KpATCC43816 Protein target profile

dimethyl sulfoxide reductase, chain A

Accession: VK055_0920

Gene: AIK79543.1 dmsA 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GMZ1

Export view

Length 811

Pocket druggability (P2Rank · AlphaFold DB model) 0.966

Direct ligand evidence 0 63 total records

Functional annotation 0 EC 9 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.97, FPocket 0.91). 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 0.91. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. 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: 3.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 63.772 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 92.99 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.966

Structure A0A0H3GMZ1

Pocket Pocket 1

Druggability (FPocket) 0.909

Structure A0A0H3GMZ1

Pocket Pocket 2

ColabFold model

P2Rank 0.975 · Pocket 1

FPocket 0.954 · Pocket 2

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 152 / 4744 genomes with a hit

Prevalence 3.2%

Cross-references

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

Sequence

UniProt A0A0H3GMZ1

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSNQESPGGVSRRALLKSTALGSLALAAGGLTLPFTLRRAAAAVQQATGDTTRIVWGACSVNCGSRCALRLHVRDDEVVYVETDNTGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTLADRLKSVVAQYGNEAVYINYSSGIVGGNITRSSPSASPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYGSNDGNSTSDIENSKLVVMFGNNPAETRMSGGGITWYLEQARERSNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVLINEDLVDQPFLDKYCVGYDEKTLPAGAPANGHYKAYILGEGDDGIAKTPQWASRITGIPTDRIIKLAREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGNSGARESTYTITIERLPVLENPVKTAISCFTWTDAIARGPEMTASRDGVRGKEKLDVPIKFLWNYAGNTIINQHSDINKTHEILQEESKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIIPNDYAGNMGYLIFIQPATSAKFERKPIYWILSEVAKRLGDDVHQRFTEGRTQEQWLQYLYAKMVAKDPVLPAYEDLKRMGIYKRKDPNGHFVAYRDFRRDPEAHPLKTPSGKIEIYSSRLAEIAARWQLEKDEVISPLPVYASTFEGWDDPLRSQYPLQLFGFHYKARTHSSYGNVDVLQAACRQEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWHDANMTGDRIDHGACMNTLTTHRPSPLAKGNPQHTNLVDIEKV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Subcellular localization

Localization: CytoplasmicMembrane

Gene Ontology (GO)

GO:0030151 Binding to a molybdenum ion (Mo).
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: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:0009389 Catalysis of the reaction: dimethyl sulfide + a menaquinone + H2O = dimethyl sulfoxide + a menaquinol.
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:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
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: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.

36 records

Show feature table

Start	End	DB	Term	Name
665	811	Gene3D	G3DSA:2.40.40.20	-
19	37	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	42	Phobius	SIGNAL_PEPTIDE	Signal peptide region
10	811	NCBIfam	TIGR02166	anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family
10	811	InterPro	IPR011888	Anaerobic dimethyl sulphoxide reductase, subunit A, DmsA/YnfE
38	42	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
206	649	Gene3D	G3DSA:3.40.228.10	Dimethylsulfoxide Reductase, domain 2
1	18	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
680	811	SUPERFAMILY	SSF50692	ADC-like
680	811	InterPro	IPR009010	Aspartate decarboxylase-like domain superfamily
47	115	Gene3D	G3DSA:2.20.25.90	-
688	810	CDD	cd02794	MopB_CT_DmsA-EC
53	111	Pfam	PF04879	Molybdopterin oxidoreductase Fe4S4 domain
53	111	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
410	618	FunFam	G3DSA:3.40.50.740:FF:000015	Anaerobic dimethyl sulfoxide reductase subunit A
116	637	Gene3D	G3DSA:3.40.50.740	-
56	679	CDD	cd02770	MopB_DmsA-EC
665	811	FunFam	G3DSA:2.40.40.20:FF:000010	Anaerobic dimethyl sulfoxide reductase subunit A
690	803	Pfam	PF01568	Molydopterin dinucleotide binding domain
690	803	InterPro	IPR006657	Molybdopterin dinucleotide-binding domain
1	42	ProSiteProfiles	PS51318	Twin arginine translocation (Tat) signal profile.
1	42	InterPro	IPR006311	Twin-arginine translocation pathway, signal sequence
54	692	SUPERFAMILY	SSF53706	Formate dehydrogenase/DMSO reductase, domains 1-3
52	111	SMART	SM00926	Molybdop_Fe4S4_2
52	111	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
726	753	ProSitePatterns	PS00932	Prokaryotic molybdopterin oxidoreductases signature 3.
726	753	InterPro	IPR006655	Molybdopterin oxidoreductase, prokaryotic, conserved site
124	337	FunFam	G3DSA:3.40.50.12440:FF:000003	Anaerobic dimethyl sulfoxide reductase subunit A
10	811	PANTHER	PTHR43742	TRIMETHYLAMINE-N-OXIDE REDUCTASE
206	429	FunFam	G3DSA:3.40.228.10:FF:000004	Dimethyl sulfoxide reductase subunit A
52	113	ProSiteProfiles	PS51669	Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile.
52	113	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
53	123	FunFam	G3DSA:3.40.50.12440:FF:000002	Anaerobic dimethyl sulfoxide reductase, A subunit
43	811	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
114	569	Pfam	PF00384	Molybdopterin oxidoreductase
114	569	InterPro	IPR006656	Molybdopterin oxidoreductase

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.966

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.161

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.143

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.108

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.106

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #2

0.909

Show in viewer

Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.975

Likely same site as FPocket 2 4.8 Å 31 shared residues 67% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.228

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.141

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.137

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.13

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #2

0.954 Unusual size

Likely same site as P2Rank 1 4.8 Å 31 shared residues 67% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #1

0.701

Likely same site as P2Rank 1 6.7 Å 29 shared residues 97% of smaller site

Show in viewer

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_A0A0H3GMZ1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0920	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.

63 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 50 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]`
MGD RCSB PDB	6CZ8	Q7WTU0	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@@](=…`
MO RCSB PDB	6CZ8	Q7WTU0	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo]`
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`
PG5 RCSB PDB	6CZ8	Q7WTU0	178.2 Da LogP 0.31 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOC`
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@@](=…`
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
ZINC1692489 ZINC	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC4530388 ZINC	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172 ZINC	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC34764844 ZINC	0.733	206.3 Da LogP 1.09 TPSA 36.9	✓ Ro5	✓ Clean	`CCCOCCOCCOCCOC`
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)(…`
ZINC140264883 ZINC	0.688	223.3 Da LogP -0.43 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCON`
ZINC143705779 ZINC	0.688	443.5 Da LogP -0.34 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC33358855 ZINC	0.688	207.3 Da LogP -0.36 TPSA 62.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCN`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44583772 ZINC	0.688	356.5 Da LogP 0.66 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCS`
ZINC5024003 ZINC	0.688	251.3 Da LogP -0.34 TPSA 72.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCN`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC575432090 ZINC	0.688	355.4 Da LogP -0.38 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCON`
ZINC575432265 ZINC	0.688	399.5 Da LogP -0.36 TPSA 109.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCON`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC71254558 ZINC	0.688	444.6 Da LogP 0.70 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC71254563 ZINC	0.688	488.6 Da LogP 0.71 TPSA 92.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC80685077 ZINC	0.688	427.5 Da LogP -0.28 TPSA 109.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC83253927 ZINC	0.688	400.5 Da LogP 0.68 TPSA 73.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC83253930 ZINC	0.688	224.3 Da LogP 0.61 TPSA 36.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCS`
ZINC83253936 ZINC	0.688	383.5 Da LogP -0.29 TPSA 99.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC90556279 ZINC	0.688	295.4 Da LogP -0.33 TPSA 81.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCN`
ZINC90556280 ZINC	0.688	339.4 Da LogP -0.31 TPSA 90.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCN`
ZINC90556286 ZINC	0.688	312.4 Da LogP 0.65 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCS`
ZINC90556287 ZINC	0.688	268.4 Da LogP 0.63 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCS`
ZINC96503353 ZINC	0.688	471.6 Da LogP -0.26 TPSA 118.3	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCN`
ZINC104869865 ZINC	0.684	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	0.684	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	0.684	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	0.684	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	0.684	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	0.684	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)(…`
ZINC113456917 ZINC	0.647	220.3 Da LogP 1.48 TPSA 36.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCOC`
ZINC146934560 ZINC	0.647	397.5 Da LogP -0.03 TPSA 85.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCNCCOCCOCCOCCOC`
ZINC218810670 ZINC	0.647	308.4 Da LogP 1.52 TPSA 55.4	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCOCCOCCOC`
ZINC33506597 ZINC	0.647	309.4 Da LogP -0.06 TPSA 67.4	✓ Ro5	✓ Clean	`COCCOCCOCCNCCOCCOCCOC`
ZINC34303570 ZINC	0.647	264.4 Da LogP 1.50 TPSA 46.2	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCOCCOC`
ZINC3860567 ZINC	0.647	323.4 Da LogP 0.28 TPSA 58.6	✓ Ro5	✓ Clean	`COCCOCCN(CCOCCOC)CCOCCOC`
ZINC5701149 ZINC	0.647	221.3 Da LogP -0.10 TPSA 49.0	✓ Ro5	✓ Clean	`COCCOCCNCCOCCOC`
ZINC1083807936 ZINC	0.611	202.2 Da LogP 1.23 TPSA 27.7	✓ Ro5	✓ Clean	`COCCOCCOCC(F)(F)F`
ZINC115163232 ZINC	0.611	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC125689999 ZINC	0.611	221.3 Da LogP 0.03 TPSA 62.9	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCN`
ZINC2571901 ZINC	0.611	204.3 Da LogP 0.87 TPSA 36.9	✓ Ro5	✓ Clean	`C=CCOCCOCCOCCOC`
ZINC258837490 ZINC	0.611	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC4583025 ZINC	0.611	234.3 Da LogP 0.84 TPSA 46.2	✓ Ro5	✓ Clean	`C=COCCOCCOCCOCCOC`

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.