Protein target profile

VK055_0406

diacetyl reductase (S-acetoin forming)

Genome: KpATCC43816 Gene: AIK79032.1 budC 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt Q48436

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Length 256

Pocket druggability 0.457

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 56 total records

Functional annotation 1 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. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. 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 (%): 41.86 Lower values reduce human off-target concern.
Human E-value: 7.64e-11
Gut microbiome similarity: 3.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 40.784 Higher values support similarity to known essential genes.
DEG E-value: 3.27e-36 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.24 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 1GEG

Pocket Pocket 5

P2Rank 0.958

Structure 3WYE

Pocket Pocket 1

ColabFold model

FPocket 0.569 · Pocket 7

P2Rank 0.95 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 152 / 4744 genomes with a hit

Prevalence 3.2%

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 consuming chokepoint reaction in Butanoate metabolism, no isoenzyme backup detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKKVALVTGAGQGIGKAIALRLVKDGFAVAIADYNDATAKAVASEINQAGGRAMAVKVDVSDRDQVFAAVEQARKTLGGFDVIVNNAGVAPSTPIESITPEIVDKVYNINVKGVIWGIQAAVEAFKKEGHGGKIINACSQAGHVGNPELAVYSSSKFAVRGLTQTAARDLAPLGITVNGYCPGIVKTPMWAEIDRQVSEAAGKPLGYGTAEFAKRITLGRLSEPEDVAACVSYLASPDSDYMTGQSLLIDGGMVFN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1.1.1.304

Gene Ontology (GO)

GO:0045150 The chemical reactions and pathways resulting in the breakdown of acetoin, 3-hydroxy-2-butanone.
GO:0019152 Catalysis of the reaction: acetoin + NAD+ = diacetyl + NADH + H+. This reaction is catalyzed in the reverse direction.
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:0052588 Catalysis of the reaction: (S)-acetoin + NAD+ = diacetyl + H+ + NADH. This reaction is catalyzed in the reverse direction.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
20	256	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
78	89	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
78	89	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
152	171	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
152	171	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
132	140	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
132	140	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
1	256	FunFam	G3DSA:3.40.50.720:FF:000084	Short-chain dehydrogenase reductase
3	256	NCBIfam	TIGR02415	acetoin reductase
3	256	InterPro	IPR014007	Acetoin reductase
3	196	Pfam	PF00106	short chain dehydrogenase
3	196	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
1	256	CDD	cd05366	meso-BDH-like_SDR_c
1	256	Gene3D	G3DSA:3.40.50.720	-
139	167	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
139	167	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
12	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
173	190	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
173	190	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
4	21	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
4	21	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
126	142	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
126	142	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
78	89	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
152	171	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
217	237	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
217	237	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
3	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.
2	254	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
2	254	InterPro	IPR036291	NAD(P)-binding domain superfamily
2	255	PANTHER	PTHR24321	DEHYDROGENASES, SHORT CHAIN
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
4	11	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.

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

0.958

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #7

0.569

Likely same site as P2Rank 1 4.2 Å 20 shared residues 91% of smaller site

Show in viewer

Surrounding area

Site 2 FPocket #21

0.363

Unusual size

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Surrounding area

Site 3 FPocket #2

0.338

Likely same site as P2Rank 1 6.0 Å 18 shared residues 86% of smaller site

Unusual size

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:152-152 Proton acceptor

UniProt: Binding site:139-139

UniProt: Binding site:156-156

UniProt: Binding site:59-59

UniProt: Binding site:6-33

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 3WYE	X-ray	1.58 Å	A,B	100.0% 1-256	PDBe RCSB PDBj File	Viewing
PDB 1GEG	X-ray	1.70 Å	A,B,C,D,E,F,G,H	100.0% 1-256	PDBe RCSB PDBj File	Loaded
ColabFold VK055_0406	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

A6O PDB via homolog 314.4 Da · LogP 3.93 · TPSA 46.5 Open detail RCSB PDB

AOI PDB via homolog Detail RCSB PDB

F3V PDB via homolog Detail RCSB PDB

RM4 PDB via homolog Detail RCSB PDB

TAM 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
A6O RCSB PDB	6IHH	C0IR58	314.4 Da LogP 3.93 TPSA 46.5	✓ Ro5	✓ Clean	`CC[C@]1([C@H](CCC1=O)O)C/C=C/2\CCCc3c2ccc(c3)OC`
AOI RCSB PDB	1NFQ	P9WGT1	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](C[C@@H]1CC[C@@H]3[C@@H]2CC[C@]4(…`
F3V RCSB PDB	6CI9	A0QP46	73.1 Da LogP -0.47 TPSA 43.1	✓ Ro5	✓ Clean	`CC(=O)CN`
RM4 RCSB PDB	7DO7	C1DMX5	164.2 Da LogP -2.19 TPSA 90.2	✓ Ro5	✓ Clean	`C[C@H]1[C@@H]([C@H]([C@H]([C@H](O1)O)O)O)O`
TAM RCSB PDB	4BMN	C0IR58	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`
TLA RCSB PDB	5U9P	B4EEX4	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=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
ZINC1691401 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@]43…`
ZINC253497590 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@@H]1CC[C@H]1[C@H]2CC[C@@]2…`
ZINC253497948 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@]43…`
ZINC253928529 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@@H]4C[C@@H](O)CC[C@]…`
ZINC38145858 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC38145859 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC[C@H]4C[C@H](O)CC[C@@]…`
ZINC3849577 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@@H]1CC[C@@H]1[C@@H]2CC[C@]…`
ZINC3849581 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC[C@H]4C[C@@H](O)CC[C@@…`
ZINC3849584 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@@H](O)CC[C@@]…`
ZINC3849784 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC[C@H]4C[C@H](O)CC[C@@]…`
ZINC3849785 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC3861550 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC3861661 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC[C@H]4C[C@@H](O)CC[C@@]…`
ZINC3869419 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@@H]1CC[C@@H]1[C@@H]2CC[C@@…`
ZINC3875364 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC[C@@H]4C[C@H](O)CC[C@]3…`
ZINC4073949 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC[C@H]4C[C@@H](O)CC[C@@…`
ZINC4743888 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC[C@@H]4C[C@@H](O)CC[C@]…`
ZINC7996759 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@@H](O)CC[C@@]…`
ZINC81132361 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@@H]4C[C@@H](O)CC[C@@…`
ZINC81132362 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@@H]4C[C@@H](O)CC[C@@…`
ZINC82230076 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@@H]1CC[C@@H]1[C@@H]2CC[C@@…`
ZINC9231975 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H](O)C[C@@H]1CC[C@H]1[C@H]2CC[C@@]…`
ZINC948 ZINC	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@@H]4C[C@@H](O)CC[C@]…`
ZINC257345656 ZINC	0.854	304.5 Da LogP 4.35 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@]43…`
ZINC257345657 ZINC	0.854	304.5 Da LogP 4.35 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC257345658 ZINC	0.854	304.5 Da LogP 4.35 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@]43…`
ZINC257345659 ZINC	0.854	304.5 Da LogP 4.35 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC254714590 ZINC	0.721	292.4 Da LogP 4.94 TPSA 17.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](F)CC[C@@]4…`
ZINC257346299 ZINC	0.721	292.4 Da LogP 4.94 TPSA 17.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](F)CC[C@]43…`
ZINC257346300 ZINC	0.721	292.4 Da LogP 4.94 TPSA 17.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](F)CC[C@]43…`
ZINC257346301 ZINC	0.721	292.4 Da LogP 4.94 TPSA 17.1	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](F)CC[C@@]4…`
ZINC118914949 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@]2(C)[C@H]3CC[C@]4(C)C(=O)CC[…`
ZINC118914950 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@]2(C)[C@H]3CC[C@]4(C)C(=O)CC[C…`
ZINC118914951 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@]2(C)[C@@H](CC[C@H]3[C@@H]4C…`
ZINC118914952 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@]2(C)[C@@H](CC[C@H]3[C@@H]4CC…`
ZINC13399905 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@]2(C)[C@@H](CC[C@@H]3[C@@H]2C…`
ZINC2049238309 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@]2(C)[C@@H](CC[C@@H]3[C@@H]2C…`
ZINC2049238310 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@]2(C)[C@@H](CC[C@@H]3[C@@H]2C…`
ZINC245239066 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@]2(C)[C@@H](CC[C@@H]3[C@H]4C…`
ZINC245239069 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@]2(C)[C@@H](CC[C@@H]3[C@H]4CC…`
ZINC253611246 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@@]2(C)[C@@H](CC[C@H]3[C@H]2CC[…`
ZINC253611248 ZINC	0.711	316.5 Da LogP 4.80 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CC[C@@]2(C)[C@@H](CC[C@H]3[C@H]2CC…`
ZINC118930984 ZINC	0.698	306.4 Da LogP 2.93 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](C[C@@H](O)[C@H]4C[C@@H](O…`
ZINC118930985 ZINC	0.698	306.4 Da LogP 2.93 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](C[C@@H](O)[C@H]4C[C@H](O)…`
ZINC118930986 ZINC	0.698	306.4 Da LogP 2.93 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](C[C@@H](O)[C@@H]4C[C@@H](…`
ZINC118930987 ZINC	0.698	306.4 Da LogP 2.93 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](C[C@@H](O)[C@@H]4C[C@H](O…`
ZINC19943608 ZINC	0.696	304.4 Da LogP 3.14 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@H]3[C@@H](CC[C@@H]4C[C@@H](O)CC…`
ZINC2382313444 ZINC	0.696	304.5 Da LogP 4.21 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H]1C[C@@]2(C)C(=O)CC[C@H]2[C@@H]2CC[C@H]3C[…`
ZINC247643489 ZINC	0.696	304.4 Da LogP 3.14 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C…`
ZINC253614914 ZINC	0.696	304.4 Da LogP 3.14 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC(=O)[C@@H]3[C@H](CC[C@@H]4C[C@H](O)CC[…`

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_0406

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 · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence