Protein target profile

VK055_1987

oxygen-insensitive NAD(P)H nitroreductase

Genome: KpATCC43816 Gene: AIK80593.1 nfnB 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt A6T5Y2

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Length 217

Pocket druggability 0.435

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 65 total records

Functional annotation 0 EC 1 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 89.5% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. 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: No hit
Gut microbiome similarity: 1.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 29.744 Higher values support similarity to known essential genes.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 98.58 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 0.435

Structure 8DOR

Pocket Pocket 1

P2Rank 0.03

Structure 8DOR

Pocket Pocket 1

ColabFold model

FPocket 0.262 · Pocket 9

P2Rank 0.005 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 69 / 4744 genomes with a hit

Prevalence 1.5%

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 89.5% of genes in this genome, no human homolog detected.

Relative network centrality 89.5% more central than 89.5% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MDIVSVALKRYSTKAFDATKKLTAGEAEQLKTLLQYSPSSTNSQPWHFIVASTDEGKARVAKAASGTYVFNERKILDASHVVVFCAKTAMDDAWLQRVVDQEEADGRFATPDAKAANHKGRTFFADMHRKELKDDDQWMAKQVYLNVGNFLLGVAAMGLDAVPIEGVDFAILDEEFDLKAQGYTSLVVVPVGHHSVEDFNATLPKSRLPQSTTITEI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

Gene Ontology (GO)

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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

10 records

Show feature table

Start	End	DB	Term	Name
2	211	CDD	cd02149	NfsB-like
2	211	InterPro	IPR033878	Oxygen-insensitive NAD(P)H nitroreductase NfsB-like
3	210	PANTHER	PTHR23026	NADPH NITROREDUCTASE
8	193	Pfam	PF00881	Nitroreductase family
8	193	InterPro	IPR029479	Nitroreductase
1	216	SUPERFAMILY	SSF55469	FMN-dependent nitroreductase-like
1	216	InterPro	IPR000415	Nitroreductase-like
1	217	Gene3D	G3DSA:3.40.109.10	NADH Oxidase
1	217	InterPro	IPR000415	Nitroreductase-like
1	217	FunFam	G3DSA:3.40.109.10:FF:000002	Oxygen-insensitive NAD(P)H nitroreductase

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

0.435

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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

0.03

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Surrounding area

Site 2 P2Rank #2

0.023

Show in viewer

Surrounding area

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #9

0.262

Show in viewer

Surrounding area

Site 2 FPocket #5

0.259

Show in viewer

Surrounding area

Site 3 FPocket #13

0.235

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Surrounding area

Residue sets

UniProt: Binding site:10-10

UniProt: Binding site:12-12

UniProt: Binding site:14-14

UniProt: Binding site:165-165

UniProt: Binding site:166-166

UniProt: Binding site:205-205

UniProt: Binding site:207-207

UniProt: Binding site:39-39

UniProt: Binding site:71-71

UniProt: Binding site:74-74

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 8DOR	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
ColabFold VK055_1987	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.

65 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 15 records from similar proteins

Structural ligands 15 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2HC PDB via homolog 164.2 Da · LogP 1.49 · TPSA 57.5 Open detail RCSB PDB

4HC PDB via homolog Detail RCSB PDB

4NB PDB via homolog Detail RCSB PDB

BEL PDB via homolog Detail RCSB PDB

BEZ 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
2HC RCSB PDB	1V5Z	P46072	164.2 Da LogP 1.49 TPSA 57.5	✓ Ro5	✓ Clean	`c1ccc(c(c1)\C=C\C(=O)O)O`
4HC RCSB PDB	1V5Y	P46072	162.1 Da LogP 1.50 TPSA 50.4	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=CC(=O)O2)O`
4NB RCSB PDB	5J8G	Q01234	167.1 Da LogP 1.29 TPSA 80.4	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)[N+](=O)[O-]`
BEL RCSB PDB	1OON	P38489	510.1 Da LogP 1.60 TPSA 152.8	1 viol.	✓ Clean	`c1c(c(cc(c1N(CCBr)CCBr)[N+](=O)[O-])[N+](=O)[O-…`
BEZ RCSB PDB	1KQB	Q01234	122.1 Da LogP 1.38 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)O`
CB1 RCSB PDB	1IDT	P38489	252.2 Da LogP 0.42 TPSA 132.4	✓ Ro5	✓ Clean	`c1c(c(cc(c1N2CC2)[N+](=O)[O-])[N+](=O)[O-])C(=O…`
DND RCSB PDB	5J8D	Q01234	665.4 Da LogP -2.42 TPSA 312.5	3 viol.	✓ Clean	`c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(…`
DTC RCSB PDB	1OOQ	P38489	336.3 Da LogP 2.21 TPSA 86.7	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=O)C(C(=O)O2)CC3C(=O)c4ccccc4OC3=O`
FLC RCSB PDB	3HZN	P15888	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
MLI RCSB PDB	3HZN	P15888	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
NFZ RCSB PDB	1YKI	P38489	198.1 Da LogP 0.19 TPSA 123.8	✓ Ro5	✓ Clean	`c1cc(oc1\C=N\NC(=O)N)[N+](=O)[O-]`
NIO RCSB PDB	6WT2	A0A0U1RIB4	123.1 Da LogP 0.78 TPSA 50.2	✓ Ro5	✓ Clean	`c1cc(cnc1)C(=O)O`
SIN RCSB PDB	3HZN	P15888	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)O`
SN2 RCSB PDB	1OO6	P38489	351.1 Da LogP 1.89 TPSA 132.6	✓ Ro5	✓ Clean	`c1c(c(cc(c1N(CCCl)CCCl)[N+](=O)[O-])[N+](=O)[O-…`
TLA RCSB PDB	3HZN	P15888	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
ZINC4475105 ZINC	1.000	252.2 Da LogP 0.42 TPSA 132.4	✓ Ro5	✓ Clean	`NC(=O)c1cc(N2CC2)c([N+](=O)[O-])cc1[N+](=O)[O-]`
ZINC168904 ZINC	0.875	243.2 Da LogP 2.96 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc([N+](=O)[O-])cc2)cc1`
ZINC281559 ZINC	0.875	271.2 Da LogP 2.52 TPSA 97.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)c2ccc([N+](=O)[O-])cc2)cc1`
ZINC3269660 ZINC	0.824	254.2 Da LogP 2.45 TPSA 71.4	✓ Ro5	Alert	`O=C(O)c1ccc(C(=O)C(=O)c2ccccc2)cc1`
ZINC238950253 ZINC	0.785	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950256 ZINC	0.785	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950259 ZINC	0.785	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950261 ZINC	0.785	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC1675827 ZINC	0.778	307.3 Da LogP 2.13 TPSA 114.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(S(=O)(=O)c2ccc([N+](=O)[O-])cc2)cc1`
ZINC19806403 ZINC	0.778	275.3 Da LogP 3.44 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc(Sc2ccc([N+](=O)[O-])cc2)cc1`
ZINC235952 ZINC	0.778	259.2 Da LogP 3.09 TPSA 89.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(Oc2ccc([N+](=O)[O-])cc2)cc1`
ZINC2504355 ZINC	0.778	226.2 Da LogP 2.62 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)c2ccccc2)cc1`
ZINC16892582 ZINC	0.769	214.2 Da LogP 0.35 TPSA 106.7	✓ Ro5	✓ Clean	`NC(=S)N/N=C\c1ccc([N+](=O)[O-])o1`
ZINC967470 ZINC	0.769	214.2 Da LogP 0.35 TPSA 106.7	✓ Ro5	✓ Clean	`NC(=S)N/N=C/c1ccc([N+](=O)[O-])o1`
ZINC1592410 ZINC	0.739	212.2 Da LogP 1.54 TPSA 59.9	✓ Ro5	Alert	`O=C(C(=O)c1cccnc1)c1cccnc1`
ZINC2173334 ZINC	0.739	300.2 Da LogP 2.57 TPSA 120.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc([N+](=O)[O-])cc1)c1ccc([N+](=O)[…`
ZINC4892440 ZINC	0.724	301.3 Da LogP 2.94 TPSA 121.6	✓ Ro5	✓ Clean	`O=C(Nc1ccc(C(=O)O)cc1)Nc1ccc([N+](=O)[O-])cc1`
ZINC1556486 ZINC	0.720	266.3 Da LogP 3.39 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1O)/C=C/c1ccccc1O`
ZINC1688116 ZINC	0.708	272.2 Da LogP 2.73 TPSA 103.3	✓ Ro5	✓ Clean	`O=C(c1ccc([N+](=O)[O-])cc1)c1ccc([N+](=O)[O-])c…`
ZINC1857777485 ZINC	0.704	224.3 Da LogP 3.29 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(C=Cc1ccccc1O)c1ccccc1`
ZINC3894725 ZINC	0.704	224.3 Da LogP 3.29 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1O)c1ccccc1`
ZINC4566597 ZINC	0.704	224.3 Da LogP 3.29 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(/C=C\c1ccccc1O)c1ccccc1`
ZINC123863 ZINC	0.700	286.2 Da LogP 2.55 TPSA 109.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc(NC(=O)c2ccc([N+](=O)[O-])cc2)cc1`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC15636539 ZINC	0.700	287.2 Da LogP 2.51 TPSA 106.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(OC(=O)c2ccc([N+](=O)[O-])cc2)cc1`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC3129761 ZINC	0.700	383.4 Da LogP 3.79 TPSA 114.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(S(=O)(=O)c2ccc(-c3ccc([N+](=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`
ZINC2555760 ZINC	0.692	255.2 Da LogP 2.66 TPSA 77.3	✓ Ro5	Alert	`O=C(C(=O)c1ccc([N+](=O)[O-])cc1)c1ccccc1`
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`
ZINC1672966 ZINC	0.688	210.2 Da LogP 2.75 TPSA 34.1	✓ Ro5	Alert	`O=C(C(=O)c1ccccc1)c1ccccc1`
ZINC34057267 ZINC	0.684	274.3 Da LogP 4.72 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(-c3ccccc3)cc2)cc1`
ZINC1556187 ZINC	0.679	316.2 Da LogP 2.43 TPSA 140.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)c2cc([N+](=O)[O-])cc([N+](=O)[…`
ZINC12360002 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.671	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`

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_1987

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 · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence