Protein target profile

KP13_03365

putative biotin sulfoxide reductase

Genome: KpKP13 Gene: AHE45744.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GLB2

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Length 760

Pocket druggability 0.997

Direct ligand evidence 0 58 total records

Functional annotation 0 EC 6 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

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 1.00, P2Rank 0.99). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Strong predicted binding pocket FPocket selected-pocket score 1.00. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.99. Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

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: 0.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 96.56 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 0.997

Structure A0A0H3GLB2

Pocket Pocket 1

P2Rank 0.995

Structure A0A0H3GLB2

Pocket Pocket 1

ColabFold model

FPocket 0.998 · Pocket 1

P2Rank 0.988 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 13 / 4744 genomes with a hit

Prevalence 0.3%

Cross-references

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

Sequence

UniProt A0A0H3GLB2

Sequence

Primary amino-acid sequence viewer.

MHWGTWQVESREGEIVAVKPVPWDKNPSRIGQSLPDAVTSQTRIRRPAVRAGYLQHGPASREGRGKEPFVEVSWEVALDLLARELRSVKARCGNEAIYGGSYGWASAGRFHHAQSQLHRFLKGFGGYTASTNTYSSAAGERILPHILGPLSPLHRQHTHFSELARECQLFVAIGGLPLRNAQVNGGGANDHMLQYWLDKMQANGTRFINISPVRNDLSAVPEAEWLAIRPGTDTALLLALSYVLIAESLYDQAFVASHTVGFAPYRAYLLGEHDGVAKTPAWAAAITGLDAQRIADLAREMARHRTMVNISWSIQRARQGEQAYWATVALTALLGQIGTPGGGLGFGYACTNLAGAVRKAFSGPRLPAGENAVDSVIPVARLSDMLLHPGETYEFDGQQRRYPDIRLVYWAGGNAFHHHQDINRLCEAWRRPETVVVHEQYWTAQAKFSDIVLPATTSLEREDIGSGGHDGFMIAMSAQIPPVGEARDDYAIFCDLAGRLGFGEAFSEGRDAGQWLRHLYEESRPRAQEEGIALHSFDDFWQQGVLEYSAPERPQIFLADFRADPQRYPLSTPSGKIELFSATVAGFGYRECPGHPWWDEQEAARQRQEAARWPLHLLSSQPRARLHSQYDHGSVSRATKIQGREPLWMHPSDAQARDIREGSVVKVYNDRGAILAGVHLSEQILPGVVQMSTGAWYDPLDPKEERSLDKHGNPNVLTEDRGSSRLGQGCSAQSCWVEIAPWREELPPITAFDPPKFIEV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 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:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
GO:0030151 Binding to a molybdenum ion (Mo).
GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
589	752	Gene3D	G3DSA:2.40.40.20	-
610	759	SUPERFAMILY	SSF50692	ADC-like
610	759	InterPro	IPR009010	Aspartate decarboxylase-like domain superfamily
700	716	MobiDBLite	mobidb-lite	consensus disorder prediction
613	740	CDD	cd02793	MopB_CT_DMSOR-BSOR-TMAOR
613	740	InterPro	IPR041954	Trimethylamine-N-oxide reductase-like, molybdopterin-binding domain
2	741	PANTHER	PTHR43742	TRIMETHYLAMINE-N-OXIDE REDUCTASE
43	498	Pfam	PF00384	Molybdopterin oxidoreductase
43	498	InterPro	IPR006656	Molybdopterin oxidoreductase
700	724	MobiDBLite	mobidb-lite	consensus disorder prediction
2	38	Pfam	PF18364	Molybdopterin oxidoreductase N-terminal domain
2	38	InterPro	IPR041460	Molybdopterin oxidoreductase, N-terminal
615	735	Pfam	PF01568	Molydopterin dinucleotide binding domain
615	735	InterPro	IPR006657	Molybdopterin dinucleotide-binding domain
135	581	Gene3D	G3DSA:3.40.228.10	Dimethylsulfoxide Reductase, domain 2
2	616	SUPERFAMILY	SSF53706	Formate dehydrogenase/DMSO reductase, domains 1-3
37	548	Gene3D	G3DSA:3.90.55.10	Dimethylsulfoxide Reductase, domain 3
43	507	Gene3D	G3DSA:3.40.50.740	-

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

0.997

Unusual size

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Surrounding area

Site 2 FPocket #3

0.887

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Surrounding area

Site 3 FPocket #39

0.838

Likely same site as P2Rank 2 2.2 Å 18 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 4 FPocket #2

0.457

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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

0.995

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Surrounding area

Site 2 P2Rank #2

0.304

Likely same site as FPocket 39 2.2 Å 18 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.243

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Surrounding area

Site 4 P2Rank #4

0.174

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Surrounding area

Site 5 P2Rank #5

0.14

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #1

0.998

Likely same site as P2Rank 1 6.8 Å 40 shared residues 95% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #2

0.936

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Surrounding area

Site 3 FPocket #42

0.394

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Surrounding area

Site 4 FPocket #44

0.232

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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

0.988

Likely same site as FPocket 1 6.8 Å 40 shared residues 95% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.875

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Surrounding area

Site 3 P2Rank #3

0.458

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Surrounding area

Site 4 P2Rank #4

0.426

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Surrounding area

Site 5 P2Rank #5

0.339

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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_A0A0H3GLB2	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03365	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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 13 records from similar proteins

Structural ligands 13 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 45 similarity-based ZINC candidates

Best available ligand signal

2MD PDB via homolog 742.6 Da · LogP -2.53 · TPSA 346.6 Open detail RCSB PDB

2MO PDB via homolog Detail RCSB PDB

4MO PDB via homolog Detail RCSB PDB

6MO PDB via homolog Detail RCSB PDB

6WO 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
2MD RCSB PDB	1TMO	O87948	742.6 Da LogP -2.53 TPSA 346.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…`
2MO RCSB PDB	1E61	Q52675	127.9 Da LogP -0.24 TPSA 34.1	✓ Ro5	✓ Clean	`O=[Mo]=O`
4MO RCSB PDB	2DMR	Q52675	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo+4]`
6MO RCSB PDB	1DMR	Q52675	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo+6]`
6WO RCSB PDB	1E18	Q52675	199.8 Da LogP -0.12 TPSA 17.1	✓ Ro5	✓ Clean	`O=[W+4]`
BTT RCSB PDB	4V4E	P80563	142.1 Da LogP 0.51 TPSA 80.9	✓ Ro5	Alert	`c1c(c(cc(c1O)O)O)O`
MGD RCSB PDB	4V4C	P80563	740.6 Da LogP -2.06 TPSA 346.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…`
NO2 RCSB PDB	1FDI	P07658	46.0 Da LogP 0.25 TPSA 52.5	✓ Ro5	✓ Clean	`N(=O)[O-]`
O RCSB PDB	1DMR	Q52675	18.0 Da LogP -0.82 TPSA 31.5	✓ Ro5	✓ Clean	`O`
PGD RCSB PDB	1DMR	Q52675	738.6 Da LogP -2.97 TPSA 343.0	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…`
PYG RCSB PDB	4V4D	P80563	126.1 Da LogP 0.80 TPSA 60.7	✓ Ro5	Alert	`c1cc(c(c(c1)O)O)O`
SO2 RCSB PDB	2DMR	Q52675	64.1 Da LogP -0.67 TPSA 34.1	✓ Ro5	✓ Clean	`O=S=O`
W RCSB PDB	2E7Z	Q71EW5	183.8 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[W+6]`

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
ZINC12504289 ZINC	0.689	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC6091722 ZINC	0.667	218.2 Da LogP 2.18 TPSA 80.9	✓ Ro5	Alert	`Oc1cccc(-c2cccc(O)c2O)c1O`
ZINC104869865 ZINC	0.642	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC34541308 ZINC	0.642	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.642	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.642	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.642	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.642	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC38229869 ZINC	0.636	324.3 Da LogP 3.38 TPSA 121.4	1 viol.	Alert	`Oc1cc2c3cc(O)c(O)cc3c3cc(O)c(O)cc3c2cc1O`
ZINC59636950 ZINC	0.588	236.0 Da LogP 1.70 TPSA 40.5	✓ Ro5	Alert	`Oc1cccc(I)c1O`
ZINC12501413 ZINC	0.573	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	0.573	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	0.573	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	0.573	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)[…`
ZINC2159505 ZINC	0.573	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	0.573	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	0.573	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	0.573	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	0.573	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)[…`
ZINC13377064 ZINC	0.571	218.2 Da LogP 2.18 TPSA 80.9	✓ Ro5	✓ Clean	`Oc1cccc(O)c1-c1c(O)cccc1O`
ZINC254871 ZINC	0.538	267.9 Da LogP 2.62 TPSA 40.5	✓ Ro5	Alert	`Oc1cc(Br)c(Br)cc1O`
ZINC17375772 ZINC	0.535	459.3 Da LogP -1.46 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(S)c2ncn([C@@H]3O[C@@H](CO[P@](=O)(O)OP(=O…`
ZINC8618621 ZINC	0.535	459.3 Da LogP -1.46 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(S)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8618622 ZINC	0.535	459.3 Da LogP -1.46 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(S)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8618623 ZINC	0.535	459.3 Da LogP -1.46 TPSA 232.6	2 viol.	✓ Clean	`Nc1nc(S)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC106686432 ZINC	0.529	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	0.529	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	0.529	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	0.529	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	0.529	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	0.529	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	0.529	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	0.529	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…`
ZINC100058967 ZINC	0.517	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@H](CO[P@](=O)(O)OP(=O)…`
ZINC12504287 ZINC	0.517	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC12504288 ZINC	0.517	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC31308647 ZINC	0.517	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC71774763 ZINC	0.516	432.3 Da LogP -2.23 TPSA 198.3	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@](=O)(O)N3CCOCC3…`
ZINC12503703 ZINC	0.506	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC8215878 ZINC	0.506	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC1713871 ZINC	0.500	267.9 Da LogP 2.62 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)c(Br)cc1Br`
ZINC221342725 ZINC	0.500	350.3 Da LogP 2.91 TPSA 121.4	1 viol.	Alert	`Oc1cc2c(cc1O)C1c3cc(O)c(O)cc3C2c2cc(O)c(O)cc21`
ZINC32257174 ZINC	0.500	236.0 Da LogP 1.70 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cccc(O)c1I`
ZINC3843434 ZINC	0.500	280.3 Da LogP 3.12 TPSA 80.9	✓ Ro5	Alert	`Oc1cc2c(cc1O)Sc1cc(O)c(O)cc1S2`
ZINC4262226 ZINC	0.500	366.4 Da LogP 3.01 TPSA 121.4	1 viol.	Alert	`Oc1cc2c(cc1O)Cc1cc(O)c(O)cc1Cc1cc(O)c(O)cc1C2`

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.