Protein target profile

KP13_00988

NADH-quinone oxidoreductase subunit G

Genome: KpKP13 Gene: nuoG AHE43482.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GT22

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Length 859

Pocket druggability 0.592

Direct ligand evidence 0 73 total records

Functional annotation 1 EC 11 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.59. This supports review but is not experimental validation. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 23 structural and 0 bioactivity records.

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: Hit
Human identity (%): 24.921 Lower values reduce human off-target concern.
Human E-value: 4.23e-46
Gut microbiome similarity: 2.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 56.068 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 97.1 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 0.592

Structure A0A0H3GT22

Pocket Pocket 11

P2Rank 0.278

Structure A0A0H3GT22

Pocket Pocket 1

ColabFold model

FPocket 0.738 · Pocket 4

P2Rank 0.534 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 131 / 4744 genomes with a hit

Prevalence 2.8%

Cross-references

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

Sequence

UniProt A0A0H3GT22

Sequence

Primary amino-acid sequence viewer.

MKQYQNAEDTRGRLVMSCMTPASDGTFISIDDSEAKQFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSFRRYRFTKRTHRNQDLGPFISHEMNRCIACYRCVRYYKDYADGTDLGVYGAHDNVYFGRPEDGTLESEFSGNLVEVCPTGVFTDKTHSERYNRKWDMQFAPSICQQCSIGCNISPGERYGELRRIENRYNGTVNRYFLCDRGRFGYGYVNLKDRPRQPVQRRGDDLITLNAEQAMQGAADILRQSKKVIGIGSPRASIESNFALRELVGADNFYTGIAKGEQARLQMMLKVLREGGIHTPSLRDIESYDAVLVLGEDITQTGARVALAVRQAVKGKAREMAAAQKVADWQIAAILNIGQRAKHPLFVTNVDDTRLDDIAAWTYRAPVEDQARLGFAIAHALDDSAPAVDGLSQDLQGKVDVIVQALAGAKKPLIISGTNAGSMEIIQAAANVAKALKGRGADVGVTMVARAVNSVGLGMIGGGSLEEALDELESGAADAVIVLENDLHRHASAARVDAALAKAPLVMVVDHQRTAIMDKAHLVLSAASFAESDGTVVNNEGRAQRFFQVYDPAYYDAKTVMLESWRWLHSLHSTVNNRQVDWTQLDHVIDAAIAALPQLAGIKDAAPDATFRIRGQKLAREPHRYSGRTAMRANISVHEPRQPQDKDTMFAFSMEGNNQPSAPRSQIPFAWAPGWNSPQAWNKFQDEVGGKLRHGDPGVRLFEASASGLEYFTAVPASFQAEEGKWRIAPYYHLFGSDELSQRAPVFQSRMPEPYIKLNPADAAKLGVNPGAMLSFSVEGQTLRLPLVISEGLTAGQVGLPMGMPGIAPVLTGSRIDSLQEAKA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

7.1.1.-

Gene Ontology (GO)

GO:0008137 Catalysis of the reaction: NADH + ubiquinone + 5 H+(in) = NAD+ + ubiquinol + 4 H+(out).
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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0042773 The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0016651 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
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:0003954 Catalysis of the reaction: NADH + H+ + acceptor = NAD+ + reduced acceptor.
GO:0048038 Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

35 records

Show feature table

Start	End	DB	Term	Name
101	111	ProSitePatterns	PS00643	Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3.
101	111	InterPro	IPR000283	NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site
6	78	Gene3D	G3DSA:3.10.20.740	-
172	226	FunFam	G3DSA:2.20.25.90:FF:000003	NADH-quinone oxidoreductase
459	642	FunFam	G3DSA:3.40.50.740:FF:000006	NADH-quinone oxidoreductase
54	66	ProSitePatterns	PS00642	Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2.
54	66	InterPro	IPR000283	NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site
31	849	PANTHER	PTHR43105	RESPIRATORY NITRATE REDUCTASE
761	844	CDD	cd02788	MopB_CT_NDH-1_NuoG2-N7
762	855	FunFam	G3DSA:2.40.40.20:FF:000014	NADH-quinone oxidoreductase
170	639	SUPERFAMILY	SSF53706	Formate dehydrogenase/DMSO reductase, domains 1-3
448	641	Gene3D	G3DSA:3.40.50.740	-
39	75	Pfam	PF10588	NADH-ubiquinone oxidoreductase-G iron-sulfur binding region
39	75	InterPro	IPR019574	NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding
176	648	CDD	cd02771	MopB_NDH-1_NuoG2-N7
172	228	ProSiteProfiles	PS51669	Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile.
172	228	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
505	589	Pfam	PF00384	Molybdopterin oxidoreductase
505	589	InterPro	IPR006656	Molybdopterin oxidoreductase
39	79	SMART	SM00929	NADH_G_4Fe_4S_3_2
39	79	InterPro	IPR019574	NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding
765	853	SUPERFAMILY	SSF50692	ADC-like
765	853	InterPro	IPR009010	Aspartate decarboxylase-like domain superfamily
32	164	SUPERFAMILY	SSF54862	4Fe-4S ferredoxins
34	73	ProSiteProfiles	PS51839	His(Cys)3-ligated-type [4Fe-4S] domain profile.
34	73	InterPro	IPR019574	NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding
172	226	SMART	SM00926	Molybdop_Fe4S4_2
172	226	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
761	858	Gene3D	G3DSA:2.40.40.20	-
172	225	Pfam	PF04879	Molybdopterin oxidoreductase Fe4S4 domain
172	225	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
163	274	Gene3D	G3DSA:3.30.200.210	-
11	606	NCBIfam	TIGR01973	NADH-quinone oxidoreductase subunit NuoG
11	606	InterPro	IPR010228	NADH:ubiquinone oxidoreductase, subunit G
163	275	FunFam	G3DSA:3.30.200.210:FF:000004	NADH-quinone 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.

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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 #11

0.592

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Surrounding area

Site 2 FPocket #4

0.513

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Surrounding area

Site 3 FPocket #49

0.496

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Surrounding area

Site 4 FPocket #15

0.329

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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

0.278

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Surrounding area

Site 2 P2Rank #2

0.274

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Surrounding area

Site 3 P2Rank #3

0.231

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Surrounding area

Site 4 P2Rank #4

0.222

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Surrounding area

Site 5 P2Rank #5

0.156

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #4

0.738

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Surrounding area

Site 2 FPocket #10

0.594

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Surrounding area

Site 3 FPocket #13

0.307

Likely same site as P2Rank 4 1.5 Å 12 shared residues 100% of smaller site

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Surrounding area

Site 4 FPocket #1

0.298

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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

0.534

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Surrounding area

Site 2 P2Rank #2

0.36

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Surrounding area

Site 3 P2Rank #3

0.309

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Surrounding area

Site 4 P2Rank #4

0.212

Likely same site as FPocket 13 1.5 Å 12 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.21

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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_A0A0H3GT22	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00988	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.

73 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 23 records from similar proteins

Structural ligands 23 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3PE PDB via homolog 748.1 Da · LogP 12.06 · TPSA 134.4 Open detail RCSB PDB

8Q1 PDB via homolog Detail RCSB PDB

CDL PDB via homolog Detail RCSB PDB

CPL PDB via homolog Detail RCSB PDB

DCQ 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
3PE RCSB PDB	6RFQ	F2Z6F1	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
8Q1 RCSB PDB	5XTB	P28331	540.7 Da LogP 3.29 TPSA 162.3	1 viol.	✓ Clean	`CCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)…`
CDL RCSB PDB	6GCS	Q9UUU3	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
CPL RCSB PDB	6RFQ	F2Z6F1	758.1 Da LogP 10.94 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])OC…`
DCQ RCSB PDB	6I0D	Q56223	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C(=O)C(=C(C1=O)OC)OC)C`
EHZ RCSB PDB	6YJ4	F2Z6F1	584.7 Da LogP 3.04 TPSA 182.5	2 viol.	✓ Clean	`CCCCCCCCCCC[C@@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H]…`
FES RCSB PDB	2FUG	Q56223	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HQH RCSB PDB	6Q8O	Q56223	415.6 Da LogP 5.05 TPSA 71.6	1 viol.	✓ Clean	`C/C=C(\C)/[C@@H]([C@H](C)/C=C(\C)/C=C/C/C(=C/CC…`
HQK RCSB PDB	6Q8X	Q56223	364.9 Da LogP 5.24 TPSA 34.9	1 viol.	✓ Clean	`CC(C)(C)c1ccc(cc1)CSC2=C(C(=O)N(N=C2)C(C)(C)C)Cl`
HQW RCSB PDB	6Q8W	Q56223	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`CC1=C(OC(=C(C1=O)C)OC)[C@H]2C/C(=C/C(=C/c3ccc(c…`
LMN RCSB PDB	6RFQ	F2Z6F1	1005.2 Da LogP -1.68 TPSA 357.1	3 viol.	✓ Clean	`CCCCCCCCCCC(CCCCCCCCCC)(CO[C@@H]1[C@@H]([C@@H](…`
LMT RCSB PDB	6YJ4	F2Z6F1	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1…`
PC1 RCSB PDB	7DGQ	P15690	790.2 Da LogP 12.17 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])…`
PEE RCSB PDB	5XTH	P28331	744.0 Da LogP 11.61 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN…`
PLC RCSB PDB	6RFQ	F2Z6F1	622.8 Da LogP 8.12 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)…`
PLX RCSB PDB	5XTD	P28331	767.1 Da LogP 11.61 TPSA 114.7	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCC[C@@H](O)O[C@H](CO[C@@H](CCCCC…`
PSC RCSB PDB	6Y79	F2Z6F1	759.1 Da LogP 11.58 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N…`
SMA RCSB PDB	2YBB	Q56223	514.7 Da LogP 6.14 TPSA 87.4	2 viol.	✓ Clean	`C/C=C(\C)/C=C/C=C[C@@H]([C@@H](C)[C@H]([C@@H](C…`
T7X RCSB PDB	6RFR	F2Z6F1	887.1 Da LogP 9.17 TPSA 209.5	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OC1[C@@…`
UQ1 RCSB PDB	2YBB	Q56223	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C`
UQ2 RCSB PDB	7DGQ	P15690	318.4 Da LogP 4.04 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CCC=C(C)C`
UQ9 RCSB PDB	6RFR	F2Z6F1	795.2 Da LogP 16.13 TPSA 52.6	2 viol.	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CC\C=C(/C)…`
ZMP RCSB PDB	6RFQ	F2Z6F1	568.7 Da LogP 4.07 TPSA 162.3	1 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](C(C)(C…`

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
ZINC100053689 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC100053691 ZINC	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC13544781 ZINC	1.000	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC1501015302 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC1559692 ZINC	1.000	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`COC1=C(OC)C(=O)C(CC=C(C)C)=C(C)C1=O`
ZINC2039285652 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285653 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285654 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285655 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2053493146 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493147 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493148 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493149 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2105913 ZINC	1.000	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`COc1oc([C@@H]2C/C(=C/C(C)=C/c3ccc([N+](=O)[O-])…`
ZINC238809244 ZINC	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC238809245 ZINC	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC252695223 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695224 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695225 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695226 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC2575028 ZINC	1.000	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C)C(=O)C(OC)=C(OC)C1=O`
ZINC4025640 ZINC	1.000	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`COc1oc([C@H]2C/C(=C/C(C)=C/c3ccc([N+](=O)[O-])c…`
ZINC58649715 ZINC	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC59978443 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](…`
ZINC66157001 ZINC	1.000	468.5 Da LogP -1.62 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC70669940 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669941 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669942 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669943 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC77311968 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H]…`
ZINC83433913 ZINC	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](CO…`
ZINC85482724 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC86002923 ZINC	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)…`
ZINC100050848 ZINC	0.811	376.5 Da LogP 2.50 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](…`
ZINC105807070 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H…`
ZINC118906375 ZINC	0.811	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H]1O`
ZINC118911494 ZINC	0.811	278.3 Da LogP -0.23 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H…`
ZINC118911909 ZINC	0.811	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@…`
ZINC141152247 ZINC	0.811	264.3 Da LogP -0.62 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@H]…`
ZINC141262250 ZINC	0.811	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@…`
ZINC2046837 ZINC	0.811	306.4 Da LogP 0.55 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCO[C@H]1O[C@@H](CO)[C@H](O)[C@@H](O)[C@…`
ZINC248251557 ZINC	0.811	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@@H](CO)[C@H](O)[C@@H](O)[C…`
ZINC40165555 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H…`
ZINC48016017 ZINC	0.811	278.3 Da LogP -0.23 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]…`
ZINC53683291 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]…`
ZINC58563863 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]…`
ZINC71788562 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC71788563 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C@…`
ZINC85590873 ZINC	0.811	320.4 Da LogP 0.94 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](O)[…`
ZINC94437834 ZINC	0.811	292.4 Da LogP 0.16 TPSA 99.4	✓ Ro5	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O`

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.