Protein target profile

VK055_0788

3-oxoacyl-(Acyl-carrier-protein) reductase

Genome: KpATCC43816 Gene: AIK79411.1 fabG2 3D evidence: Experimental + ColabFold model Metabolism 10 reactions UniProt W8VGR4

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Length 244

Pocket druggability 0.892

Metabolic reactions 10

Chokepoint Yes

Direct ligand evidence 0 73 total records

Functional annotation 0 EC 4 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. Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.89, P2Rank 0.91). Use the 3D pocket comparison to verify whether they identify the same site. 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 90.8% of genes in this genome. 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: Hit
Human identity (%): 43.056 Lower values reduce human off-target concern.
Human E-value: 1.29e-07
Gut microbiome similarity: 1.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 46.122 Higher values support similarity to known essential genes.
DEG E-value: 2.13e-64 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.41 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 0.892

Structure 6T6N

Pocket Pocket 5

P2Rank 0.908

Structure 6T6P

Pocket Pocket 1

ColabFold model

FPocket 0.533 · Pocket 5

P2Rank 0.889 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 60 / 4744 genomes with a hit

Prevalence 1.3%

Cross-references

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

Pathways

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, more central than 90.8% of genes in this genome.

Relative network centrality 90.8% more central than 90.8% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKLASKTAIVTGAARGIGFGIAQVLAREGARVIIADRDAHGEAAAASLRESGAQALFISCNIAEKTQVEALFSQAEEAFGPVDILVNNAGINRDAMLHKLTEADWDTVIDVNLKGTFLCMQQAAIRMRERGAGRIINIASASWLGNVGQTNYSASKAGVVGMTKTACRELAKKGVTVNAICPGFIDTDMTRGVPENVWQIMISKIPAGYAGEAKDVGECVAFLASDGARYINGEVINVGGGMVL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0004316 Catalysis of the reaction: (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = 3-oxoacyl-[acyl-carrier protein] + NADPH + H+.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0032787 The chemical reactions and pathways involving monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
80	91	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
80	91	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
7	24	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
7	24	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
173	190	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
173	190	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
152	171	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
152	171	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
127	143	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
127	143	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
206	226	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
206	226	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
12	242	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
139	167	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
139	167	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
6	183	SMART	SM00822	This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
1	244	Gene3D	G3DSA:3.40.50.720	-
1	243	FunFam	G3DSA:3.40.50.720:FF:000115	3-oxoacyl-[acyl-carrier-protein] reductase FabG
80	91	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
133	141	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
133	141	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
152	171	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
1	243	PANTHER	PTHR42879	3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE
6	243	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
6	243	InterPro	IPR036291	NAD(P)-binding domain 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 · P2Rank

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

Site 1 P2Rank #1

0.908

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Surrounding area

Site 2 P2Rank #2

0.147

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Surrounding area

Site 3 P2Rank #3

0.109

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Surrounding area

Site 4 P2Rank #4

0.005

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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

0.889

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Surrounding area

Site 2 P2Rank #2

0.156

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Surrounding area

Site 3 P2Rank #3

0.071

Likely same site as FPocket 5 1.7 Å 9 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:15-15

UniProt: Binding site:152-152

UniProt: Binding site:156-156

UniProt: Binding site:17-17

UniProt: Binding site:185-185

UniProt: Binding site:187-187

UniProt: Binding site:36-36

UniProt: Binding site:61-61

UniProt: Binding site:62-62

UniProt: Binding site:88-88

All structural evidence 2 experimental · 1 predicted

Structural evidence

2 + 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 6T6P	X-ray	1.57 Å	A,B,C,D	100.0% 1-244	PDBe RCSB PDBj File	Viewing
PDB 6T6N	X-ray	2.50 Å	A,B,C,D,E,F,G,H	100.0% 1-244	PDBe RCSB PDBj File	Loaded
ColabFold VK055_0788	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.

73 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 23 records from similar proteins

Structural ligands 18 0 loaded crystals

Measured bioactivity 5 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

34X PDB via homolog 311.3 Da · LogP 3.05 · TPSA 85.0 Open detail RCSB PDB

36E PDB via homolog Detail RCSB PDB

36G PDB via homolog Detail RCSB PDB

36I PDB via homolog Detail RCSB PDB

36K 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
34X RCSB PDB	4BO8	O54438	311.3 Da LogP 3.05 TPSA 85.0	✓ Ro5	✓ Clean	`c1ccc(cc1)c2cn(c(n2)N)NC(=O)Nc3ccccc3F`
36E RCSB PDB	4BNT	O54438	186.1 Da LogP 2.58 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc2c(c1)[nH]c(n2)C(F)(F)F`
36G RCSB PDB	4BO4	O54438	282.3 Da LogP 3.68 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N2CCCc3c2cccc3`
36I RCSB PDB	4BNY	O54438	297.4 Da LogP 3.19 TPSA 38.2	✓ Ro5	✓ Clean	`c1ccc(cc1)c2nc3ccsc3c(n2)N4CCOCC4`
36K RCSB PDB	4BO2	O54438	310.4 Da LogP 3.71 TPSA 68.2	✓ Ro5	✓ Clean	`CCn1c2ccccc2nc1NC(=O)Nc3ccccc3OC`
36P RCSB PDB	4BO6	O54438	312.4 Da LogP 4.07 TPSA 33.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)CCN2C(=O)c3csc(n3)c4ccsc4`
3X3 RCSB PDB	4BO9	O54438	318.3 Da LogP 3.50 TPSA 66.0	✓ Ro5	✓ Clean	`c1ccc(cc1)n2nc(nn2)c3ccccc3OCc4ccco4`
8M5 RCSB PDB	4BNZ	O54438	250.3 Da LogP 3.43 TPSA 34.0	✓ Ro5	✓ Clean	`Cn1cc(c2c1cccc2)C(=O)Nc3ccccc3`
9KQ RCSB PDB	4BNU	O54438	273.3 Da LogP 2.88 TPSA 56.5	✓ Ro5	✓ Clean	`c1ccc(cc1)c2nc3ccccc3c(n2)n4cnnc4`
B3P RCSB PDB	4NBV	B3R6T4	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`C(CNC(CO)(CO)CO)CNC(CO)(CO)CO`
FXE RCSB PDB	4BO0	O54438	326.4 Da LogP 3.23 TPSA 77.4	✓ Ro5	✓ Clean	`Cn1c2cccc(c2c(n1)NC(=O)Nc3ccccc3OC)OC`
J2T RCSB PDB	4BO7	O54438	252.3 Da LogP 1.75 TPSA 68.0	✓ Ro5	✓ Clean	`c1cc2c(cc1Nc3ccc4nnnn4n3)CCC2`
MLH RCSB PDB	6T65	V5VHN7	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c2cc(c(cc2n(c1CN(C)C)c3ccccc3)Br)O`
NKH RCSB PDB	4BO1	O54438	342.8 Da LogP 4.16 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(c(cc1Cl)OC)NC(=O)c2cccc3c2nccc3`
O74 RCSB PDB	4BNX	O54438	347.8 Da LogP 4.53 TPSA 53.5	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=N/C(=C/3\C=CC=CC3=O)/N2)Nc4ccccc4…`
Q7U RCSB PDB	4BNV	O54438	300.7 Da LogP 3.87 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c2ccccc2nc1NC(=O)Nc3ccccc3Cl`
U98 RCSB PDB	4BO3	O54438	317.3 Da LogP 2.49 TPSA 85.1	✓ Ro5	✓ Clean	`c1cc(cc(c1)Nc2c(cccn2)S(=O)(=O)N)C(F)(F)F`
WI4 RCSB PDB	4BO5	O54438	271.7 Da LogP 3.06 TPSA 55.6	✓ Ro5	✓ Clean	`c1ccc(c(c1)Nc2ncnc(n2)n3cccc3)Cl`

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
KDH ChEMBL	Q965D6	6.52 ~302.0 nM	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`c1c(cc(c(c1O)O)O)[C@@H]2[C@@H](Cc3c(cc(cc3O2)O)…`
LU2 ChEMBL	Q965D6	6.10 ~794.3 nM	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`c1cc(c(cc1C2=CC(=O)c3c(cc(cc3O2)O)O)O)O`
CHEMBL129451 ChEMBL	Q965D6	6.00 ~1.0 µM	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
CHEMBL36327 ChEMBL	Q965D6	6.00 ~1.0 µM	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
NAR ChEMBL	Q965D6	—	272.3 Da LogP 2.51 TPSA 87.0	✓ Ro5	✓ Clean	`c1cc(ccc1[C@@H]2CC(=O)c3c(cc(cc3O2)O)O)O`

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
ZINC1233995 ZINC	1.000	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(O)cc12`
ZINC13152723 ZINC	1.000	310.4 Da LogP 3.71 TPSA 68.2	✓ Ro5	✓ Clean	`CCn1c(NC(=O)Nc2ccccc2OC)nc2ccccc21`
ZINC1399281 ZINC	1.000	297.4 Da LogP 3.19 TPSA 38.2	✓ Ro5	✓ Clean	`c1ccc(-c2nc(N3CCOCC3)c3sccc3n2)cc1`
ZINC18185774 ZINC	1.000	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC27923853 ZINC	1.000	300.7 Da LogP 3.87 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c(NC(=O)Nc2ccccc2Cl)nc2ccccc21`
ZINC318945 ZINC	1.000	282.3 Da LogP 3.68 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N1CCCc2ccccc21`
ZINC3870412 ZINC	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC3870413 ZINC	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC3870414 ZINC	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC3870415 ZINC	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC4521259 ZINC	1.000	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`OCC(CO)(CO)NCCCNC(CO)(CO)CO`
ZINC481463 ZINC	1.000	317.3 Da LogP 2.49 TPSA 85.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1cccnc1Nc1cccc(C(F)(F)F)c1`
ZINC7913991 ZINC	1.000	250.3 Da LogP 3.43 TPSA 34.0	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccccc2)c2ccccc21`
ZINC8231765 ZINC	1.000	342.8 Da LogP 4.16 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(NC(=O)c2cccc3cccnc23)c(OC)cc1Cl`
ZINC8429509 ZINC	1.000	312.4 Da LogP 4.07 TPSA 33.2	✓ Ro5	✓ Clean	`O=C(c1csc(-c2ccsc2)n1)N1CCc2ccccc21`
ZINC8723457 ZINC	1.000	252.3 Da LogP 1.75 TPSA 68.0	✓ Ro5	✓ Clean	`c1cc2c(cc1Nc1ccc3nnnn3n1)CCC2`
ZINC8726387 ZINC	1.000	273.3 Da LogP 2.88 TPSA 56.5	✓ Ro5	✓ Clean	`c1ccc(-c2nc(-n3cnnc3)c3ccccc3n2)cc1`
ZINC89647 ZINC	1.000	271.7 Da LogP 3.06 TPSA 55.6	✓ Ro5	✓ Clean	`Clc1ccccc1Nc1ncnc(-n2cccc2)n1`
ZINC9338279 ZINC	1.000	311.3 Da LogP 3.05 TPSA 85.0	✓ Ro5	✓ Clean	`Nc1nc(-c2ccccc2)cn1NC(=O)Nc1ccccc1F`
ZINC451821 ZINC	0.857	268.3 Da LogP 3.29 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N1CCc2ccccc21`
ZINC14436185 ZINC	0.854	472.4 Da LogP 2.54 TPSA 186.4	2 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC3978503 ZINC	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
ZINC4534390 ZINC	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)c…`
ZINC4544252 ZINC	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c1…`
ZINC8681494 ZINC	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
ZINC8453886 ZINC	0.849	431.3 Da LogP 4.65 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccc(C)cc2)c2cc(Br)c(O)c…`
ZINC14727965 ZINC	0.848	426.4 Da LogP 2.82 TPSA 156.9	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)cc1)…`
ZINC12534489 ZINC	0.833	307.4 Da LogP 3.39 TPSA 63.1	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(NC(=O)c2cn(C)c3ccccc23)cc1`
ZINC27923895 ZINC	0.833	335.2 Da LogP 4.52 TPSA 59.0	✓ Ro5	✓ Clean	`Cn1c(NC(=O)Nc2cccc(Cl)c2Cl)nc2ccccc21`
ZINC7917230 ZINC	0.833	264.3 Da LogP 3.74 TPSA 34.0	✓ Ro5	✓ Clean	`Cc1ccc(NC(=O)c2cn(C)c3ccccc23)cc1`
ZINC32497089 ZINC	0.811	278.3 Da LogP 2.79 TPSA 51.1	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccccc2)c(=O)c2ccccc21`
ZINC27923339 ZINC	0.800	340.4 Da LogP 3.72 TPSA 77.4	✓ Ro5	✓ Clean	`CCn1c(NC(=O)Nc2cc(OC)ccc2OC)nc2ccccc21`
ZINC5222178 ZINC	0.800	431.3 Da LogP 4.64 TPSA 43.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(OC)cc12`
ZINC95453238 ZINC	0.800	360.8 Da LogP 4.30 TPSA 60.5	✓ Ro5	✓ Clean	`COc1cc(NC(=O)c2cc(F)cc3cccnc23)c(OC)cc1Cl`
ZINC8074404 ZINC	0.795	293.3 Da LogP 2.53 TPSA 77.1	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccc(C(N)=O)cc2)c2ccccc21`
ZINC32726013 ZINC	0.789	251.3 Da LogP 2.83 TPSA 46.9	✓ Ro5	✓ Clean	`Cn1cc(C(=O)Nc2ccncc2)c2ccccc21`
ZINC15934558 ZINC	0.787	312.4 Da LogP 3.69 TPSA 50.8	✓ Ro5	✓ Clean	`COc1ccc(OC)c(NC(=O)N2CCCc3ccccc32)c1`
ZINC15934559 ZINC	0.787	312.4 Da LogP 3.69 TPSA 50.8	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)N2CCCc3ccccc32)c(OC)c1`
ZINC27923428 ZINC	0.784	344.8 Da LogP 4.36 TPSA 68.2	✓ Ro5	✓ Clean	`CCn1c(NC(=O)Nc2cc(Cl)ccc2OC)nc2ccccc21`
ZINC5875060 ZINC	0.780	281.4 Da LogP 3.96 TPSA 29.0	✓ Ro5	✓ Clean	`c1ccc(-c2nc(N3CCCC3)c3sccc3n2)cc1`
ZINC3871576 ZINC	0.778	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1cc(-c2ccc(O)cc2)oc2cc(O)cc(O)c12`
ZINC4348965 ZINC	0.775	270.3 Da LogP 3.11 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)O[C@H](c1ccc(O)cc1)CC2=O`
ZINC4348970 ZINC	0.775	270.3 Da LogP 3.11 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)O[C@@H](c1ccc(O)cc1)CC2=O`
ZINC2027558 ZINC	0.773	318.3 Da LogP 3.09 TPSA 79.3	✓ Ro5	✓ Clean	`O=S(=O)(O)c1cccnc1Nc1cccc(C(F)(F)F)c1`
ZINC16552269 ZINC	0.771	296.4 Da LogP 3.99 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccccc1NC(=O)N1CCCc2cc(C)ccc21`
ZINC6726962 ZINC	0.771	296.4 Da LogP 3.99 TPSA 41.6	✓ Ro5	✓ Clean	`COc1ccc(C)cc1NC(=O)N1CCCc2ccccc21`
ZINC12515506 ZINC	0.769	307.4 Da LogP 3.39 TPSA 63.1	✓ Ro5	✓ Clean	`CC(=O)Nc1cccc(NC(=O)c2cn(C)c3ccccc23)c1`
ZINC15934557 ZINC	0.766	296.4 Da LogP 4.07 TPSA 41.6	✓ Ro5	✓ Clean	`CCOc1ccccc1NC(=O)N1CCCc2ccccc21`
ZINC5903093 ZINC	0.762	309.4 Da LogP 4.74 TPSA 29.0	✓ Ro5	✓ Clean	`c1ccc(-c2nc(N3CCCCCC3)c3sccc3n2)cc1`
ZINC27646798 ZINC	0.761	313.4 Da LogP 2.90 TPSA 58.5	✓ Ro5	✓ Clean	`Oc1cccc(-c2nc(N3CCOCC3)c3sccc3n2)c1`

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_0788

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 · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence