	0.723	283.2 Da LogP -1.69 TPSA 156.6	1 viol.	✓ Clean	`OC[C@@H]1O[C@@H](c2n[nH]c3c(NO)ncnc23)[C@H](O)[…`
ZINC8638195 ZINC	0.723	283.2 Da LogP -1.69 TPSA 156.6	1 viol.	✓ Clean	`OC[C@@H]1O[C@@H](c2n[nH]c3c(NO)ncnc23)[C@@H](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.

VK055_2391

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Structure

Chemistry

Pathways

Metabolic context

Sequence

Functional annotations

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence