Protein target profile

VK055_0231

nitrite reductase [NAD(P)H], small subunit

Genome: KpATCC43816 Gene: AIK78859.1 nirD 3D evidence: ColabFold model Metabolism 2 reactions

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Length 957

Pocket druggability 0.999

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 33 total records

Functional annotation 0 EC 8 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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.79. Structure available ColabFold model Ligand evidence via structure/bioactivity 7 structural and 0 bioactivity records.

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 (%): 26.689 Lower values reduce human off-target concern.
Human E-value: 5.38e-17
Gut microbiome similarity: 2.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 33.801 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 90.74 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

ColabFold / curated 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 0.999

Structure CB_VK055_0231

Pocket Pocket 1

P2Rank 0.789

Structure CB_VK055_0231

Pocket Pocket 1

ColabFold model

FPocket 0.999 · Pocket 1

P2Rank 0.789 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 132 / 4744 genomes with a hit

Prevalence 2.8%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Pathways

BioCyc RXN0-6377-AMMONIUM/NADP/WATER//NITRITE/NADPH/PROTON.42. BioCyc RXN0-6377-AMMONIUM/NAD/WATER//NITRITE/NADH/PROTON.40.

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.

MTKPVLVLVGHGMVGHHFLEQCVSRNLHQQYRIVVFGEERYPAYDRVHLSEYFAGRSAESLSLAAGDFFIEHGIELRLGEAVATIDRDARLVRDAEGHEIHWDKLVLATGSYPFVPPIPGNDLAGCFVYRTLDDLDRIAAHAAAAKSGVVIGGGLLGLEAANALKQLGLETQVVEFAPNLMAVQLDNGGAAMLREKIVALGVGVHTSKATTAIVREADGLRLNFADGGALRTDMVVFSAGIRPQDALARGCALQVGERGGIHIDGQCRTSDPDVLAIGECALWDNKIYGLVAPGYQMARIAAATLAGEDACFSGADMSTKLKLLGVDVASFGDAQGRTPGCQSYQWTDGPQQIYKKIVVSQDGKALLGGVLVGDASDYATLLQMMLNGMALPPRPESLILPALEGAAPKALGVAALPDSAPICSCHNVSKGDICQAVNNGARDMSAIKSCTRAATGCGGCSALVKQVMEYQLAEQGVEVKKDVCEHFPWSRQEIYHLVRVNHIHTFEQLISRYGQGHGCDVCKPLVASVLASCWNEYLLKPAHLPLQDTNDRYFANIQKDGSYSVVPRMAAGEVTPDGLIAIGQIAKRYQLYSKVTGGQRIDLFGARLEQLPAIWRELADAGFETGHAYGKSLRTVKSCVGSTWCRYGVQDSTGLAVRLEHRYKGLRAPHKIKMAVSGCTRECAEAQGKDIGVIATDKGWNLYVCGNGGMKPRHADLFASDLDEATLIRSIDRLLMFYIRTADRLQRTSTWMDNLEGGVAYLRQVVLEDSLGIGEELEQEMARIVDSYQCEWQTTLNDPQRLALFRSFVNSDQPDEAVQRRDLRGQPQPLLTETLPEGELPSRPWQAVCDLDAIPAQAGIGARLGERQIALFRFGERVYALDNREPGSAANVLSRGLLGDVGGEPVVISPLYKQRIRLRDGWPCDGSEQAVRAWPVKVENGKVWVGNQQLLARAEAS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

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: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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

63 records

Show feature table

Start	End	DB	Term	Name
259	281	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
6	25	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
232	248	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
147	165	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
102	120	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
629	793	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
629	793	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
3	944	PANTHER	PTHR43809	NITRITE REDUCTASE (NADH) LARGE SUBUNIT
149	308	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
149	308	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
6	190	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
6	190	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
636	759	FunFam	G3DSA:3.30.413.10:FF:000007	Nitrite reductase [NAD(P)H] large subunit
6	799	NCBIfam	TIGR02374	nitrite reductase large subunit NirB
6	799	InterPro	IPR012744	Nitrite reductase [NAD(P)H] large subunit, NirB
421	474	Gene3D	G3DSA:1.10.10.1100	-
421	474	InterPro	IPR041854	BFD-like [2Fe-2S]-binding domain superfamily
318	396	Gene3D	G3DSA:3.30.390.30	-
318	396	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
421	473	FunFam	G3DSA:1.10.10.1100:FF:000002	Nitrite reductase large subunit
845	945	Pfam	PF13806	Rieske-like [2Fe-2S] domain
845	945	InterPro	IPR012748	Rieske-like [2Fe-2S] domain, NirD-type
677	693	ProSitePatterns	PS00365	Nitrite and sulfite reductases iron-sulfur/siroheme-binding site.
677	693	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
845	946	NCBIfam	TIGR02378	nitrite reductase small subunit NirD
845	946	InterPro	IPR012748	Rieske-like [2Fe-2S] domain, NirD-type
500	639	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
500	639	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
845	946	CDD	cd03529	Rieske_NirD
631	803	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
631	803	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
147	172	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
233	247	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
105	114	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
274	281	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
481	530	CDD	cd19944	NirB_Fer2_BFD-like_2
841	949	Gene3D	G3DSA:2.102.10.10	-
841	949	InterPro	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily
558	620	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
558	620	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
842	947	ProSiteProfiles	PS51300	NADH-nitrite reductase subunit D family profile.
7	281	Gene3D	G3DSA:3.50.50.60	-
7	281	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
318	387	Pfam	PF18267	Rubredoxin NAD+ reductase C-terminal domain
318	387	InterPro	IPR041575	NADH-rubredoxin oxidoreductase, C-terminal
318	399	FunFam	G3DSA:3.30.390.30:FF:000006	Nitrite reductase large subunit
630	768	Pfam	PF01077	Nitrite and sulphite reductase 4Fe-4S domain
630	768	InterPro	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
422	469	Pfam	PF04324	BFD-like [2Fe-2S] binding domain
422	469	InterPro	IPR007419	BFD-like [2Fe-2S]-binding domain
110	244	FunFam	G3DSA:3.50.50.60:FF:000033	Nitrite reductase [NAD(P)H], large subunit
845	945	ProSiteProfiles	PS51296	Rieske [2Fe-2S] iron-sulfur domain profile.
845	945	InterPro	IPR017941	Rieske [2Fe-2S] iron-sulphur domain
634	652	PRINTS	PR00397	Sirohaem Fe-binding site signature
634	652	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
677	695	PRINTS	PR00397	Sirohaem Fe-binding site signature
677	695	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
844	947	SUPERFAMILY	SSF50022	ISP domain
844	947	InterPro	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily
110	244	Gene3D	G3DSA:3.50.50.60	-
110	244	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
6	288	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
6	288	InterPro	IPR023753	FAD/NAD(P)-binding domain

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

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

Site 1 FPocket #1

0.999

Likely same site as P2Rank 1 3.9 Å 26 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #51

0.436

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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

0.789

Likely same site as FPocket 1 3.9 Å 26 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.778

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Surrounding area

Site 3 P2Rank #3

0.621

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Surrounding area

Site 4 P2Rank #4

0.379

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Surrounding area

Site 5 P2Rank #5

0.168

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Surrounding area

All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 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
ColabFold VK055_0231	ColabFold	—	—	full sequence	—	Viewing

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.

33 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 26 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

CA6 PDB via homolog Detail RCSB PDB

CA8 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
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`
CA6 RCSB PDB	4EM3	Q2FIA5	841.6 Da LogP -1.77 TPSA 380.7	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H](…`
CA8 RCSB PDB	4EM4	Q2FIA5	903.7 Da LogP -0.34 TPSA 380.7	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H](…`
CAJ RCSB PDB	4EMW	Q2FIA5	835.6 Da LogP -0.86 TPSA 372.9	3 viol.	✓ Clean	`CCOC(=O)CCCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](…`
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).

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
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…`
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(=…`
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(=…`
ZINC12501123 ZINC	0.553	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC4228234 ZINC	0.553	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC79671662 ZINC	0.553	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC79671663 ZINC	0.553	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC12360002 ZINC	0.511	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	0.511	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	0.511	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586019 ZINC	0.511	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	0.511	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	0.511	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC3871401 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871402 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3871403 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871404 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC4096223 ZINC	0.506	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC12501218 ZINC	0.500	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC12503850 ZINC	0.500	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC13540909 ZINC	0.500	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC141161066 ZINC	0.500	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	0.500	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	0.500	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.