Protein target profile

VK055_4939

cytidine deaminase

Genome: KpATCC43816 Gene: AIK83465.1 cdd 3D evidence: Experimental + ColabFold model Metabolism 3 reactions UniProt A6TBN1

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Length 286

Pocket druggability 0.587

Metabolic reactions 3

Chokepoint Yes

Direct ligand evidence 0 75 total records

Functional annotation 0 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 99.2% 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: Hit
Human identity (%): 33.036 Lower values reduce human off-target concern.
Human E-value: 8.75e-10
Gut microbiome similarity: 2.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 51.19 Higher values support similarity to known essential genes.
DEG E-value: 1.63e-82 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 98.21 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 0.587

Structure 6K63

Pocket Pocket 3

P2Rank 0.479

Structure 6K63

Pocket Pocket 1

ColabFold model

FPocket 0.615 · Pocket 5

P2Rank 0.338 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 123 / 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

Attractive metabolic target: catalyzes a producing chokepoint reaction in Pyrimidine metabolism, no isoenzyme backup detected, more central than 99.2% of genes in this genome.

Relative network centrality 99.2% more central than 99.2% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTTLAADLQAAIAPMLADPHFPALLEADQVATLQHATGLDEDALAFALLPLAAACARPDLSHFNVGAIARGVSGRWYFGGNMEFLGATMQQTVHAEQSAISHAWLRGETSLRAITVNYTPCGHCRQFMNELNSGLALRIHLPGREAHALEHYLPDAFGPKDLEIKTLLMDEQDHGFPVSGDALTQAAIQAANRCHAPYSHSPSGVALELKDGTIFSGSYAENAAFNPTLPPLQGALNLLSLNGYDYPAIQRAILAEKADAALIQWDATVATLKALGCHNIERVLLG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 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:0004126 Catalysis of the reaction: cytidine + H+ + H2O = uridine + NH4 and deoxycytidine + H+ + H2O = deoxyuridine + NH4+.
GO:0008270 Binding to a zinc ion (Zn).
GO:0009972 OBSOLETE. The removal of amino group in the presence of water.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
172	286	Gene3D	G3DSA:3.40.140.10	Cytidine Deaminase, domain 2
1	284	Hamap	MF_01558	Cytidine deaminase [cdd].
1	284	InterPro	IPR020797	Cytidine deaminase, bacteria
178	286	ProSiteProfiles	PS51747	Cytidine and deoxycytidylate deaminases domain profile.
178	286	InterPro	IPR002125	Cytidine and deoxycytidylate deaminase domain
144	285	SUPERFAMILY	SSF53927	Cytidine deaminase-like
144	285	InterPro	IPR016193	Cytidine deaminase-like
61	144	CDD	cd01283	cytidine_deaminase
94	128	ProSitePatterns	PS00903	Cytidine and deoxycytidylate deaminases zinc-binding region signature.
94	128	InterPro	IPR016192	APOBEC/CMP deaminase, zinc-binding
180	226	PANTHER	PTHR11644	CYTIDINE DEAMINASE
23	276	NCBIfam	TIGR01355	cytidine deaminase
23	276	InterPro	IPR006263	Cytidine deaminase, homodimeric
177	284	FunFam	G3DSA:3.40.140.10:FF:000006	Cytidine deaminase
6	141	SUPERFAMILY	SSF53927	Cytidine deaminase-like
6	141	InterPro	IPR016193	Cytidine deaminase-like
40	160	ProSiteProfiles	PS51747	Cytidine and deoxycytidylate deaminases domain profile.
40	160	InterPro	IPR002125	Cytidine and deoxycytidylate deaminase domain
6	285	PIRSF	PIRSF006334	Cdd_plus_pseudo
185	244	CDD	cd01283	cytidine_deaminase
52	131	Pfam	PF00383	Cytidine and deoxycytidylate deaminase zinc-binding region
52	131	InterPro	IPR002125	Cytidine and deoxycytidylate deaminase domain
21	171	FunFam	G3DSA:3.40.140.10:FF:000007	Cytidine deaminase
21	171	Gene3D	G3DSA:3.40.140.10	Cytidine Deaminase, domain 2
149	268	Pfam	PF08211	Cytidine and deoxycytidylate deaminase zinc-binding region
149	268	InterPro	IPR013171	Cytidine/deoxycytidylate deaminase, zinc-binding domain

