Protein target profile

VK055_3718

nitrite reductase, large subunit

Genome: KpATCC43816 Gene: nirB AIK82273.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GYE4

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Length 847

Pocket druggability 0.967

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 72 total records

Functional annotation 0 EC 12 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

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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.82. Structure available AlphaFold DB model + ColabFold model 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 (%): 28.615 Lower values reduce human off-target concern.
Human E-value: 3.81e-23
Gut microbiome similarity: 2.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 34.847 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 90.24 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 0.967

Structure A0A0H3GYE4

Pocket Pocket 20

P2Rank 0.819

Structure A0A0H3GYE4

Pocket Pocket 1

ColabFold model

FPocket 0.59 · Pocket 1

P2Rank 0.836 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 129 / 4744 genomes with a hit

Prevalence 2.7%

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.

MSKVRIAIIGNGMVGHRFIEELLDKAPAGQFDITVFCEEPRIAYDRVHLSSYFSHHTAEELSLVREGFYEKHGVKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGAETQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVKVHTSKNTKEIVQQGTEARKTMHFADGSELQVDFIVFSTGIRPRDKLATQCGLAVAQRGGIMVNDSCQTSDPDIYAIGECASWNNRVYGLVAPGYKMAQVAVDHLLGSENSFTGADLSAKLKLLGVDVGGIGDAHGRTPGARSYVYLDESKEVYKRLIVSADNKTLLGAVLVGDTSDYGNLLQLVLNAIELPENPDSLILPAHAGSGKPSIGVDKLPDSAQICSCFDVSKGDLIAAINKGCHTVAALKAETKAGTGCGGCIPLVTQVLNAELAKQGIEVNNNLCEHFAYSRQELFHLIRVEGIKTFDELLEKHGQGYGCEVCKPTVGSLLASCWNEYILKPQHTPLQDSNDNFLANIQKDGTYSVIPRSAGGEITPEGLVAVGRIAREFNLYTKITGSQRIGLFGAQKDDLPEIWRQLIEAGFETGHAYAKALRMAKTCVGSTWCRYGVGDSVGFGVELENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATEKGWNLYVCGNGGMKPRHADLLAADLDRDTLIKYLDRFMMFYIRTADKLTRTAPWLDNMEGGIDYLRSVIIDDKLGLNDHLEEELARLRAAFACEWTETVNNPAAQTRFKHFINSDQRDPNVQVVPERDQHRPATPYERIPVTLVEEKA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

12 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.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0042128 The nitrogen metabolic process that encompasses the uptake of nitrate from the environment and reduction to ammonia, and results in the incorporation of nitrogen derived from nitrate into cellular substances.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0008942 Catalysis of the reaction: NH4+ + 3 NAD(P)+ + 2 H2O = nitrite + 3 NAD(P)H + 5 H+.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0046872 Binding to a metal ion.
GO:0098809 Catalysis of the reaction: nitrite + acceptor = product(s) of nitrate reduction + reduced acceptor.
GO:0015980 The chemical reactions and pathways by which a cell derives energy from organic compounds; results in the oxidation of the compounds from which energy is released.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

57 records

Show feature table

Start	End	DB	Term	Name
1	835	PIRSF	PIRSF037149	NirB
1	835	InterPro	IPR017121	Nitrite reductase [NAD(P)H], large subunit
638	761	FunFam	G3DSA:3.30.413.10:FF:000007	Nitrite reductase [NAD(P)H] large subunit
5	292	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
5	292	InterPro	IPR023753	FAD/NAD(P)-binding domain
321	387	Pfam	PF18267	Rubredoxin NAD+ reductase C-terminal domain
321	387	InterPro	IPR041575	NADH-rubredoxin oxidoreductase, C-terminal
633	767	Pfam	PF01077	Nitrite and sulphite reductase 4Fe-4S domain
633	767	InterPro	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
423	475	FunFam	G3DSA:1.10.10.1100:FF:000002	Nitrite reductase large subunit
633	808	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
633	808	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
419	470	CDD	cd19943	NirB_Fer2_BFD-like_1
261	283	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
102	120	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
6	25	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
147	165	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
234	250	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
6	801	NCBIfam	TIGR02374	nitrite reductase large subunit NirB
6	801	InterPro	IPR012744	Nitrite reductase [NAD(P)H] large subunit, NirB
2	189	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	189	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
110	246	Gene3D	G3DSA:3.50.50.60	-
110	246	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
8	283	Gene3D	G3DSA:3.50.50.60	-
8	283	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
679	695	ProSitePatterns	PS00365	Nitrite and sulfite reductases iron-sulfur/siroheme-binding site.
679	695	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
424	471	Pfam	PF04324	BFD-like [2Fe-2S] binding domain
424	471	InterPro	IPR007419	BFD-like [2Fe-2S]-binding domain
423	476	Gene3D	G3DSA:1.10.10.1100	-
423	476	InterPro	IPR041854	BFD-like [2Fe-2S]-binding domain superfamily
320	401	Gene3D	G3DSA:3.30.390.30	-
320	401	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
639	761	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
639	761	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
769	789	Coils	Coil	Coil
560	622	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
560	622	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
542	638	Gene3D	G3DSA:3.90.480.20	-
502	627	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
502	627	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
483	532	CDD	cd19944	NirB_Fer2_BFD-like_2
144	310	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
144	310	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
320	401	FunFam	G3DSA:3.30.390.30:FF:000006	Nitrite reductase large subunit
110	246	FunFam	G3DSA:3.50.50.60:FF:000033	Nitrite reductase [NAD(P)H], large subunit
276	283	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
235	249	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
147	172	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
105	114	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
2	833	PANTHER	PTHR43809	NITRITE REDUCTASE (NADH) LARGE SUBUNIT
545	638	FunFam	G3DSA:3.90.480.20:FF:000001	Nitrite reductase [NAD(P)H] large subunit
679	697	PRINTS	PR00397	Sirohaem Fe-binding site signature
679	697	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
636	654	PRINTS	PR00397	Sirohaem Fe-binding site signature
636	654	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site

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 #20

0.967

Likely same site as P2Rank 1 6.7 Å 25 shared residues 89% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #23

0.373

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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

0.819

Likely same site as FPocket 20 6.7 Å 25 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.816

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Surrounding area

Site 3 P2Rank #3

0.574

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Surrounding area

Site 4 P2Rank #4

0.15

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Surrounding area

Site 5 P2Rank #5

0.075

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Surrounding area

Residue sets

UniProt: Binding site:641-641

UniProt: Binding site:647-647

UniProt: Binding site:681-681

UniProt: Binding site:685-685

Binding pockets · FPocket

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

Site 1 FPocket #1

0.59

Unusual size

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Surrounding area

Site 2 FPocket #64

0.539

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Surrounding area

Site 3 FPocket #53

0.441

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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

0.836

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Surrounding area

Site 2 P2Rank #2

0.834

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Surrounding area

Site 3 P2Rank #3

0.493

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Surrounding area

Site 4 P2Rank #4

0.192

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Surrounding area

Site 5 P2Rank #5

0.078

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Surrounding area

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_A0A0H3GYE4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3718	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.

72 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 22 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 18 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

APR PDB via homolog 559.3 Da · LogP -3.28 · TPSA 291.5 Open detail RCSB PDB

AZI PDB via homolog Detail RCSB PDB

BU3 PDB via homolog Detail RCSB PDB

OXY PDB via homolog Detail RCSB PDB

CHEMBL1836603 ChEMBL via homolog · pchembl 6.72 (~190.5 nM) Detail ChEMBL

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
APR RCSB PDB	2GR2	Q52437	559.3 Da LogP -3.28 TPSA 291.5	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
AZI RCSB PDB	2BCP	Q5XC60	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BU3 RCSB PDB	6TUK	Q47QF8	90.1 Da LogP -0.25 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H]([C@@H](C)O)O`
OXY RCSB PDB	5ER0	Q03Q85	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`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
CHEMBL1836603 ChEMBL	P39051	6.72 ~190.5 nM	355.9 Da LogP 5.06 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(C)cc2)N1CCCN(C)C`
CHEMBL1836570 ChEMBL	P39051	6.57 ~269.2 nM	454.0 Da LogP 3.50 TPSA 42.4	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C(=O)CN(C…`
CHEMBL1836378 ChEMBL	P39051	6.50 ~316.2 nM	382.9 Da LogP 4.04 TPSA 22.1	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C)CC1`
CHEMBL1836574 ChEMBL	P39051	6.46 ~346.7 nM	459.4 Da LogP 5.23 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(I)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836567 ChEMBL	P39051	6.38 ~416.9 nM	463.0 Da LogP 4.85 TPSA 52.3	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C(=O)c2cc…`
CHEMBL1836559 ChEMBL	P39051	6.36 ~436.5 nM	393.9 Da LogP 4.82 TPSA 57.8	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCNC(=O)c1ccco1`
CHEMBL1836615 ChEMBL	P39051	6.23 ~588.8 nM	382.0 Da LogP 5.59 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(C)cc2)N1CCN1CCCCC1`
CHEMBL1836612 ChEMBL	P39051	6.14 ~724.4 nM	402.4 Da LogP 5.93 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(Cl)cc2)N1CCN1CCCCC1`
CHEMBL1836571 ChEMBL	P39051	6.11 ~776.2 nM	333.5 Da LogP 4.63 TPSA 18.8	✓ Ro5	✓ Clean	`CC1=Nc2ccccc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836572 ChEMBL	P39051	6.10 ~794.3 nM	412.4 Da LogP 5.39 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Br)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836577 ChEMBL	P39051	6.10 ~794.3 nM	415.6 Da LogP 6.36 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(-c3ccsc3)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836371 ChEMBL	P39051	6.09 ~812.8 nM	389.9 Da LogP 6.06 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1cccc(N(C)C)c1`
CHEMBL1836562 ChEMBL	P39051	6.09 ~812.8 nM	384.9 Da LogP 3.47 TPSA 47.9	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCNC(=O)CN(C)C`
CHEMBL1836606 ChEMBL	P39051	6.05 ~891.3 nM	385.9 Da LogP 5.42 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2cccc(F)c2)N1CCN1CCCCC1`
CHEMBL1836365 ChEMBL	P39051	6.03 ~933.3 nM	346.9 Da LogP 6.00 TPSA 15.6	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1ccccc1`
CHEMBL1836368 ChEMBL	P39051	6.03 ~933.3 nM	364.9 Da LogP 6.13 TPSA 15.6	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1ccccc1F`
CHEMBL1836380 ChEMBL	P39051	6.00 ~1.0 µM	341.9 Da LogP 4.75 TPSA 18.8	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCCN(C)C`
CHEMBL4859269 ChEMBL	P39051	6.00 ~1.0 µM	1157.2 Da LogP 7.07 TPSA 297.0	4 viol.	✓ Clean	`NCCCCc1cn(-c2ccc(-c3nc(-c4cccc(-c5csc(-c6ccc(-n…`

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
ZINC12360002 ZINC	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224 ZINC	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.738	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC105469665 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC5615251 ZINC	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615253 ZINC	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC5615258 ZINC	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615263 ZINC	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC31516918 ZINC	0.703	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC1582675 ZINC	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730 ZINC	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486734 ZINC	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC5486740 ZINC	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`

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_3718

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