Protein target profile

VK055_3340

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase

Genome: KpATCC43816 Gene: glmU AIK81897.1 3D evidence: Experimental + ColabFold model Metabolism 2 reactions UniProt A6TG34

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Length 456

Pocket druggability 0.669

Metabolic reactions 2

Chokepoint Yes

Direct ligand evidence 0 97 total records

Functional annotation 0 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. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Central metabolic position More central than 97.6% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. 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: 5.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 89.912 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: 96.22 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 0.669

Structure 8CU9

Pocket Pocket 1

P2Rank 0.146

Structure 8CU9

Pocket Pocket 1

ColabFold model

FPocket 0.576 · Pocket 19

P2Rank 0.653 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 247 / 4744 genomes with a hit

Prevalence 5.2%

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 Amino sugar and nucleotide sugar metabolism, no isoenzyme backup detected, more central than 97.6% of genes in this genome, no human homolog detected.

Relative network centrality 97.6% more central than 97.6% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSNSAMSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDAANDLGACAVHLVYGHGGDLLRQTLHEDNLNWVLQAEQLGTGHAMQQAAPFFNDDEDILMLYGDVPLISVETLQRLRAAKPQGGIGLLTVKLDDPTGYGRITRENGQVTGIVEHKDASEAQRQIQEINTGILIAGGADLKRWLAKLTNNNAQGEYYITDIIAMAHQEGHQIVAVHPQRLSEVEGVNNRLQLARLERVYQAEQAEKLLLAGVMLRDPARFDLRGTLQHGRDVEIDTNVILEGNVVLGDRVKIGAGCVIKNSTIGDDCEISPYSVVEDAQLQAACTIGPFARLRPGAELLEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKHKTIIGDDVFVGSDTQLVAPVTVGNGVTIAAGTTVTRNIADNELVLSRVPQVHKQGWQRPVKKK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
GO:0000902 The developmental process in which the size or shape of a cell is generated and organized.
GO:0003977 Catalysis of the reaction: N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.
GO:0006048 The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0019134 Catalysis of the reaction: alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H+.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
395	429	Pfam	PF00132	Bacterial transferase hexapeptide (six repeats)
395	429	InterPro	IPR001451	Hexapeptide repeat
267	300	Pfam	PF00132	Bacterial transferase hexapeptide (six repeats)
267	300	InterPro	IPR001451	Hexapeptide repeat
6	455	NCBIfam	TIGR01173	UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase
6	455	InterPro	IPR005882	Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
228	456	Gene3D	G3DSA:2.160.10.10	Hexapeptide repeat proteins
6	423	PANTHER	PTHR43584	NUCLEOTIDYL TRANSFERASE
1	227	Gene3D	G3DSA:3.90.550.10	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
1	227	InterPro	IPR029044	Nucleotide-diphospho-sugar transferases
6	252	SUPERFAMILY	SSF53448	Nucleotide-diphospho-sugar transferases
6	252	InterPro	IPR029044	Nucleotide-diphospho-sugar transferases
5	452	Hamap	MF_01631	Bifunctional protein GlmU [glmU].
5	452	InterPro	IPR005882	Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
403	431	ProSitePatterns	PS00101	Hexapeptide-repeat containing-transferases signature.
403	431	InterPro	IPR018357	Hexapeptide transferase, conserved site
1	227	FunFam	G3DSA:3.90.550.10:FF:000006	Bifunctional protein GlmU
8	232	CDD	cd02540	GT2_GlmU_N_bac
8	124	Pfam	PF12804	MobA-like NTP transferase domain
8	124	InterPro	IPR025877	MobA-like NTP transferase
255	439	SUPERFAMILY	SSF51161	Trimeric LpxA-like enzymes
255	439	InterPro	IPR011004	Trimeric LpxA-like superfamily
251	443	CDD	cd03353	LbH_GlmU_C
251	443	InterPro	IPR038009	GlmU, C-terminal LbH domain
228	456	FunFam	G3DSA:2.160.10.10:FF:000011	Bifunctional protein GlmU

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 #1

0.669

Likely same site as P2Rank 1 1.0 Å 15 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #9

0.369

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Surrounding area

Site 3 FPocket #18

0.353

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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

0.146

Likely same site as FPocket 1 1.0 Å 15 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.119

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Surrounding area

Site 3 P2Rank #3

0.003

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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

0.653

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Surrounding area

Site 2 P2Rank #2

0.164

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Surrounding area

Site 3 P2Rank #3

0.027

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Surrounding area

Site 4 P2Rank #4

0.018

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Surrounding area

Site 5 P2Rank #5

0.009

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Surrounding area

Residue sets

UniProt: Active site:363-363 Proton acceptor

UniProt: Binding site:103-105

UniProt: Binding site:105-105

UniProt: Binding site:11-14

UniProt: Binding site:140-140

UniProt: Binding site:154-154

UniProt: Binding site:169-169

UniProt: Binding site:227-227

UniProt: Binding site:25-25

UniProt: Binding site:333-333

UniProt: Binding site:351-351

UniProt: Binding site:366-366

UniProt: Binding site:377-377

UniProt: Binding site:380-380

UniProt: Binding site:386-387

UniProt: Binding site:405-405

UniProt: Binding site:423-423

UniProt: Binding site:440-440

UniProt: Binding site:76-76

UniProt: Binding site:81-82

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 8CU9	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
ColabFold VK055_3340	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.

97 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 47 records from similar proteins

Structural ligands 12 0 loaded crystals

Measured bioactivity 35 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0N5 PDB via homolog 386.4 Da · LogP 4.34 · TPSA 96.4 Open detail RCSB PDB

1S8 PDB via homolog Detail RCSB PDB

1S9 PDB via homolog Detail RCSB PDB

1SE PDB via homolog Detail RCSB PDB

1SF 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
0N5 RCSB PDB	4E1K	P43889	386.4 Da LogP 4.34 TPSA 96.4	✓ Ro5	✓ Clean	`COc1cc2c(cc1O)ncnc2Nc3ccc(cc3)NC(=O)c4ccccc4`
1S8 RCSB PDB	4KNR	P43889	476.5 Da LogP 5.93 TPSA 96.4	1 viol.	✓ Clean	`COc1cc2c(cc1O)nc(nc2Nc3ccc(cc3)NC(=O)c4ccccc4)C…`
1S9 RCSB PDB	4KNX	P43889	444.4 Da LogP 4.10 TPSA 122.7	✓ Ro5	✓ Clean	`COc1cc2c(cc1OCC(=O)O)ncnc2Nc3ccc(cc3)NC(=O)c4cc…`
1SE RCSB PDB	4KPX	P43889	378.3 Da LogP 3.20 TPSA 134.5	✓ Ro5	✓ Clean	`c1ccnc(c1)C(=O)Nc2ccc(cc2)NC(=O)c3ccc(c(c3)[N+]…`
1SF RCSB PDB	4KPZ	P43889	235.2 Da LogP 1.04 TPSA 92.6	✓ Ro5	✓ Clean	`c1cc(cc(c1)[N+](=O)[O-])N2CCC(=O)NC2=O`
1SG RCSB PDB	4KQL	P43889	457.4 Da LogP 2.64 TPSA 146.0	✓ Ro5	✓ Clean	`COc1cc(cc(c1)C(=O)Nc2ccc(cc2)NC(=O)c3ccccn3)C4=…`
LZR RCSB PDB	2W0V	P43889	446.5 Da LogP 2.63 TPSA 89.4	✓ Ro5	✓ Clean	`COc1cc2c(cc1OCC3C=C3)C(=O)NC(=N2)N4CCC5=C(C4)C=…`
LZS RCSB PDB	2W0W	P43889	595.6 Da LogP 4.11 TPSA 115.7	1 viol.	✓ Clean	`CC(C)CN1C=CC2=C(C1=O)CCN(C2)c3nc4cc(c(cc4c(n3)N…`
P21 RCSB PDB	2VD4	P43889	415.0 Da LogP 4.53 TPSA 32.8	✓ Ro5	✓ Clean	`COCCCN([C@H]1CCC[N@](C1)CCc2ccccc2)C(=O)c3ccc(c…`
R82 RCSB PDB	4AA7	P0ACC7	390.5 Da LogP 2.80 TPSA 84.9	✓ Ro5	✓ Clean	`C[C@@H]1Cc2ccccc2N1S(=O)(=O)c3cc(c(cc3OC)OC)NC(…`
R83 RCSB PDB	4AC3	Q8DQ18	447.6 Da LogP 3.13 TPSA 97.0	✓ Ro5	✓ Clean	`CC(=O)Nc1cc(c(cc1OC)OC)S(=O)(=O)NCc2ccccc2N3CCC…`
UD1 RCSB PDB	1FWY	P0ACC7	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`

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
CHEMBL2207603 ChEMBL	P0ACC7	8.00 ~10.0 nM	498.5 Da LogP 4.14 TPSA 131.5	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3Oc3ccccc32)cc1NC…`
CHEMBL2207606 ChEMBL	P0ACC7	8.00 ~10.0 nM	496.5 Da LogP 3.92 TPSA 131.5	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3Oc3ccccc32)cc1NC…`
GOB ChEMBL	P0ACC7	7.70 ~20.0 nM	499.5 Da LogP 3.62 TPSA 148.3	✓ Ro5	Alert	`COc1cc(c(cc1NC(=O)CCC(=O)O)S(=O)(=O)N(c2ccccc2)…`
CHEMBL2207605 ChEMBL	P0ACC7	7.52 ~30.2 nM	512.5 Da LogP 4.01 TPSA 131.5	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2Cc3ccccc3Oc3ccccc32)cc1N…`
CHEMBL3415068 ChEMBL	P0ACC7	7.52 ~30.2 nM	524.6 Da LogP 4.24 TPSA 131.5	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3Oc3ccccc32)cc1NC…`
CHEMBL2207599 ChEMBL	P0ACC7	7.40 ~39.8 nM	484.5 Da LogP 4.03 TPSA 122.2	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N(c2ccccc2)c2ccccc2)cc1NC(…`
CHEMBL2207600 ChEMBL	P0ACC7	7.40 ~39.8 nM	512.6 Da LogP 4.65 TPSA 122.2	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N(c2ccc(C)cc2)c2ccc(C)cc2)…`
CHEMBL2207602 ChEMBL	P0ACC7	7.40 ~39.8 nM	534.6 Da LogP 5.19 TPSA 122.2	2 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N(c2ccccc2)c2ccc3ccccc3c2)…`
CHEMBL3415072 ChEMBL	P0ACC7	7.30 ~50.1 nM	448.5 Da LogP 2.73 TPSA 133.2	✓ Ro5	✓ Clean	`COc1cc(O)c(S(=O)(=O)N2c3ccccc3CC[C@H]2C)cc1NC(=…`
CHEMBL2207224 ChEMBL	P0ACC7	7.22 ~60.3 nM	517.6 Da LogP 4.91 TPSA 107.1	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3Oc3ccccc32)cc1NC…`
CHEMBL3415115 ChEMBL	P0ACC7	7.22 ~60.3 nM	510.5 Da LogP 3.94 TPSA 142.5	1 viol.	✓ Clean	`COc1cc(O)c(S(=O)(=O)N2c3ccccc3Oc3ccccc32)cc1NC(…`
CHEMBL2207226 ChEMBL	P0ACC7	7.05 ~89.1 nM	535.6 Da LogP 5.05 TPSA 107.1	2 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3Oc3ccccc32)cc1NC…`
CHEMBL2207604 ChEMBL	P0ACC7	7.05 ~89.1 nM	514.6 Da LogP 4.50 TPSA 122.2	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3Sc3ccccc32)cc1NC…`
CHEMBL3414903 ChEMBL	P0ACC7	7.05 ~89.1 nM	462.5 Da LogP 3.04 TPSA 122.2	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@@H]2C)cc1NC…`
CHEMBL3414904 ChEMBL	P0ACC7	7.00 ~100.0 nM	494.6 Da LogP 2.99 TPSA 122.2	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@H]2C)cc1NC(…`
CHEMBL3343057 ChEMBL	C3SLB7	6.92 ~120.2 nM	463.5 Da LogP 2.07 TPSA 145.2	✓ Ro5	✓ Clean	`COc1cc(C(=O)Nc2ccc(NC(=O)C3CCCCN3)cc2)cc(-c2c[n…`
CHEMBL3414901 ChEMBL	P0ACC7	6.70 ~199.5 nM	478.5 Da LogP 2.27 TPSA 131.5	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@@H]2C)cc1NC…`
R84 ChEMBL	P0ACC7	6.60 ~251.2 nM	635.7 Da LogP 2.61 TPSA 197.9	1 viol.	✓ Clean	`COc1cc(c(cc1NC(=O)CCC(=O)O)S(=O)(=O)NCc2ccccc2N…`
CHEMBL3343050 ChEMBL	C3SLB7	6.58 ~263.0 nM	472.5 Da LogP 2.95 TPSA 153.4	✓ Ro5	✓ Clean	`COc1cc(C(=O)Nc2ccc(NC(=O)c3ccccc3)cc2)cc(-c2c[n…`
CHEMBL3343051 ChEMBL	C3SLB7	6.46 ~346.7 nM	427.4 Da LogP 2.63 TPSA 136.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(NC(=O)c2ccccn2)cc1)c1cccc(-c2c[nH]c(…`
CHEMBL3343041 ChEMBL	C3SLB7	6.43 ~371.5 nM	420.9 Da LogP 4.99 TPSA 96.4	✓ Ro5	✓ Clean	`COc1cc2c(Nc3ccc(NC(=O)c4ccccc4)cc3)nc(Cl)nc2cc1O`
CHEMBL1951187 ChEMBL	P0ACC7	6.40 ~398.1 nM	563.6 Da LogP 2.68 TPSA 171.6	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)NCc2ccccc2N2CCC(CC(=O)O)CC…`
CHEMBL3415069 ChEMBL	P0ACC7	6.40 ~398.1 nM	488.6 Da LogP 3.14 TPSA 122.2	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@@H]2C)cc1NC…`
CHEMBL3415067 ChEMBL	P0ACC7	6.37 ~426.6 nM	486.6 Da LogP 2.32 TPSA 139.4	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@@H]2C)cc1NC…`
CHEMBL3415116 ChEMBL	P0ACC7	6.32 ~478.6 nM	474.5 Da LogP 2.84 TPSA 133.2	✓ Ro5	✓ Clean	`COc1cc(O)c(S(=O)(=O)N2c3ccccc3CC[C@H]2C)cc1NC(=…`
CHEMBL1951186 ChEMBL	P0ACC7	6.30 ~501.2 nM	549.6 Da LogP 2.29 TPSA 171.6	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)NCc2ccccc2N2CCC(C(=O)O)CC2…`
CHEMBL3414898 ChEMBL	P0ACC7	6.30 ~501.2 nM	479.6 Da LogP 2.60 TPSA 117.2	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@H]2C)cc1NC(…`
CHEMBL3414899 ChEMBL	P0ACC7	6.30 ~501.2 nM	463.5 Da LogP 2.44 TPSA 134.3	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@H]2C)cc1NC(…`
CHEMBL3414902 ChEMBL	P0ACC7	6.30 ~501.2 nM	460.5 Da LogP 2.81 TPSA 122.2	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@@H]2C)cc1NC…`
CHEMBL3343042 ChEMBL	C3SLB7	6.19 ~645.7 nM	506.6 Da LogP 5.39 TPSA 121.3	2 viol.	✓ Clean	`COc1cc2c(Nc3ccc(NC(=O)c4ccccc4)cc3)nc(NCCc3cccc…`
CHEMBL3415071 ChEMBL	P0ACC7	6.17 ~676.1 nM	506.6 Da LogP 3.68 TPSA 121.6	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@@H]2C)cc1NC…`
CHEMBL3415070 ChEMBL	P0ACC7	6.10 ~794.3 nM	499.6 Da LogP 3.95 TPSA 97.8	✓ Ro5	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@@H]2C)cc1NC…`
CHEMBL1951185 ChEMBL	P0ACC7	6.05 ~891.3 nM	542.6 Da LogP 3.35 TPSA 168.3	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)NCc2ccccc2-c2ccc(C(=O)O)cc…`
CHEMBL3343058 ChEMBL	C3SLB7	6.01 ~977.2 nM	423.4 Da LogP 2.13 TPSA 145.2	✓ Ro5	✓ Clean	`CCNC(=O)Nc1ccc(NC(=O)c2cc(OC)cc(-c3c[nH]c(=O)[n…`
CHEMBL3414905 ChEMBL	P0ACC7	6.00 ~1.0 µM	513.6 Da LogP 4.36 TPSA 97.8	1 viol.	✓ Clean	`COc1cc(OC)c(S(=O)(=O)N2c3ccccc3CC[C@H]2C)cc1NC(…`

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
ZINC590935 ZINC	0.878	400.4 Da LogP 4.64 TPSA 85.4	✓ Ro5	✓ Clean	`COc1cc2ncnc(Nc3ccc(NC(=O)c4ccccc4)cc3)c2cc1OC`
ZINC16134038 ZINC	0.727	258.2 Da LogP 2.55 TPSA 92.5	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)c1ccc(O)c([N+](=O)[O-])c1`
ZINC11614162 ZINC	0.706	331.4 Da LogP 3.45 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(C)c(C)cc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC11614163 ZINC	0.706	331.4 Da LogP 3.45 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(C)c(C)cc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC210301298 ZINC	0.692	235.2 Da LogP 1.04 TPSA 92.6	✓ Ro5	✓ Clean	`O=C1CCN(c2ccc([N+](=O)[O-])cc2)C(=O)N1`
ZINC11614178 ZINC	0.679	347.4 Da LogP 3.15 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(S(=O)(=O)N2c3ccccc3C[C@@H]2C)c(OC)cc1C`
ZINC11614179 ZINC	0.679	347.4 Da LogP 3.15 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(S(=O)(=O)N2c3ccccc3C[C@H]2C)c(OC)cc1C`
ZINC27824167 ZINC	0.667	412.3 Da LogP 3.61 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(S(=O)(=O)N2c3ccccc3C[C@@H]2C)c(OC)cc1Br`
ZINC27824176 ZINC	0.667	412.3 Da LogP 3.61 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(S(=O)(=O)N2c3ccccc3C[C@H]2C)c(OC)cc1Br`
ZINC2853502 ZINC	0.667	367.9 Da LogP 3.50 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(S(=O)(=O)N2c3ccccc3C[C@@H]2C)c(OC)cc1Cl`
ZINC810977 ZINC	0.667	367.9 Da LogP 3.50 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(S(=O)(=O)N2c3ccccc3C[C@H]2C)c(OC)cc1Cl`
ZINC11614180 ZINC	0.660	317.4 Da LogP 3.14 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(C)ccc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC11614181 ZINC	0.660	317.4 Da LogP 3.14 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(C)ccc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC13947823 ZINC	0.660	333.4 Da LogP 2.84 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2c3ccccc3C[C@@H]2C)c(OC)c1`
ZINC13947824 ZINC	0.660	333.4 Da LogP 2.84 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2c3ccccc3C[C@H]2C)c(OC)c1`
ZINC1728432 ZINC	0.659	207.2 Da LogP 1.12 TPSA 75.5	✓ Ro5	✓ Clean	`O=C1NCCN1c1cccc([N+](=O)[O-])c1`
ZINC1903672 ZINC	0.655	325.3 Da LogP 3.09 TPSA 93.6	✓ Ro5	✓ Clean	`COc1cc2ncnc(Nc3ccc(C(=O)O)cc3)c2cc1OC`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC1424347 ZINC	0.648	337.8 Da LogP 3.49 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(Cl)ccc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC1424348 ZINC	0.648	337.8 Da LogP 3.49 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(Cl)ccc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC269980 ZINC	0.648	333.4 Da LogP 2.84 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(OC)c(S(=O)(=O)N2c3ccccc3C[C@@H]2C)c1`
ZINC269983 ZINC	0.648	333.4 Da LogP 2.84 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(OC)c(S(=O)(=O)N2c3ccccc3C[C@H]2C)c1`
ZINC4667072 ZINC	0.648	359.5 Da LogP 4.13 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(C(C)(C)C)cc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC4667073 ZINC	0.648	359.5 Da LogP 4.13 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(C(C)(C)C)cc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC610959 ZINC	0.648	317.4 Da LogP 3.14 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(C)cc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC610962 ZINC	0.648	317.4 Da LogP 3.14 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(C)cc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC1067672 ZINC	0.643	351.9 Da LogP 3.80 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(C)c(Cl)cc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC1067675 ZINC	0.643	351.9 Da LogP 3.80 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(C)c(Cl)cc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC4722314 ZINC	0.643	396.3 Da LogP 3.91 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(C)c(Br)cc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC4722316 ZINC	0.643	396.3 Da LogP 3.91 TPSA 46.6	✓ Ro5	✓ Clean	`COc1cc(C)c(Br)cc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC27824133 ZINC	0.642	331.4 Da LogP 3.45 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2c3ccccc3C[C@@H]2C)c(C)c1C`
ZINC27824142 ZINC	0.642	331.4 Da LogP 3.45 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2c3ccccc3C[C@H]2C)c(C)c1C`
ZINC5511126 ZINC	0.638	339.4 Da LogP 3.02 TPSA 93.6	✓ Ro5	✓ Clean	`COc1cc2ncnc(Nc3ccc(CC(=O)O)cc3)c2cc1OC`
ZINC1120495 ZINC	0.636	382.3 Da LogP 3.60 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(Br)cc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC1120497 ZINC	0.636	382.3 Da LogP 3.60 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(Br)cc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC16661446 ZINC	0.636	321.4 Da LogP 2.97 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(F)cc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC16661447 ZINC	0.636	321.4 Da LogP 2.97 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(F)cc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC621546 ZINC	0.636	337.8 Da LogP 3.49 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(Cl)cc1S(=O)(=O)N1c2ccccc2C[C@@H]1C`
ZINC621547 ZINC	0.636	337.8 Da LogP 3.49 TPSA 46.6	✓ Ro5	✓ Clean	`COc1ccc(Cl)cc1S(=O)(=O)N1c2ccccc2C[C@H]1C`
ZINC97112447 ZINC	0.636	338.3 Da LogP 2.80 TPSA 110.3	✓ Ro5	✓ Clean	`O=C(Nc1ccc(Cn2cccn2)cc1)c1ccc(O)c([N+](=O)[O-])…`
ZINC13366973 ZINC	0.633	373.4 Da LogP 2.93 TPSA 83.9	✓ Ro5	✓ Clean	`COc1ccc(/C=C/C(=O)O)cc1S(=O)(=O)N1c2ccccc2C[C@@…`
ZINC13366976 ZINC	0.633	373.4 Da LogP 2.93 TPSA 83.9	✓ Ro5	✓ Clean	`COc1ccc(/C=C/C(=O)O)cc1S(=O)(=O)N1c2ccccc2C[C@H…`
ZINC12959016 ZINC	0.632	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O…`
ZINC13548378 ZINC	0.632	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3861755 ZINC	0.632	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875257 ZINC	0.632	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC88466482 ZINC	0.632	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=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_3340

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