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 #3

0.587

Likely same site as P2Rank 3 5.2 Å 5 shared residues 56% of smaller site

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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

0.479

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Surrounding area

Site 2 P2Rank #2

0.086

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Surrounding area

Site 3 P2Rank #3

0.066

Likely same site as FPocket 3 5.2 Å 5 shared residues 56% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.037

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Surrounding area

Site 5 P2Rank #5

0.006

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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

0.338

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Surrounding area

Site 2 P2Rank #2

0.151

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Surrounding area

Site 3 P2Rank #3

0.039

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Surrounding area

Site 4 P2Rank #4

0.034

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Surrounding area

Site 5 P2Rank #5

0.025

Likely same site as FPocket 5 7.4 Å 5 shared residues 56% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:104-104 Proton donor

UniProt: Binding site:102-102

UniProt: Binding site:129-129

UniProt: Binding site:132-132

UniProt: Binding site:89-91

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 6K63	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
ColabFold VK055_4939	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.

75 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 25 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 16 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

CTD PDB via homolog 242.2 Da · LogP -1.96 · TPSA 117.9 Open detail RCSB PDB

CTN PDB via homolog Detail RCSB PDB

DHZ PDB via homolog Detail RCSB PDB

NH3 PDB via homolog Detail RCSB PDB

THU 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
CTD RCSB PDB	1ALN	P0ABF6	242.2 Da LogP -1.96 TPSA 117.9	✓ Ro5	✓ Clean	`C1=CN(C(=O)C=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
CTN RCSB PDB	2FR6	P56389	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
DHZ RCSB PDB	1CTT	P0ABF6	230.2 Da LogP -2.04 TPSA 102.3	✓ Ro5	✓ Clean	`C1C=CN(C(=O)N1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO)…`
NH3 RCSB PDB	2FR6	P56389	17.0 Da LogP 0.16 TPSA 35.0	✓ Ro5	✓ Clean	`N`
THU RCSB PDB	1JTK	P19079	230.2 Da LogP -1.60 TPSA 99.1	✓ Ro5	✓ Clean	`C1CN(C(=O)NC1=O)C2C[C@@H]([C@H](O2)CO)O`
TYU RCSB PDB	2FR5	P56389	248.2 Da LogP -2.84 TPSA 122.5	✓ Ro5	✓ Clean	`C1CN(C(=O)N[C@@H]1O)[C@H]2[C@@H]([C@@H]([C@H](O…`
URD RCSB PDB	1ZAB	P56389	243.2 Da LogP -2.26 TPSA 107.3	✓ Ro5	✓ Clean	`C1C(=O)C=CN(C1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
URI RCSB PDB	2FR6	P56389	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
ZEB RCSB PDB	1CTU	P0ABF6	246.2 Da LogP -2.72 TPSA 122.5	✓ Ro5	✓ Clean	`C1=CN(C(=O)N[C@@H]1O)C2[C@@H]([C@@H]([C@H](O2)C…`

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
CHEMBL604436 ChEMBL	P56389	10.00 ~0.1 nM	286.3 Da LogP -3.54 TPSA 130.1	✓ Ro5	✓ Clean	`OC[C@H]1OC(N2C=NC3C(O)CN=CNC32)[C@H](O)[C@@H]1O`
CHEMBL2311129 ChEMBL	P56389	7.70 ~20.0 nM	262.3 Da LogP -2.80 TPSA 122.5	✓ Ro5	✓ Clean	`O=C1NCC(O)CCN1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
CHEMBL610997 ChEMBL	P56389	7.16 ~69.2 nM	244.2 Da LogP -1.99 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1NCC=CCN1C1O[C@H](CO)[C@@H](O)[C@H]1O`
CHEMBL3658871 ChEMBL	P32320	7.00 ~100.0 nM	244.2 Da LogP -1.99 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1NCC=CCN1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
CHEMBL3658873 ChEMBL	P32320	6.85 ~141.3 nM	246.2 Da LogP -1.02 TPSA 82.0	✓ Ro5	✓ Clean	`O=C1NCC=CCN1[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1F`
CHEMBL2311128 ChEMBL	P56389	6.82 ~151.4 nM	248.2 Da LogP -2.84 TPSA 122.5	✓ Ro5	✓ Clean	`O=C1NC(O)CCN1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
CHEMBL3237548 ChEMBL	P32320	6.70 ~199.5 nM	250.2 Da LogP -1.86 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1N[C@H](O)CCN1[C@@H]1O[C@H](CO)[C@@H](O)[C@H…`
CHEMBL3665107 ChEMBL	P32320	6.70 ~199.5 nM	250.2 Da LogP -1.86 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1N[C@H](O)CCN1C1O[C@H](CO)[C@@H](O)[C@@H]1F`
CHEMBL3658870 ChEMBL	P32320	6.62 ~239.9 nM	264.2 Da LogP -0.72 TPSA 82.0	✓ Ro5	✓ Clean	`O=C1NCC=CCN1[C@@H]1O[C@H](CO)[C@@H](O)C1(F)F`
CHEMBL2367576 ChEMBL	P56389	6.52 ~302.0 nM	246.3 Da LogP -1.77 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1NCCCCN1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
CHEMBL3237547 ChEMBL	P32320	6.40 ~398.1 nM	268.2 Da LogP -1.57 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1N[C@H](O)CCN1[C@@H]1O[C@H](CO)[C@@H](O)C1(F…`
CHEMBL3237549 ChEMBL	P32320	6.40 ~398.1 nM	250.2 Da LogP -1.86 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1N[C@H](O)CCN1[C@@H]1O[C@H](CO)[C@@H](O)[C@@…`
CHEMBL3665106 ChEMBL	P32320	6.40 ~398.1 nM	268.2 Da LogP -1.57 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1N[C@H](O)CCN1C1O[C@H](CO)[C@@H](O)C1(F)F`
CHEMBL3665108 ChEMBL	P32320	6.40 ~398.1 nM	268.2 Da LogP -1.57 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1NC(O)CCN1C1O[C@H](CO)[C@@H](O)C1(F)F`
CHEMBL3665114 ChEMBL	P32320	6.40 ~398.1 nM	250.2 Da LogP -1.86 TPSA 102.3	✓ Ro5	✓ Clean	`O=C1N[C@H](O)CCN1C1O[C@H](CO)[C@@H](O)[C@H]1F`
CHEMBL605877 ChEMBL	P56389	6.40 ~398.1 nM	260.2 Da LogP -2.67 TPSA 122.5	✓ Ro5	✓ Clean	`O=C1NC(CO)C=CN1C1O[C@H](CO)[C@@H](O)[C@H]1O`

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
ZINC11525575 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[n…`
ZINC11525576 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[…`
ZINC1446448 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)[…`
ZINC2565479 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O…`
ZINC2583633 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3834164 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O…`
ZINC3870261 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3870262 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O…`
ZINC3870263 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O…`
ZINC3870264 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=…`
ZINC3870927 ZINC	1.000	242.2 Da LogP -1.96 TPSA 117.9	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)c1`
ZINC6091549 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)[…`
ZINC6524831 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)…`
ZINC7998085 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC8613151 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)…`
ZINC8613153 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)[…`
ZINC895165 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)…`
ZINC13546398 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2F)c(=O)[…`
ZINC17174165 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2F)c(=O…`
ZINC195751891 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2F)c(=O)…`
ZINC21999985 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2F)c(=O)…`
ZINC2570870 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2F)c(=O)[…`
ZINC2572671 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2F)c(=O)…`
ZINC26657838 ZINC	0.800	243.2 Da LogP -2.89 TPSA 130.6	✓ Ro5	✓ Clean	`N[C@@H]1[C@H](O)[C@@H](CO)O[C@@H]1n1ccc(=O)[nH]…`
ZINC26657844 ZINC	0.800	243.2 Da LogP -2.89 TPSA 130.6	✓ Ro5	✓ Clean	`N[C@H]1[C@H](O)[C@@H](CO)O[C@@H]1n1ccc(=O)[nH]c…`
ZINC34085613 ZINC	0.800	243.2 Da LogP -2.89 TPSA 130.6	✓ Ro5	✓ Clean	`N[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1n1ccc(=O)[nH]c…`
ZINC34248194 ZINC	0.800	243.2 Da LogP -2.89 TPSA 130.6	✓ Ro5	✓ Clean	`N[C@@H]1[C@H](O)[C@H](CO)O[C@@H]1n1ccc(=O)[nH]c…`
ZINC34248196 ZINC	0.800	243.2 Da LogP -2.89 TPSA 130.6	✓ Ro5	✓ Clean	`N[C@@H]1[C@H](O)[C@H](CO)O[C@H]1n1ccc(=O)[nH]c1…`
ZINC34248198 ZINC	0.800	243.2 Da LogP -2.89 TPSA 130.6	✓ Ro5	✓ Clean	`N[C@H]1[C@H](O)[C@H](CO)O[C@@H]1n1ccc(=O)[nH]c1…`
ZINC34248200 ZINC	0.800	243.2 Da LogP -2.89 TPSA 130.6	✓ Ro5	✓ Clean	`N[C@H]1[C@H](O)[C@H](CO)O[C@H]1n1ccc(=O)[nH]c1=O`
ZINC34248202 ZINC	0.800	243.2 Da LogP -2.89 TPSA 130.6	✓ Ro5	✓ Clean	`N[C@H]1[C@H](O)[C@@H](CO)O[C@H]1n1ccc(=O)[nH]c1…`
ZINC4016691 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2F)c(=O)…`
ZINC5541271 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2F)c(=O)…`
ZINC5541274 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2F)c(=O…`
ZINC5541275 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2F)c(=O…`
ZINC5541279 ZINC	0.800	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2F)c(=…`
ZINC5106305 ZINC	0.789	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CF)[C@@H](O)[C@H]2O)c(=O)…`
ZINC5106307 ZINC	0.789	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CF)[C@@H](O)[C@H]2O)c(=O…`
ZINC5106312 ZINC	0.789	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CF)[C@@H](O)[C@@H]2O)c(=O…`
ZINC5106314 ZINC	0.789	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CF)[C@@H](O)[C@@H]2O)c(=…`
ZINC6524890 ZINC	0.786	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](F)[C@H]2O)c(=O)n1`
ZINC85475812 ZINC	0.786	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](F)[C@H]2O)c(=O)n1`
ZINC26277487 ZINC	0.775	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](F)[C@@H]2O)c(=O…`
ZINC28636439 ZINC	0.775	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](F)[C@@H]2O)c(=O)…`
ZINC34268369 ZINC	0.775	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](F)[C@H]2O)c(=O)[…`
ZINC6524827 ZINC	0.775	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](F)[C@H]2O)c(=O)…`
ZINC78143070 ZINC	0.775	246.2 Da LogP -1.87 TPSA 104.5	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](F)[C@H]2O)c(=O)[…`
ZINC257373216 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](O)[C@H](CO)O[C@H]1n1ccc(N)nc1=O`
ZINC4556822 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](n2ccc(N)nc2=O)O[C@@H](CO)[C@H]1O`
ZINC4556824 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@@H](O)[C@H](CO)O[C@@H]1n1ccc(N)nc1=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_4939

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 · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence