Protein target profile

VK055_3495

pantetheine-phosphate adenylyltransferase

Genome: KpATCC43816 Gene: AIK82051.1 coaD 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt Q9XC89

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Length 159

Pocket druggability 0.457

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 72 total records

Functional annotation 1 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. Central metabolic position More central than 95.2% 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: 5.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 86.164 Higher values support similarity to known essential genes.
DEG E-value: 1.1100000000000001e-103 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.3 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 0.457

Structure 8I8I

Pocket Pocket 1

P2Rank 0.615

Structure 8I8I

Pocket Pocket 1

ColabFold model

FPocket 0.271 · Pocket 2

P2Rank 0.827 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 237 / 4744 genomes with a hit

Prevalence 5.0%

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 & consuming chokepoint reaction in Pantothenate and CoA biosynthesis, no isoenzyme backup detected, more central than 95.2% of genes in this genome, no human homolog detected.

Relative network centrality 95.2% more central than 95.2% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSTKAIYPGTFDPITNGHIDIVTRAASMFDKVVLAIAASPSKKPMFSLDERIALAEQATAHLVNVEVIGFSDLMANFARAQQANILIRGLRAVADFEYEMQLAHMNRHLMPTLESVFLMPCKEWSFISSSLVKEVARHQGDVSHFLPANVHQALLNKLK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

2.7.7.3

Gene Ontology (GO)

GO:0004595 Catalysis of the reaction: ATP + pantetheine 4'-phosphate = 3'-dephospho-CoA + diphosphate.
GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
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:0015937 The chemical reactions and pathways resulting in the formation of coenzyme A, 3'-phosphoadenosine-(5')diphospho(4')pantatheine, an acyl carrier in many acylation and acyl-transfer reactions in which the intermediate is a thiol ester.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
5	157	NCBIfam	TIGR01510	pantetheine-phosphate adenylyltransferase
5	157	InterPro	IPR001980	Phosphopantetheine adenylyltransferase
3	159	Hamap	MF_00151	Phosphopantetheine adenylyltransferase [coaD].
3	159	InterPro	IPR001980	Phosphopantetheine adenylyltransferase
1	159	FunFam	G3DSA:3.40.50.620:FF:000012	Phosphopantetheine adenylyltransferase
6	134	Pfam	PF01467	Cytidylyltransferase-like
6	134	InterPro	IPR004821	Cytidyltransferase-like domain
1	159	Gene3D	G3DSA:3.40.50.620	HUPs
1	159	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
3	156	SUPERFAMILY	SSF52374	Nucleotidylyl transferase
3	157	PANTHER	PTHR21342	PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE
5	63	NCBIfam	TIGR00125	cytidyltransferase-like domain
5	63	InterPro	IPR004821	Cytidyltransferase-like domain
4	156	CDD	cd02163	PPAT
4	156	InterPro	IPR001980	Phosphopantetheine adenylyltransferase
3	21	PRINTS	PR01020	Lipopolysaccharide core biosynthesis protein signature
3	21	InterPro	IPR001980	Phosphopantetheine adenylyltransferase
113	135	PRINTS	PR01020	Lipopolysaccharide core biosynthesis protein signature
113	135	InterPro	IPR001980	Phosphopantetheine adenylyltransferase
86	102	PRINTS	PR01020	Lipopolysaccharide core biosynthesis protein signature
86	102	InterPro	IPR001980	Phosphopantetheine adenylyltransferase
21	42	PRINTS	PR01020	Lipopolysaccharide core biosynthesis protein signature
21	42	InterPro	IPR001980	Phosphopantetheine adenylyltransferase
50	74	PRINTS	PR01020	Lipopolysaccharide core biosynthesis protein signature
50	74	InterPro	IPR001980	Phosphopantetheine adenylyltransferase

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

0.457

Likely same site as P2Rank 1 1.4 Å 17 shared residues 94% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.615

Likely same site as FPocket 1 1.4 Å 17 shared residues 94% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.008

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:10-10

UniProt: Binding site:10-11

UniProt: Binding site:124-130

UniProt: Binding site:18-18

UniProt: Binding site:42-42

UniProt: Binding site:74-74

UniProt: Binding site:88-88

UniProt: Binding site:89-91

UniProt: Binding site:99-99

UniProt: Site:18-18 Transition state stabilizer

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 8I8I	X-ray	2.59 Å	A,B,C	100.0% 1-159	PDBe RCSB PDBj File	Viewing
ColabFold VK055_3495	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.

72 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 22 records from similar proteins

Structural ligands 22 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ASC PDB via homolog 176.1 Da · LogP -1.41 · TPSA 107.2 Open detail RCSB PDB

COD PDB via homolog Detail RCSB PDB

CW4 PDB via homolog Detail RCSB PDB

CWA PDB via homolog Detail RCSB PDB

CWG 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
ASC RCSB PDB	6JOG	A0A059ZFC5	176.1 Da LogP -1.41 TPSA 107.2	✓ Ro5	✓ Clean	`C([C@@H]([C@@H]1C(=C(C(=O)O1)O)O)O)O`
COD RCSB PDB	1B6T	P0A6I6	687.6 Da LogP -1.78 TPSA 300.0	3 viol.	✓ Clean	`CC(C)(CO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]…`
CW4 RCSB PDB	6B7F	P0A6I6	268.3 Da LogP 3.06 TPSA 44.1	✓ Ro5	✓ Clean	`CC1([C@@H](c2ccccc2C(=O)O1)n3cncc3C=C)C`
CWA RCSB PDB	6B7E	P0A6I6	292.3 Da LogP 3.36 TPSA 44.1	✓ Ro5	✓ Clean	`CC1([C@@H](c2ccccc2C(=O)O1)n3cncc3C(F)F)C`
CWG RCSB PDB	6B7D	P0A6I6	248.7 Da LogP 3.42 TPSA 35.0	✓ Ro5	✓ Clean	`Cc1c(c(nnc1c2ccc(cc2)Cl)OC)C`
CWJ RCSB PDB	6B7B	P0A6I6	161.2 Da LogP 2.48 TPSA 25.0	✓ Ro5	✓ Clean	`Cc1cc2cc(ccc2[nH]1)OC`
CWM RCSB PDB	6B7A	P0A6I6	148.2 Da LogP 1.58 TPSA 48.9	✓ Ro5	✓ Clean	`Cc1[nH]c2c(n1)cccc2O`
CWP RCSB PDB	6B7C	P0A6I6	256.3 Da LogP 1.92 TPSA 71.4	✓ Ro5	✓ Clean	`Cc1ccc2c(n1)[nH]c(n2)NCc3cc(nn3C)C`
EX7 RCSB PDB	6CCQ	P0A6I6	272.7 Da LogP 3.71 TPSA 48.9	✓ Ro5	✓ Clean	`c1cc(cc(c1)Cl)CCc2[nH]c3c(n2)cccc3O`
EXD RCSB PDB	6CCS	P0A6I6	202.1 Da LogP 2.29 TPSA 48.9	✓ Ro5	✓ Clean	`c1cc2c(c(c1)O)[nH]c(n2)C(F)(F)F`
EXG RCSB PDB	6CCL	P0A6I6	209.3 Da LogP 2.48 TPSA 30.7	✓ Ro5	✓ Clean	`c1ccc(cc1)Cn2cnc3c2cccn3`
EXJ RCSB PDB	6CCK	P0A6I6	328.8 Da LogP 3.13 TPSA 96.0	✓ Ro5	✓ Clean	`CC1=Nc2nc(nn2C(=O)C1)NC(CC#N)c3cccc(c3)Cl`
EXP RCSB PDB	6CCM	P0A6I6	334.2 Da LogP 2.79 TPSA 72.2	✓ Ro5	✓ Clean	`CC1=Nc2nc(nn2C(=O)C1)NCc3cccc(c3)Br`
EXS RCSB PDB	6CCN	P0A6I6	307.4 Da LogP 0.31 TPSA 118.5	✓ Ro5	✓ Clean	`CC(C)(CO)[C@H](C(=O)NCCc1[nH]c2c(n1)cccc2O)O`
EXV RCSB PDB	6CCO	P0A6I6	322.4 Da LogP 4.02 TPSA 86.2	✓ Ro5	✓ Clean	`c1cc(cc(c1)C(=O)O)[C@H]2CCC[C@@H]2c3[nH]c4c(n3)…`
F0V RCSB PDB	6CHQ	P0A6I6	364.9 Da LogP 4.15 TPSA 57.7	✓ Ro5	✓ Clean	`Cc1ccc(cc1Cl)Nc2cc(nc3[n+]2nc([nH]3)Cc4ccccc4)C`
F0Y RCSB PDB	6CHP	P0A6I6	432.5 Da LogP 4.35 TPSA 106.9	✓ Ro5	✓ Clean	`Cc1ccc2c(n1)[nH]c(n2)NC(CC#N)c3cccc(c3)CC4CCN(C…`
F14 RCSB PDB	6CHO	P0A6I6	391.4 Da LogP 4.39 TPSA 90.6	✓ Ro5	✓ Clean	`CC1=Nc2nc(nn2C(=O)C1)N[C@H](C)c3cccc(c3)Oc4ccc(…`
F1D RCSB PDB	6CHN	P0A6I6	451.5 Da LogP 3.09 TPSA 134.7	✓ Ro5	✓ Clean	`CC1=Nc2nc(nn2C(=O)C1)NC(CC#N)c3cccc(c3)OC4CCN(C…`
F1V RCSB PDB	6CHM	P0A6I6	274.4 Da LogP 2.88 TPSA 54.1	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)NCCc1c[nH]c2c1cc(cc2)OC`
F6D RCSB PDB	6CKW	P0A6I6	477.0 Da LogP 4.27 TPSA 126.2	✓ Ro5	✓ Clean	`Cc1cc(n2c(n1)nc(n2)NC(CC#N)c3cccc(c3)Cl)NCC(c4c…`
POP RCSB PDB	6J3M	A0A059ZFC5	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=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).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC38435336 ZINC	1.000	209.3 Da LogP 2.48 TPSA 30.7	✓ Ro5	✓ Clean	`c1ccc(Cn2cnc3ncccc32)cc1`
ZINC4487699 ZINC	1.000	274.4 Da LogP 2.88 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)C(C)(C)C)c2c1`
ZINC76214064 ZINC	1.000	202.1 Da LogP 2.29 TPSA 48.9	✓ Ro5	✓ Clean	`Oc1cccc2nc(C(F)(F)F)[nH]c12`
ZINC8252 ZINC	0.809	286.3 Da LogP 2.40 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)C(F)(F)F)c2c1`
ZINC49478729 ZINC	0.771	290.4 Da LogP 3.24 TPSA 63.3	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)OC(C)(C)C)c2c1`
ZINC519625 ZINC	0.761	248.3 Da LogP 2.07 TPSA 63.3	✓ Ro5	✓ Clean	`COC(=O)NCCc1c[nH]c2ccc(OC)cc12`
ZINC57060 ZINC	0.761	232.3 Da LogP 1.86 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(C)=O)c2c1`
ZINC1385145 ZINC	0.755	289.4 Da LogP 2.82 TPSA 66.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)NC(C)(C)C)c2c1`
ZINC290474 ZINC	0.745	233.3 Da LogP 1.39 TPSA 80.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(N)=O)c2c1`
ZINC8879695 ZINC	0.745	260.3 Da LogP 2.49 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)C(C)C)c2c1`
ZINC317413 ZINC	0.729	246.3 Da LogP 2.25 TPSA 54.1	✓ Ro5	✓ Clean	`CCC(=O)NCCc1c[nH]c2ccc(OC)cc12`
ZINC9875576 ZINC	0.729	247.3 Da LogP 1.65 TPSA 66.2	✓ Ro5	✓ Clean	`CNC(=O)NCCc1c[nH]c2ccc(OC)cc12`
ZINC10146611 ZINC	0.725	350.5 Da LogP 4.45 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)c3ccc(C(C)(C)C)cc3)c2c1`
ZINC10146664 ZINC	0.714	260.3 Da LogP 2.64 TPSA 54.1	✓ Ro5	✓ Clean	`CCCC(=O)NCCc1c[nH]c2ccc(OC)cc12`
ZINC287711 ZINC	0.714	324.4 Da LogP 3.16 TPSA 63.3	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NCCc2c[nH]c3ccc(OC)cc23)cc1`
ZINC3641660 ZINC	0.714	247.3 Da LogP 0.79 TPSA 80.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)CN)c2c1`
ZINC4856838 ZINC	0.714	261.3 Da LogP 1.99 TPSA 57.4	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)N(C)C)c2c1`
ZINC1518851 ZINC	0.710	203.3 Da LogP 3.47 TPSA 25.0	✓ Ro5	✓ Clean	`COc1ccc2[nH]c(C(C)(C)C)cc2c1`
ZINC100637954 ZINC	0.700	206.1 Da LogP -2.05 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@@H](O)[C@@H](O)CO)C(O)=C1O`
ZINC100637955 ZINC	0.700	206.1 Da LogP -2.05 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@@H](O)[C@H](O)CO)C(O)=C1O`
ZINC100637956 ZINC	0.700	206.1 Da LogP -2.05 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@H](O)[C@@H](O)CO)C(O)=C1O`
ZINC100637957 ZINC	0.700	206.1 Da LogP -2.05 TPSA 127.5	✓ Ro5	✓ Clean	`O=C1O[C@H]([C@H](O)[C@H](O)CO)C(O)=C1O`
ZINC10146608 ZINC	0.700	354.4 Da LogP 3.17 TPSA 72.6	✓ Ro5	✓ Clean	`COc1cc(OC)cc(C(=O)NCCc2c[nH]c3ccc(OC)cc23)c1`
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`
ZINC202422814 ZINC	0.700	244.3 Da LogP 2.02 TPSA 54.1	✓ Ro5	✓ Clean	`C=CC(=O)NCCc1c[nH]c2ccc(OC)cc12`
ZINC8765348 ZINC	0.700	308.4 Da LogP 3.08 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)Cc3ccccc3)c2c1`
ZINC1887503626 ZINC	0.692	260.3 Da LogP 1.23 TPSA 66.6	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)[C@H]3CO3)c2c1`
ZINC1887503627 ZINC	0.692	260.3 Da LogP 1.23 TPSA 66.6	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)[C@@H]3CO3)c2c1`
ZINC76214040 ZINC	0.688	254.1 Da LogP 3.60 TPSA 28.7	✓ Ro5	✓ Clean	`FC(F)(F)c1nc2cccc(C(F)(F)F)c2[nH]1`
ZINC94217 ZINC	0.688	232.3 Da LogP 1.20 TPSA 86.9	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=N)N)c2c1`
ZINC1783593 ZINC	0.686	290.3 Da LogP 1.70 TPSA 91.4	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)CCC(=O)O)c2c1`
ZINC4487700 ZINC	0.686	326.4 Da LogP 3.22 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)Cc3ccc(F)cc3)c2c1`
ZINC4814513 ZINC	0.686	387.3 Da LogP 3.84 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)Cc3ccc(Br)cc3)c2c1`
ZINC75063 ZINC	0.686	294.4 Da LogP 3.15 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)c3ccccc3)c2c1`
ZINC79051016 ZINC	0.686	278.4 Da LogP 2.20 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)CSC)c2c1`
ZINC8253 ZINC	0.686	258.3 Da LogP 2.25 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)C3CC3)c2c1`
ZINC115226262 ZINC	0.680	272.3 Da LogP 1.91 TPSA 64.4	✓ Ro5	✓ Clean	`CC1(C)OC(=O)c2ccccc2[C@@H]1n1cncc1CO`
ZINC115226266 ZINC	0.680	272.3 Da LogP 1.91 TPSA 64.4	✓ Ro5	✓ Clean	`CC1(C)OC(=O)c2ccccc2[C@H]1n1cncc1CO`
ZINC43175532 ZINC	0.680	286.3 Da LogP 2.12 TPSA 81.4	✓ Ro5	✓ Clean	`CC1(C)OC(=O)c2ccccc2[C@H]1n1cncc1C(=O)O`
ZINC43175534 ZINC	0.680	286.3 Da LogP 2.12 TPSA 81.4	✓ Ro5	✓ Clean	`CC1(C)OC(=O)c2ccccc2[C@@H]1n1cncc1C(=O)O`
ZINC648323866 ZINC	0.678	394.5 Da LogP 3.53 TPSA 96.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)c3ccc(NC(=O)C(C)(C)C)nc3…`
ZINC408650 ZINC	0.673	347.4 Da LogP 3.56 TPSA 69.9	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)Cc3c[nH]c4ccccc34)c2c1`
ZINC4487680 ZINC	0.673	312.3 Da LogP 3.29 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)c3ccc(F)cc3)c2c1`
ZINC4814474 ZINC	0.673	373.2 Da LogP 3.91 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)c3ccc(Br)cc3)c2c1`
ZINC4866159 ZINC	0.673	308.4 Da LogP 3.46 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)c3ccc(C)cc3)c2c1`
ZINC6847770 ZINC	0.673	342.8 Da LogP 3.73 TPSA 54.1	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)Cc3ccc(Cl)cc3)c2c1`
ZINC8764617 ZINC	0.673	354.4 Da LogP 3.17 TPSA 72.6	✓ Ro5	✓ Clean	`COc1ccc2[nH]cc(CCNC(=O)c3c(OC)cccc3OC)c2c1`
ZINC8765178 ZINC	0.673	352.4 Da LogP 3.48 TPSA 63.3	✓ Ro5	✓ Clean	`COc1ccc(CCC(=O)NCCc2c[nH]c3ccc(OC)cc23)cc1`
ZINC96405929 ZINC	0.673	286.4 Da LogP 3.19 TPSA 54.1	✓ Ro5	✓ Clean	`CC/C=C(\C)C(=O)NCCc1c[nH]c2ccc(OC)cc12`

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_3495

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

Pathways

Metabolic context

Sequence

Functional annotations

Enzyme Commission (EC)

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