Protein target profile

VK055_3645

4-aminobutyrate transaminase

Genome: KpATCC43816 Gene: AIK82200.1 gabT2 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt A0A0H3GYJ5

Export view

Length 421

Pocket druggability 0.076

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 56 total records

Functional annotation 0 EC 7 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

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 95.4% of genes in this genome. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Structure available Experimental + ColabFold model Review the complete evidence below

Risks to review

Human similarity Top human hit identity: 33.103%. Microbiome similarity 121 of 4744 screened genomes (2.6%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.08. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.23.

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 (%): 33.103 Lower values reduce human off-target concern.
Human E-value: 2.79e-15
Gut microbiome similarity: 2.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 46.963 Higher values support similarity to known essential genes.
DEG E-value: 1.11e-135 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 98.33 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 0.076

Structure 6WJ8

Pocket Pocket 7

P2Rank 0.225

Structure 6WJ8

Pocket Pocket 1

ColabFold model

FPocket 0.26 · Pocket 21

P2Rank 0.417 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 121 / 4744 genomes with a hit

Prevalence 2.6%

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

Metabolic context: more central than 95.4% of genes in this genome.

Relative network centrality 95.4% more central than 95.4% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKSSELNQRRQQATPRGVGVMCNYFVEKAENATLWDIEGNEVIDFAAGIAVLNTGHRHPKVVAAVADQLQAFTHTAYQIVPYESYVSLAERINDLAPIDGPAKTAFFTTGAEAVENAVKIARAYTGRPGLITFGGGFHGRTFMTMALTGKVAPYKIGFGPFPGSVYHGVYPNAAHGVTTADALKSLERIFKADIAPDQVAAIILEPIQGEGGFNVAPADFMQALRDLCDTHGILLIADEVQTGFARTGKLFAMQHYEVKPDLMTMAKSLAGGFPLSGVVGRAEVMDAPAPGGLGGTYAGNPLAVAAAHAVLDVIAEEQLCQRAEQLGSHLQEVLNQARATCPAIVDVRGRGSMVAVEFNDPQTGEPSPEFTRQVQQKAQENGLLLLSCGVYGNVIRFLYPLTIPDTQFSKALDILARVLKS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0009448 The chemical reactions and pathways involving gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms.
GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
GO:0003867 OBSOLETE. Catalysis of the reaction: 4-aminobutanoate + amino group acceptor = succinate semialdehyde + amino acid.
GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
GO:0034386 Catalysis of the reaction: 2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate semialdehyde.
GO:0042802 Binding to an identical protein or proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
125	421	PIRSF	PIRSF000521	Transaminase_4ab_Lys_Orn
125	421	InterPro	IPR005814	Aminotransferase class-III
1	128	PIRSF	PIRSF000521	Transaminase_4ab_Lys_Orn
1	128	InterPro	IPR005814	Aminotransferase class-III
235	272	ProSitePatterns	PS00600	Aminotransferases class-III pyridoxal-phosphate attachment site.
235	272	InterPro	IPR005814	Aminotransferase class-III
5	415	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
5	415	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
58	317	FunFam	G3DSA:3.40.640.10:FF:000013	4-aminobutyrate aminotransferase
20	419	Pfam	PF00202	Aminotransferase class-III
20	419	InterPro	IPR005814	Aminotransferase class-III
23	420	SUPERFAMILY	SSF53383	PLP-dependent transferases
23	420	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
6	419	CDD	cd00610	OAT_like
6	419	InterPro	IPR005814	Aminotransferase class-III
58	317	Gene3D	G3DSA:3.40.640.10	-
58	317	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
8	420	NCBIfam	TIGR00700	4-aminobutyrate--2-oxoglutarate transaminase
8	420	InterPro	IPR004632	4-aminobutyrate aminotransferase, bacterial
23	420	PANTHER	PTHR11986	AMINOTRANSFERASE CLASS III

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.225

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.184

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.181

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.016

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.01

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.417

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.388

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.194

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.187

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.022

Show in viewer

Surrounding area

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 6WJ8	X-ray	2.59 Å	A,B,C,D	100.0% 1-421	PDBe RCSB PDBj File	Viewing
ColabFold VK055_3645	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

ABU PDB via homolog 103.1 Da · LogP -0.19 · TPSA 63.3 Open detail RCSB PDB

IK2 PDB via homolog Detail RCSB PDB

PLZ PDB via homolog Detail RCSB PDB

PMP PDB via homolog Detail RCSB PDB

SSN 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
ABU RCSB PDB	4ATQ	A1R958	103.1 Da LogP -0.19 TPSA 63.3	✓ Ro5	✓ Clean	`C(CC(=O)O)CN`
IK2 RCSB PDB	1SFF	P22256	322.2 Da LogP -0.19 TPSA 158.4	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNOCC(=O)O)O`
PLZ RCSB PDB	6J2V	Q8NT35	334.3 Da LogP 0.66 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNCCCC(=O)O)O`
PMP RCSB PDB	1SZK	P22256	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)O`
SSN RCSB PDB	3Q8N	A0QQ04	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`C(CC(=O)O)C=O`
TAR RCSB PDB	6WOP	D0CCF6	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
ZINC13357569 ZINC	0.778	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCC(=O)O`
ZINC1763117 ZINC	0.778	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCC(=O)O`
ZINC1845814 ZINC	0.778	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCC(=O)O`
ZINC22048354 ZINC	0.778	229.4 Da LogP 3.32 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCC(=O)O`
ZINC34552398 ZINC	0.778	257.4 Da LogP 4.10 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCC(=O)O`
ZINC34628306 ZINC	0.778	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCC(=O)O`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3074822 ZINC	0.667	229.3 Da LogP 2.11 TPSA 80.4	✓ Ro5	✓ Clean	`NCCCCCC(=O)CCCCCC(=O)O`
ZINC4822737 ZINC	0.667	313.5 Da LogP 4.45 TPSA 80.4	✓ Ro5	✓ Clean	`NCCCCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC1532708 ZINC	0.620	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC13512355 ZINC	0.619	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`O=CCCCCCCCCCC(=O)O`
ZINC1532705 ZINC	0.600	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC1529497 ZINC	0.588	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	0.588	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC1593115 ZINC	0.588	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	0.588	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	0.588	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	0.588	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	0.588	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC40470158 ZINC	0.577	216.3 Da LogP 0.49 TPSA 92.4	✓ Ro5	✓ Clean	`NCCCC(=O)NCCCCCC(=O)O`
ZINC2114966 ZINC	0.576	332.2 Da LogP 0.99 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(/C=N/CCCC(=O)O)c1O`
ZINC1656021 ZINC	0.571	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C)c1O`
ZINC78311249 ZINC	0.565	203.3 Da LogP -0.54 TPSA 92.6	✓ Ro5	✓ Clean	`NCCCN(CCCN)CCC(=O)O`
ZINC13433578 ZINC	0.550	201.3 Da LogP 1.68 TPSA 80.4	✓ Ro5	✓ Clean	`NC(=O)CCCCCCCCC(=O)O`
ZINC201768036 ZINC	0.542	279.3 Da LogP -0.12 TPSA 100.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCCC(=O)O`
ZINC1532514 ZINC	0.538	247.1 Da LogP 0.52 TPSA 117.0	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C=O)c1O`
ZINC1703342 ZINC	0.526	202.2 Da LogP 1.07 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCCC(=O)O`
ZINC2508031 ZINC	0.526	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCC(=O)O`
ZINC13526937 ZINC	0.519	357.5 Da LogP 1.94 TPSA 121.5	✓ Ro5	✓ Clean	`NCCCCCC(=O)NCCCCCC(=O)NCCCCCC(=O)O`
ZINC1532906 ZINC	0.519	244.3 Da LogP 1.27 TPSA 92.4	✓ Ro5	✓ Clean	`NCCCCCC(=O)NCCCCCC(=O)O`
ZINC40479778 ZINC	0.519	272.4 Da LogP 2.05 TPSA 92.4	✓ Ro5	✓ Clean	`NCCCCCCC(=O)NCCCCCCC(=O)O`
ZINC1529331 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529334 ZINC	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)O)[C@H](O)C(=O)O`
ZINC26897400 ZINC	0.500	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC3074813 ZINC	0.500	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC34423725 ZINC	0.500	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC4822898 ZINC	0.500	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900 ZINC	0.500	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC79832968 ZINC	0.500	203.2 Da LogP 0.82 TPSA 100.6	✓ Ro5	✓ Clean	`NC(CCCC(=O)O)CCCC(=O)O`
ZINC82505156 ZINC	0.500	215.3 Da LogP -0.57 TPSA 69.8	✓ Ro5	✓ Clean	`NCCCN1CCN(CCC(=O)O)CC1`

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_3645

Promising target candidate with multiple supporting evidence streams.

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

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence