Protein target profile

VK055_2464

guanosine monophosphate reductase

Genome: KpATCC43816 Gene: AIK81061.1 guaC 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GRS0

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Length 347

Pocket druggability 0.659

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 79 total records

Functional annotation 0 EC 5 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

Central metabolic position More central than 96.9% of genes in this genome. 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. Moderate predicted binding pocket FPocket selected-pocket score 0.66. This supports review but is not experimental validation. 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 (%): 87.5 Lower values reduce human off-target concern.
Human E-value: 2.28e-18
Gut microbiome similarity: 3.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 42.009 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.28 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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 0.659

Structure A0A0H3GRS0

Pocket Pocket 13

P2Rank 0.952

Structure A0A0H3GRS0

Pocket Pocket 1

ColabFold model

FPocket 0.603 · Pocket 9

P2Rank 0.953 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 170 / 4744 genomes with a hit

Prevalence 3.6%

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 96.9% of genes in this genome.

Relative network centrality 96.9% more central than 96.9% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELEREFTFKHSGLTWSGVPIIAANMDTVGTFSMAKALATFGILTAVHKHYTAEEWLAFTQGASADVLKHVMVSTGTSDADFEKTQQILSQNPQLNFVCIDVANGYSEHFVQFVAKAREAWPQKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTIVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRVQEQENRVFNSL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0003920 Catalysis of the reaction: IMP + NADP+ + NH4 = GMP + 2 H+ + NADPH.
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: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:1902560 An oxidoreductase complex which is capable of GMP reductase activity. It catalyses the irreversible reaction: GMP + 2 H+ + NADPH => IMP + NADP+ + NH4.
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.

18 records

Show feature table

Start	End	DB	Term	Name
1	345	Hamap	MF_00596	GMP reductase [guaC].
1	345	InterPro	IPR005993	GMP reductase
6	336	SUPERFAMILY	SSF51412	Inosine monophosphate dehydrogenase (IMPDH)
9	336	CDD	cd00381	IMPDH
9	336	InterPro	IPR001093	IMP dehydrogenase/GMP reductase
1	345	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	345	InterPro	IPR013785	Aldolase-type TIM barrel
1	345	FunFam	G3DSA:3.20.20.70:FF:000012	GMP reductase
9	338	Pfam	PF00478	IMP dehydrogenase / GMP reductase domain
9	338	InterPro	IPR001093	IMP dehydrogenase/GMP reductase
2	344	NCBIfam	TIGR01305	GMP reductase
2	344	InterPro	IPR005993	GMP reductase
176	188	ProSitePatterns	PS00487	IMP dehydrogenase / GMP reductase signature.
176	188	InterPro	IPR015875	IMP dehydrogenase / GMP reductase, conserved site
1	347	PIRSF	PIRSF000235	GMP_reductase
1	347	InterPro	IPR005993	GMP reductase
2	345	PANTHER	PTHR43170	GMP REDUCTASE
7	344	SMART	SM01240	IMPDH_2

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 #13

0.659

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Surrounding area

Site 2 FPocket #11

0.382

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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

0.952

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Surrounding area

Site 2 P2Rank #2

0.283

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Surrounding area

Site 3 P2Rank #3

0.155

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Surrounding area

Site 4 P2Rank #4

0.097

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Surrounding area

Site 5 P2Rank #5

0.019

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Surrounding area

Residue sets

UniProt: Active site:186-186 Thioimidate intermediate

UniProt: Binding site:108-131

UniProt: Binding site:181-181

UniProt: Binding site:183-183

UniProt: Binding site:216-239

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.953

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Surrounding area

Site 2 P2Rank #2

0.137

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Surrounding area

Site 3 P2Rank #3

0.095

Likely same site as FPocket 9 2.1 Å 7 shared residues 88% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.085

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Surrounding area

Site 5 P2Rank #5

0.038

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Surrounding area

Residue sets

UniProt: Active site:186-186 Thioimidate intermediate

UniProt: Binding site:108-131

UniProt: Binding site:181-181

UniProt: Binding site:183-183

UniProt: Binding site:216-239

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

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
AlphaFold DB AF_A0A0H3GRS0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2464	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.

79 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 29 records from similar proteins

Structural ligands 13 0 loaded crystals

Measured bioactivity 16 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2EY PDB via homolog 366.8 Da · LogP 3.90 · TPSA 72.8 Open detail RCSB PDB

2F1 PDB via homolog Detail RCSB PDB

2F2 PDB via homolog Detail RCSB PDB

5GP PDB via homolog Detail RCSB PDB

8L1 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
2EY RCSB PDB	4MYA	A0A6L8P2U9	366.8 Da LogP 3.90 TPSA 72.8	✓ Ro5	✓ Clean	`C[C@H](c1cn(nn1)c2ccc(cc2)Cl)OC3=CC(=O)Nc4c3ccc…`
2F1 RCSB PDB	4MZ1	Q0P9J4	373.3 Da LogP 5.54 TPSA 41.1	1 viol.	✓ Clean	`CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(cc2)Br`
2F2 RCSB PDB	4MZ8	Q0P9J4	46.1 Da LogP 0.26 TPSA 9.2	✓ Ro5	✓ Clean	`COC`
5GP RCSB PDB	2A1Y	Q81JJ9	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
8L1 RCSB PDB	5UUV	A0A6L8P2U9	496.9 Da LogP 6.74 TPSA 86.6	1 viol.	✓ Clean	`C/C(=N\O)/c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)c3…`
8L4 RCSB PDB	5UUZ	A0A6L8P2U9	346.8 Da LogP 3.70 TPSA 97.2	✓ Ro5	✓ Clean	`[H]/N=C(/c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(cc2)Cl)\…`
8LA RCSB PDB	5URS	A0A6L8P2U9	477.0 Da LogP 3.25 TPSA 120.3	✓ Ro5	✓ Clean	`CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)O[C@@H…`
C91 RCSB PDB	4MZ8	Q0P9J4	378.4 Da LogP 4.89 TPSA 59.8	✓ Ro5	✓ Clean	`c1ccc2cc(ccc2c1)NC(=O)Cn3c4ccccc4nc3c5ccccn5`
IMP RCSB PDB	4MY1	A0A6L8P2U9	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
JQS RCSB PDB	6MGU	A0A6L8P2U9	366.2 Da LogP -2.07 TPSA 209.9	1 viol.	✓ Clean	`c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…`
MLI RCSB PDB	4MY9	A0A6L8P2U9	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
TAR RCSB PDB	3TSD	A0A6L8P2U9	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@@H](C(=O)O)O)(C(=O)O)O`
XMP RCSB PDB	5UPX	Q926Y9	365.2 Da LogP -3.44 TPSA 201.2	1 viol.	✓ Clean	`c1[nH+]c2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=…`

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
2F0 ChEMBL	A0A6L8P2U9	8.82 ~1.5 nM	388.9 Da LogP 3.69 TPSA 116.8	✓ Ro5	✓ Clean	`C/C(=N\O)/c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)C(…`
CHEMBL2178644 ChEMBL	A0A6L8P2U9	8.70 ~2.0 nM	413.8 Da LogP 5.61 TPSA 73.7	1 viol.	✓ Clean	`C/C(=N\O)c1cccc(C(C)(C)NC(=O)Nc2ccc(Cl)c(C(F)(F…`
P68 ChEMBL	A0A6L8P2U9	8.64 ~2.3 nM	390.3 Da LogP 4.70 TPSA 73.7	✓ Ro5	✓ Clean	`C/C(=N\O)/c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(cc2)Br`
Q67 ChEMBL	A0A6L8P2U9	8.30 ~5.0 nM	427.3 Da LogP 5.64 TPSA 80.1	1 viol.	✓ Clean	`C[C@@H](C(=O)Nc1ccc2c(c1)nc(o2)c3ccncc3)Nc4cccc…`
CHEMBL2178652 ChEMBL	A0A6L8P2U9	8.10 ~7.9 nM	396.8 Da LogP 6.45 TPSA 41.1	1 viol.	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(Cl)c(C(F)(F)F)…`
CHEMBL2348627 ChEMBL	A0A6L8P2U9	8.00 ~10.0 nM	428.3 Da LogP 5.60 TPSA 77.2	1 viol.	✓ Clean	`C[C@H](Oc1cccc(Cl)c1Cl)C(=O)Nc1ccc2nc(-c3ccncc3…`
CHEMBL2348796 ChEMBL	A0A6L8P2U9	8.00 ~10.0 nM	428.3 Da LogP 5.60 TPSA 77.2	1 viol.	✓ Clean	`C[C@H](Oc1cccc(Cl)c1Cl)C(=O)Nc1ccc2oc(-c3ccncc3…`
CHEMBL3329564 ChEMBL	A0A6L8P2U9	7.85 ~14.1 nM	438.8 Da LogP 4.86 TPSA 120.4	✓ Ro5	✓ Clean	`CC(Oc1cccc([N+](=O)[O-])c1Cl)C(=O)Nc1ccc2oc(-c3…`
Q21 ChEMBL	A0A6L8P2U9	7.77 ~17.0 nM	409.4 Da LogP 5.45 TPSA 77.3	1 viol.	✓ Clean	`C[C@@H](C(=O)Nc1ccc2c(c1)nc(o2)c3ccncc3)Oc4cccc…`
2YA ChEMBL	A0A6L8P2U9	7.42 ~38.0 nM	366.8 Da LogP 3.85 TPSA 66.9	✓ Ro5	Alert	`C[C@H](c1cn(nn1)c2ccc(cc2)Cl)Oc3cc[n+](c4c3cccc…`
CHEMBL3329561 ChEMBL	A0A6L8P2U9	7.02 ~95.5 nM	380.3 Da LogP 5.25 TPSA 73.7	1 viol.	✓ Clean	`C/C(=N\O)c1cccc(C(C)(C)NC(=O)Nc2ccc(Cl)c(Cl)c2)…`
CHEMBL3329563 ChEMBL	A0A6L8P2U9	7.00 ~100.0 nM	472.0 Da LogP 3.98 TPSA 97.3	✓ Ro5	✓ Clean	`C/C(=N\O)c1cccc(C(C)(C)NC(=O)Nc2ccc(Cl)c(C(=O)N…`
CHEMBL557281 ChEMBL	A0A6L8P2U9	6.92 ~120.2 nM	353.8 Da LogP 5.54 TPSA 38.3	1 viol.	✓ Clean	`CC(C)C(Oc1cccc2ccccc12)C(=O)Nc1ccc(Cl)cc1`
CHEMBL564117 ChEMBL	A0A6L8P2U9	6.80 ~158.5 nM	351.8 Da LogP 5.29 TPSA 38.3	1 viol.	✓ Clean	`O=C(Nc1ccc(Cl)cc1)C(Oc1cccc2ccccc12)C1CC1`
CHEMBL2348631 ChEMBL	A0A6L8P2U9	6.52 ~302.0 nM	430.3 Da LogP 5.05 TPSA 80.3	1 viol.	✓ Clean	`C[C@H](Oc1cccc(Cl)c1Cl)C(=O)Nc1cccc(NC(=O)c2ccn…`
CHEMBL2348634 ChEMBL	A0A6L8P2U9	6.05 ~891.3 nM	343.4 Da LogP 4.63 TPSA 68.0	✓ Ro5	✓ Clean	`C[C@H](C(=O)Nc1ccc2oc(-c3ccncc3)nc2c1)c1ccccc1`

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
ZINC14951284 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC1532551 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC16969369 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC4228242 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@…`
ZINC43020550 ZINC	1.000	366.8 Da LogP 3.85 TPSA 66.9	✓ Ro5	Alert	`C[C@@H](Oc1cc[n+]([O-])c2ccccc12)c1cn(-c2ccc(Cl…`
ZINC4353761 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC8614392 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC106686432 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP…`
ZINC12958393 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)O…`
ZINC35024781 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024785 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024786 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)…`
ZINC4261903 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC80601236 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC95921560 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC1178445 ZINC	0.837	351.5 Da LogP 4.73 TPSA 70.2	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(NC(C)=O)cc2)c1`
ZINC454732 ZINC	0.800	336.4 Da LogP 4.98 TPSA 58.2	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(C(C)=O)cc2)c1`
ZINC77319466 ZINC	0.792	364.3 Da LogP -0.78 TPSA 163.0	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(=S)[nH]cnc32)[…`
ZINC4724858 ZINC	0.783	312.4 Da LogP 4.92 TPSA 41.1	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(F)cc2)c1`
ZINC28539620 ZINC	0.780	328.4 Da LogP 3.74 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccccc1`
ZINC286872 ZINC	0.766	337.4 Da LogP 3.88 TPSA 84.2	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(C(N)=O)cc2)c1`
ZINC28539779 ZINC	0.759	342.4 Da LogP 4.05 TPSA 59.8	✓ Ro5	✓ Clean	`Cc1cccc(NC(=O)Cn2c(-c3ccccn3)nc3ccccc32)c1`
ZINC73310355 ZINC	0.755	362.8 Da LogP 4.39 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccc(Cl)cc1`
ZINC225456440 ZINC	0.750	282.3 Da LogP -1.61 TPSA 122.5	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@H](O)[…`
ZINC230149202 ZINC	0.750	282.3 Da LogP -1.61 TPSA 122.5	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)…`
ZINC266599 ZINC	0.750	324.4 Da LogP 4.79 TPSA 50.4	✓ Ro5	✓ Clean	`C=C(C)c1cccc(C(C)(C)NC(=O)Nc2ccc(OC)cc2)c1`
ZINC23144110 ZINC	0.745	362.8 Da LogP 4.39 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1cccc(Cl)c1`
ZINC46084891 ZINC	0.740	329.4 Da LogP 3.13 TPSA 72.7	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccccn1`
ZINC12501413 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC17484666 ZINC	0.732	384.5 Da LogP 4.95 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2cscn2)nc2ccccc21)Nc1ccc2ccccc2c1`
ZINC2159505 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496 ZINC	0.732	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC23144100 ZINC	0.727	370.4 Da LogP 3.94 TPSA 76.9	✓ Ro5	✓ Clean	`CC(=O)c1ccc(NC(=O)Cn2c(-c3ccccn3)nc3ccccc32)cc1`
ZINC4531685 ZINC	0.727	332.2 Da LogP -1.12 TPSA 159.8	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1C[C@H](O)[C@H](COP(=O)…`
ZINC4531686 ZINC	0.727	332.2 Da LogP -1.12 TPSA 159.8	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1C[C@H](O)[C@H](COP(=O)(…`
ZINC4531687 ZINC	0.727	332.2 Da LogP -1.12 TPSA 159.8	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1C[C@@H](O)[C@H](COP(=O)…`
ZINC33979258 ZINC	0.714	364.2 Da LogP -2.45 TPSA 200.2	1 viol.	✓ Clean	`O=c1[nH]c(O)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)…`
ZINC33979259 ZINC	0.714	364.2 Da LogP -2.45 TPSA 200.2	1 viol.	✓ Clean	`O=c1[nH]c(O)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)…`
ZINC78920152 ZINC	0.714	364.2 Da LogP -2.45 TPSA 200.2	1 viol.	✓ Clean	`O=c1[nH]c(O)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)…`
ZINC8614391 ZINC	0.709	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1nc[nH]c2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC8614393 ZINC	0.709	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1nc[nH]c2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC23144061 ZINC	0.707	412.4 Da LogP 4.64 TPSA 69.0	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1ccc(OC(F)(F)F)…`
ZINC28539789 ZINC	0.707	396.4 Da LogP 4.76 TPSA 59.8	✓ Ro5	✓ Clean	`O=C(Cn1c(-c2ccccn2)nc2ccccc21)Nc1cccc(C(F)(F)F)…`
ZINC8652273 ZINC	0.706	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@…`

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_2464

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

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