Protein target profile

VK055_2857

2',3'-cyclic-nucleotide 2'-phosphodiesterase

Genome: KpATCC43816 Gene: AIK81446.1 cpdB 3D evidence: Experimental + ColabFold model Metabolism 8 reactions UniProt A6THC4

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Length 647

Pocket druggability 0.579

Metabolic reactions 8

Chokepoint No

Direct ligand evidence 1 59 total records

Functional annotation 0 EC 7 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

Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Direct ligand evidence 1 direct ligand records. Strong known ligand: co-crystal structure 1 PDB record(s) show a ligand actually co-crystallized with this exact protein - real experimental evidence, not a computational prediction. 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 (%): 34.266 Lower values reduce human off-target concern.
Human E-value: 3.31e-08
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 62.366 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Periplasmic

Structure confidence

ColabFold pLDDT: 94.33 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 0.579

Structure 3JYF

Pocket Pocket 1

P2Rank 0.434

Structure 3JYF

Pocket Pocket 1

ColabFold model

FPocket 0.967 · Pocket 1

P2Rank 0.989 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 144 / 4744 genomes with a hit

Prevalence 3.0%

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

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

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MIKFSATLLATLIAASVNAATVDLRIMETTDLHSNMMDFDYYKDAATEKFGLVRTASLIEQARAEVKNSVLVDNGDVLQGSPLGDYMAAKGLKEGDVHPVYKAMNTLNYAVGNLGNHEFNYGLDFLHKALAGAKFPYVNANIIDAKTGKPMFTPYLIQNTRVVDSDGQSHTLRIGYIGFVPPQIMTWDKANLNGKVTVNDITETARKYIPEMRAKGADVVVVVAHSGLSADPYQAMAENSVYYLSQVPGVDAIMFGHAHAVFPGKDFANIKGADIAKGTLNGVPAVMPGMWGDHLGVVDLVLNNDSGKWQVTQSKAEARPIYDAVAKKSLAAEDGKLVAVLKADHDATREFVSKPIGKSADNMYSYLALVQDDPTVQVVNMAQKAYVEHYIQGDPDLAKLPVLSAAAPFKVGGRKNDPASFVEVEKGQLTFRNAADLYLYPNTLVVMKVSGKEVKEWLECSAGQFNQIDPASSKPQSLINWDGFRTYNFDVIDGVNYQIDVTQPARYDGECQMIHPQAERIKHLTFNGKPVDPQATFLVATNNYRAYGGKFAGTGESHIAFASPDENRSVLAAWIGAQSKKEGAIHPAADNNWRLAPIHSNTPLDIRFETSPGDKAAAFIKEKAQYPMRQVATDDIGFAIYQLDLSK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0009166 The chemical reactions and pathways resulting in the breakdown of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates).
GO:0016788 Catalysis of the hydrolysis of any ester bond.
GO:0008663 Catalysis of the reaction: nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate.
GO:0046872 Binding to a metal ion.
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:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0009117 The chemical reactions and pathways involving a nucleotide, a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic nucleotides (nucleoside cyclic phosphates).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
365	594	Gene3D	G3DSA:3.90.780.10	-
365	594	InterPro	IPR036907	5'-Nucleotidase, C-terminal domain superfamily
24	321	CDD	cd07410	MPP_CpdB_N
24	321	InterPro	IPR041827	CpdB, N-terminal metallophosphatase domain
16	354	FunFam	G3DSA:3.60.21.10:FF:000037	Bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
20	647	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
109	120	ProSitePatterns	PS00786	5'-nucleotidase signature 2.
109	120	InterPro	IPR006146	5'-Nucleotidase, conserved site
22	647	NCBIfam	TIGR01390	2',3'-cyclic-nucleotide 2'-phosphodiesterase
22	647	InterPro	IPR006294	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
355	597	SUPERFAMILY	SSF55816	5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain
355	597	InterPro	IPR036907	5'-Nucleotidase, C-terminal domain superfamily
24	36	ProSitePatterns	PS00785	5'-nucleotidase signature 1.
24	36	InterPro	IPR006146	5'-Nucleotidase, conserved site
14	595	PANTHER	PTHR11575	5'-NUCLEOTIDASE-RELATED
14	595	InterPro	IPR006179	5'-Nucleotidase/apyrase
15	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
24	259	Pfam	PF00149	Calcineurin-like phosphoesterase
24	259	InterPro	IPR004843	Calcineurin-like phosphoesterase domain, ApaH type
530	549	PRINTS	PR01607	Apyrase family signature
530	549	InterPro	IPR006179	5'-Nucleotidase/apyrase
243	266	PRINTS	PR01607	Apyrase family signature
243	266	InterPro	IPR006179	5'-Nucleotidase/apyrase
283	303	PRINTS	PR01607	Apyrase family signature
283	303	InterPro	IPR006179	5'-Nucleotidase/apyrase
22	40	PRINTS	PR01607	Apyrase family signature
22	40	InterPro	IPR006179	5'-Nucleotidase/apyrase
215	232	PRINTS	PR01607	Apyrase family signature
215	232	InterPro	IPR006179	5'-Nucleotidase/apyrase
428	451	PRINTS	PR01607	Apyrase family signature
428	451	InterPro	IPR006179	5'-Nucleotidase/apyrase
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	19	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
4	14	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	19	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
16	354	Gene3D	G3DSA:3.60.21.10	-
16	354	InterPro	IPR029052	Metallo-dependent phosphatase-like
356	550	Pfam	PF02872	5'-nucleotidase, C-terminal domain
356	550	InterPro	IPR008334	5'-Nucleotidase, C-terminal
19	353	SUPERFAMILY	SSF56300	Metallo-dependent phosphatases
19	353	InterPro	IPR029052	Metallo-dependent phosphatase-like
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
363	594	FunFam	G3DSA:3.90.780.10:FF:000002	Bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase

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 #1

0.579

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Surrounding area

Site 2 FPocket #12

0.526

Likely same site as P2Rank 2 1.1 Å 9 shared residues 100% 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

0.434

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Surrounding area

Site 2 P2Rank #2

0.063

Likely same site as FPocket 12 1.1 Å 9 shared residues 100% 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

0.989

Likely same site as FPocket 1 2.8 Å 28 shared residues 90% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.551

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Surrounding area

Site 3 P2Rank #3

0.339

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Surrounding area

Site 4 P2Rank #4

0.058

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Surrounding area

Site 5 P2Rank #5

0.029

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Surrounding area

Residue sets

UniProt: Binding site:116-116

UniProt: Binding site:225-225

UniProt: Binding site:257-257

UniProt: Binding site:259-259

UniProt: Binding site:31-31

UniProt: Binding site:33-33

UniProt: Binding site:76-76

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 3JYF	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
ColabFold VK055_2857	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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 1 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 9 1 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

TAM PDB co-crystal 163.2 Da · LogP -1.17 · TPSA 86.7 Open detail RCSB PDB

3D1 PDB via homolog Detail RCSB PDB

A12 PDB via homolog Detail RCSB PDB

ADN PDB via homolog Detail RCSB PDB

AKG 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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
TAM RCSB PDB	3JYF Open crystal	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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
3D1 RCSB PDB	4Q7F	Q2G1L5	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO)O)N`
A12 RCSB PDB	1HPU	P07024	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ADN RCSB PDB	1HO5	P07024	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
AKG RCSB PDB	3QFK	Q2G1L5	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
MLT RCSB PDB	5EQV	A0A5P8YBY3	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
MTN RCSB PDB	4WWL	P07024	264.4 Da LogP 1.82 TPSA 57.3	✓ Ro5	✓ Clean	`CC1(C=C(C(N1[O])(C)C)CSS(=O)(=O)C)C`
THM RCSB PDB	2Z1A	Q5SIP1	242.2 Da LogP -1.51 TPSA 104.6	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)O`
WO4 RCSB PDB	2USH	P07024	247.8 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][W](=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
ZINC2047403 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC2047673 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC2169830 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC3201876 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC3201878 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC3830178 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3830179 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3978047 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC3978048 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC3978049 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC4048240 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC8580514 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC895113 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC896706 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC970363 ZINC	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC4188096 ZINC	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188103 ZINC	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4188112 ZINC	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188116 ZINC	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4804742 ZINC	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)…`
ZINC4804743 ZINC	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)[…`
ZINC4804744 ZINC	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O…`
ZINC4804745 ZINC	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O)…`
ZINC4809089 ZINC	0.833	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](S)[C@H]1O`
ZINC4809090 ZINC	0.833	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](S)[C@H]1O`
ZINC4809091 ZINC	0.833	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](S)[C@@H]1O`
ZINC4809092 ZINC	0.833	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](S)[C@@H]…`
ZINC13470207 ZINC	0.814	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](N)[C@H]1O`
ZINC14418140 ZINC	0.814	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](N)[C@H]1O`
ZINC79682926 ZINC	0.814	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](N)[C@@H]1O`
ZINC16928956 ZINC	0.810	258.3 Da LogP -0.14 TPSA 87.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=S`
ZINC5085194 ZINC	0.805	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CF)O2)c(=O)[nH]c1=O`
ZINC5085195 ZINC	0.805	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CF)O2)c(=O)[nH]c1=O`
ZINC5085196 ZINC	0.805	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CF)O2)c(=O)[nH]c1=O`
ZINC5085197 ZINC	0.805	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CF)O2)c(=O)[nH]c1=O`
ZINC12618466 ZINC	0.795	269.2 Da LogP -1.00 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](F)[C@@H]1O`
ZINC11677083 ZINC	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](F)[C@@H](CO)O2)c(=O)[nH]c1…`
ZINC11677088 ZINC	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](F)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC17187169 ZINC	0.791	241.2 Da LogP -1.55 TPSA 110.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](N)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC1725270 ZINC	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](F)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC2130970 ZINC	0.791	241.2 Da LogP -1.55 TPSA 110.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](N)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC25054 ZINC	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](F)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC3785451 ZINC	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](F)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC4537463 ZINC	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](F)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC4537467 ZINC	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](F)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC56790 ZINC	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](F)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC5833725 ZINC	0.791	255.3 Da LogP -1.29 TPSA 96.4	✓ Ro5	✓ Clean	`CN[C@H]1C[C@@H](n2cc(C)c(=O)[nH]c2=O)O[C@H]1CO`
ZINC5833727 ZINC	0.791	255.3 Da LogP -1.29 TPSA 96.4	✓ Ro5	✓ Clean	`CN[C@H]1C[C@H](n2cc(C)c(=O)[nH]c2=O)O[C@H]1CO`
ZINC5833731 ZINC	0.791	255.3 Da LogP -1.29 TPSA 96.4	✓ Ro5	✓ Clean	`CN[C@@H]1C[C@@H](n2cc(C)c(=O)[nH]c2=O)O[C@H]1CO`
ZINC6667024 ZINC	0.791	256.3 Da LogP -0.86 TPSA 93.5	✓ Ro5	✓ Clean	`COC[C@H]1O[C@@H](n2cc(C)c(=O)[nH]c2=O)C[C@@H]1O`

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_2857

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

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