Protein target profile

VK055_4699

dihydrodipicolinate synthase

Genome: KpATCC43816 Gene: dapA AIK83233.1 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt W9BBZ5

Export view

Length 280

Pocket druggability 0.574

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 5 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 92.0% of genes in this genome. 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 (%): 29.167 Lower values reduce human off-target concern.
Human E-value: 3.67e-22
Gut microbiome similarity: 3.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 91.786 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: 98.77 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 0.574

Structure 6UE0

Pocket Pocket 1

P2Rank 0.787

Structure 6UE0

Pocket Pocket 1

ColabFold model

FPocket 0.968 · Pocket 4

P2Rank 0.982 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 182 / 4744 genomes with a hit

Prevalence 3.8%

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 Lysine biosynthesis, more central than 92.0% of genes in this genome.

Relative network centrality 92.0% more central than 92.0% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MDENGNVCRTSLKKLIDYHVANGTSAIVSVGTTGESATLSHEEHGDVVMMTLELADGRIPVIAGTGANATAEAISLTKRFNDSGVVGCLTVTPYYNRPTQEGLFQHFKAIAEHTDLPQILYNVPSRTGCDMLPETVGRLAEIKNIVGIKEATGNLSRVHQIKELVSDDFILLSGDDATGMDFMQLGGVGVISVTANVAAREMADMCRLALAGQFAEARAINQRLMPLHTKLFVEPNPIPVKWGCKALGLVATDTLRLPMTPITDHGREAVTAALKHAGLL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

4.3.3.7

Gene Ontology (GO)

GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
GO:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
GO:0008840 Catalysis of the reaction: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O + H+.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0019877 OBSOLETE. The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

29 records

Show feature table

Start	End	DB	Term	Name
121	151	ProSitePatterns	PS00666	Dihydrodipicolinate synthase signature 2.
121	151	InterPro	IPR020625	Schiff base-forming aldolase, active site
26	43	ProSitePatterns	PS00665	Dihydrodipicolinate synthase signature 1.
26	43	InterPro	IPR020624	Schiff base-forming aldolase, conserved site
1	276	Pfam	PF00701	Dihydrodipicolinate synthetase family
1	276	InterPro	IPR002220	DapA-like
1	276	Hamap	MF_00418	4-hydroxy-tetrahydrodipicolinate synthase [dapA].
1	276	InterPro	IPR005263	4-hydroxy-tetrahydrodipicolinate synthase, DapA
2	279	PANTHER	PTHR12128	DIHYDRODIPICOLINATE SYNTHASE
2	279	InterPro	IPR002220	DapA-like
1	276	NCBIfam	TIGR00674	4-hydroxy-tetrahydrodipicolinate synthase
59	77	PRINTS	PR00146	Dihydrodipicolinate synthase signature
59	77	InterPro	IPR002220	DapA-like
91	107	PRINTS	PR00146	Dihydrodipicolinate synthase signature
91	107	InterPro	IPR002220	DapA-like
116	133	PRINTS	PR00146	Dihydrodipicolinate synthase signature
116	133	InterPro	IPR002220	DapA-like
23	44	PRINTS	PR00146	Dihydrodipicolinate synthase signature
23	44	InterPro	IPR002220	DapA-like
1	280	SUPERFAMILY	SSF51569	Aldolase
1	280	PIRSF	PIRSF001365	DHDPS
1	280	InterPro	IPR002220	DapA-like
1	280	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	280	InterPro	IPR013785	Aldolase-type TIM barrel
1	278	SMART	SM01130	DHDPS_2
1	278	InterPro	IPR002220	DapA-like
1	280	FunFam	G3DSA:3.20.20.70:FF:000046	4-hydroxy-tetrahydrodipicolinate synthase
1	274	CDD	cd00950	DHDPS
1	274	InterPro	IPR005263	4-hydroxy-tetrahydrodipicolinate synthase, DapA

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

0.982

Likely same site as FPocket 4 3.3 Å 43 shared residues 88% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.602

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.143

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:133-133 Proton donor/acceptor

UniProt: Active site:161-161 Schiff-base intermediate with substrate

UniProt: Binding site:203-203

UniProt: Binding site:45-45

UniProt: Site:106-106 L-lysine inhibitor binding

UniProt: Site:107-107 Part of a proton relay during catalysis

UniProt: Site:44-44 Part of a proton relay during catalysis

UniProt: Site:49-49 L-lysine inhibitor binding; via carbonyl oxygen

UniProt: Site:80-80 L-lysine inhibitor binding

UniProt: Site:84-84 L-lysine inhibitor binding

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 6UE0	X-ray	1.89 Å	AAA,BBB	100.0% 1-280	PDBe RCSB PDBj File	Viewing
ColabFold VK055_4699	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.

58 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2KT PDB via homolog 102.1 Da · LogP 0.05 · TPSA 54.4 Open detail RCSB PDB

3OH PDB via homolog Detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

LYZ PDB via homolog Detail RCSB PDB

OXL 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
2KT RCSB PDB	3TDF	D0CFC3	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CCC(=O)C(=O)O`
3OH RCSB PDB	3S8H	Q9I4W3	90.1 Da LogP -0.55 TPSA 57.5	✓ Ro5	✓ Clean	`C(CO)C(=O)O`
FLC RCSB PDB	4PFM	A9DKW4	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
LYZ RCSB PDB	3TCE	D0CFC3	162.2 Da LogP -1.50 TPSA 109.6	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)[C@H](CN)O`
OXL RCSB PDB	3U8G	D0CFC3	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`
PYR RCSB PDB	3RK8	D0CFC3	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=O)O`
TLA RCSB PDB	5T26	P0A6L2	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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL456197 ChEMBL	P0A6L2	—	226.2 Da LogP 0.79 TPSA 69.7	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/C(=O)/C=C/C(=O)OCC`

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
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`
ZINC32298862 ZINC	0.652	226.0 Da LogP 1.50 TPSA 26.3	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/I`
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`
ZINC4975987 ZINC	0.652	226.0 Da LogP 1.50 TPSA 26.3	✓ Ro5	✓ Clean	`CCOC(=O)/C=C\I`
ZINC4195949 ZINC	0.630	338.4 Da LogP -0.10 TPSA 93.2	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/C(=O)N1CCN(C(=O)/C=C/C(=O)OCC)CC1`
ZINC5113885 ZINC	0.630	307.3 Da LogP -2.32 TPSA 179.1	1 viol.	✓ Clean	`N[C@@H](CC[C@H](O)CNC[C@H](O)CC[C@H](N)C(=O)O)C…`
ZINC5113891 ZINC	0.630	307.3 Da LogP -2.32 TPSA 179.1	1 viol.	✓ Clean	`N[C@@H](CC[C@@H](O)CNC[C@H](O)CC[C@H](N)C(=O)O)…`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC115979184 ZINC	0.615	200.2 Da LogP 1.45 TPSA 52.6	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/C(=O)OC(C)(C)C`
ZINC136715593 ZINC	0.593	304.4 Da LogP 3.67 TPSA 52.6	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/C(C)=C/C=C/C=C(C)/C=C/C(=O)OCC`
ZINC2159520 ZINC	0.593	274.4 Da LogP 3.53 TPSA 43.4	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/C(=O)c1c(C)c(C)c(C)c(C)c1C`
ZINC33380881 ZINC	0.593	274.4 Da LogP 3.53 TPSA 43.4	✓ Ro5	✓ Clean	`CCOC(=O)/C=C\C(=O)c1c(C)c(C)c(C)c(C)c1C`
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`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC1670412 ZINC	0.577	254.3 Da LogP 2.79 TPSA 52.6	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/CCCC/C=C/C(=O)OCC`
ZINC17300545 ZINC	0.577	254.3 Da LogP 2.79 TPSA 52.6	✓ Ro5	✓ Clean	`CCOC(=O)/C=C\CCCC/C=C/C(=O)OCC`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC8615431 ZINC	0.577	254.3 Da LogP 2.79 TPSA 52.6	✓ Ro5	✓ Clean	`CCOC(=O)/C=C\CCCC/C=C\C(=O)OCC`
ZINC12506611 ZINC	0.571	201.1 Da LogP 0.10 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](CC[C@@H](O)C(F)(F)F)C(=O)O`
ZINC12506613 ZINC	0.571	201.1 Da LogP 0.10 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](CC[C@@H](O)C(F)(F)F)C(=O)O`
ZINC12506615 ZINC	0.571	201.1 Da LogP 0.10 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](CC[C@H](O)C(F)(F)F)C(=O)O`
ZINC12506617 ZINC	0.571	201.1 Da LogP 0.10 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](CC[C@H](O)C(F)(F)F)C(=O)O`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC14510370 ZINC	0.556	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCO`
ZINC1531061 ZINC	0.556	216.3 Da LogP 2.96 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCO`
ZINC1610426 ZINC	0.556	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCO`
ZINC1684804 ZINC	0.556	217.5 Da LogP 2.48 TPSA 26.3	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/C(Cl)(Cl)Cl`
ZINC2168567 ZINC	0.556	202.3 Da LogP 2.57 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCO`
ZINC3861297 ZINC	0.556	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCO`
ZINC4284502 ZINC	0.556	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCO`
ZINC5287109 ZINC	0.556	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCCO`
ZINC2028757 ZINC	0.552	215.2 Da LogP 0.50 TPSA 85.2	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/C(=N/O)C(=O)OCC`
ZINC26896999 ZINC	0.552	234.2 Da LogP 1.82 TPSA 52.6	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/C(F)=C(\F)C(=O)OCC`
ZINC100135524 ZINC	0.542	200.2 Da LogP 1.45 TPSA 52.6	✓ Ro5	✓ Clean	`CCCOC(=O)/C=C\C(=O)OCCC`
ZINC4404469 ZINC	0.542	200.2 Da LogP 1.45 TPSA 52.6	✓ Ro5	✓ Clean	`CCCOC(=O)/C=C/C(=O)OCCC`
ZINC2040347175 ZINC	0.536	274.3 Da LogP 2.84 TPSA 52.6	✓ Ro5	✓ Clean	`CCOC(=O)C=Cc1ccc(C=CC(=O)OCC)cc1`
ZINC96301090 ZINC	0.536	200.2 Da LogP 0.07 TPSA 89.3	✓ Ro5	✓ Clean	`N[C@H](CC[C@@H](N)C(F)(F)F)C(=O)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_4699

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

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence