Protein target profile

VK055_4454

NADH-Ubiquinone/plastoquinone (complex I), various chains family protein

Genome: KpATCC43816 Gene: AIK82997.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GX92

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Length 602

Pocket druggability 0.971

Direct ligand evidence 0 60 total records

Functional annotation 0 EC 4 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 0.97, P2Rank 0.71). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.97. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.71. 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: Hit
Human identity (%): 27.027 Lower values reduce human off-target concern.
Human E-value: 2.35e-14
Gut microbiome similarity: 1.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 33.333 Higher values support similarity to known essential genes.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 93.73 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 0.971

Structure A0A0H3GX92

Pocket Pocket 15

P2Rank 0.707

Structure A0A0H3GX92

Pocket Pocket 1

ColabFold model

FPocket 0.797 · Pocket 9

P2Rank 0.625 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 55 / 4744 genomes with a hit

Prevalence 1.2%

Cross-references

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

Sequence

UniProt A0A0H3GX92

Sequence

Primary amino-acid sequence viewer.

MNQAVAWYAASAVLAFLFAMRKPLSGAIAGIGGAVASAMLVVAGGAALLMPERIHGGMLQFLHLMIRVGGVNALWLLAIGLSALPVSLFNISWHRHPQVKPNGPLVNLLLAAATCAVVVTNIGSLVVMAEIMALCAAFLTGCAASGKLWFALGRLGTLLMAWTCWLVWSTYGTLELAQINLQAVDMMQNPLLWLPGLVGFALLAGAIPLHGWAPQAHAGASAPAAALFSTVVMKVGLYGMLTVSLAGGVPPLWWGVMLLALGMITAFIGGLYALMEHNIQRLLAYHTLENIGIILLGLGAFVTGVATRNSTLMVLGFIGGMYHLINHSLFKTTLFLGAGAVWFRTGHRDIEKLGGIGKKMPLISLAMLVGLMAMAALPPLNGFAGEWVIYQSFFKMSTGDLFIGRLLGPLLAVGLAITGALAVMCMAKVYGVTFLGAPRTKEAENATCAPWLMTLSVVLAAVFCLVGGIAAPWLLPLVSGAFPVQAQVSSVVSQPMIALLLIACPLLPFLLMIFFKGDRLAARSRGAAWVCGYDHEQSMVITAHGFAMPVKEAFAPLLKLRHWLNPVRLVPGWQSASAPALLRGIALVELAVLVVIVISRGA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

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:0008137 Catalysis of the reaction: NADH + ubiquinone + 5 H+(in) = NAD+ + ubiquinol + 4 H+(out).
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: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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

55 records

Show feature table

Start	End	DB	Term	Name
368	394	PRINTS	PR01437	NADH-ubiquinone oxidoreductase subunit 4 signature
368	394	InterPro	IPR003918	NADH:ubiquinone oxidoreductase
218	242	PRINTS	PR01437	NADH-ubiquinone oxidoreductase subunit 4 signature
218	242	InterPro	IPR003918	NADH:ubiquinone oxidoreductase
391	409	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
495	515	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
253	275	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
455	477	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
192	214	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
305	323	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
451	475	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
4	14	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
282	304	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
516	579	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
3	600	PANTHER	PTHR42682	HYDROGENASE-4 COMPONENT F
224	246	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
4	21	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
213	223	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
324	343	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
89	107	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
61	88	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
252	275	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
172	190	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
29	49	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
580	599	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
155	177	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
282	304	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
344	362	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
140	150	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
401	423	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
410	430	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
476	494	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
144	399	Pfam	PF00361	Proton-conducting membrane transporter
144	399	InterPro	IPR001750	NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit
247	251	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
15	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
191	212	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
50	60	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
363	390	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
108	139	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
319	341	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
151	171	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
28	50	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
105	127	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
492	514	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
431	450	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
362	381	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
227	249	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
600	602	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
70	92	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
276	281	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
131	153	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
20	28	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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 #15

0.971

Likely same site as P2Rank 3 2.2 Å 13 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #7

0.692

Likely same site as P2Rank 1 1.2 Å 14 shared residues 93% of smaller site

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Surrounding area

Site 3 FPocket #30

0.679

Unusual size

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Surrounding area

Site 4 FPocket #29

0.246

Likely same site as P2Rank 4 5.5 Å 13 shared residues 81% of smaller site

Unusual size

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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

0.707

Likely same site as FPocket 7 1.2 Å 14 shared residues 93% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.569

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Surrounding area

Site 3 P2Rank #3

0.546

Likely same site as FPocket 15 2.2 Å 13 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.33

Likely same site as FPocket 29 5.5 Å 13 shared residues 81% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.248

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #9

0.797

Likely same site as P2Rank 1 0.9 Å 13 shared residues 93% of smaller site

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Surrounding area

Site 2 FPocket #6

0.738

Likely same site as P2Rank 4 3.6 Å 12 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #34

0.59

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Surrounding area

Site 4 FPocket #31

0.279

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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

0.625

Likely same site as FPocket 9 0.9 Å 13 shared residues 93% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.62

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Surrounding area

Site 3 P2Rank #3

0.589

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Surrounding area

Site 4 P2Rank #4

0.252

Likely same site as FPocket 6 3.6 Å 12 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.244

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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_A0A0H3GX92	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4454	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.

60 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

BCR PDB via homolog 536.9 Da · LogP 12.61 · TPSA 0.0 Open detail RCSB PDB

DGD PDB via homolog Detail RCSB PDB

FES PDB via homolog Detail RCSB PDB

LHG PDB via homolog Detail RCSB PDB

LMG 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
BCR RCSB PDB	6L7O	Q8DKY0	536.9 Da LogP 12.61 TPSA 0.0	2 viol.	✓ Clean	`CC1=C(C(CCC1)(C)C)\C=C\C(=C\C=C\C(=C\C=C\C=C(/C…`
DGD RCSB PDB	6KHI	Q8DKY0	949.3 Da LogP 7.61 TPSA 231.1	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[C@H]1[C@@H]([C…`
FES RCSB PDB	6KHI	Q8DKY0	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
LHG RCSB PDB	6KHI	Q8DKY0	723.0 Da LogP 9.89 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@…`
LMG RCSB PDB	6HUM	Q8DKY0	787.2 Da LogP 9.78 TPSA 152.0	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[C@H]1[C@@H]([C…`
LMT RCSB PDB	7D3U	A0A221C8X0	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…`
PL9 RCSB PDB	6KHJ	Q8DKY0	749.2 Da LogP 16.57 TPSA 34.1	2 viol.	Alert	`CC1=C(C(=O)C(=CC1=O)CC=C(C)CCC=C(C)CCC=C(C)CCC=…`
PQN RCSB PDB	6L7P	Q8DKY0	450.7 Da LogP 9.16 TPSA 34.1	1 viol.	Alert	`CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CCC[C@H](C)CC…`
PTY RCSB PDB	6Z16	B7GL84	734.1 Da LogP 11.67 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCCCC…`
SQD RCSB PDB	6KHI	Q8DKX9	795.1 Da LogP 8.12 TPSA 186.1	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](COC1[C@@H]([C@H]([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
ZINC102191119 ZINC	1.000	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
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…`
ZINC58649551 ZINC	1.000	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC102191158 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC14880760 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OC[C…`
ZINC53683910 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[…`
ZINC62592202 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC62592203 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC62592204 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`
ZINC96094841 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC102190506 ZINC	0.729	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	0.729	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC36178999 ZINC	0.711	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	0.711	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC44830468 ZINC	0.711	346.5 Da LogP 4.93 TPSA 60.7	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C=C/C(C)=C\CCC(O)(O)O)C(C)(C)…`
ZINC95908757 ZINC	0.711	346.5 Da LogP 4.93 TPSA 60.7	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C=C\C(C)=C/CCC(O)(O)O)C(C)(C)…`
ZINC27416437 ZINC	0.708	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.708	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC13543394 ZINC	0.694	455.4 Da LogP 2.15 TPSA 171.7	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](N)C(=O)…`
ZINC5820131 ZINC	0.689	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134 ZINC	0.689	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC13544781 ZINC	0.686	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…`
ZINC13544783 ZINC	0.686	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)…`
ZINC13543439 ZINC	0.667	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441 ZINC	0.667	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC17284934 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C(=O)O)C(C)(C)CCC1`
ZINC17284937 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C\C(=O)O)C(C)(C)CCC1`
ZINC22061499 ZINC	0.650	220.4 Da LogP 4.01 TPSA 20.2	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C/CO)C(C)(C)CCC1`
ZINC4430042 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C/C(=O)O)C(C)(C)CCC1`
ZINC65748979 ZINC	0.650	214.4 Da LogP 4.65 TPSA 0.0	✓ Ro5	✓ Clean	`C#C/C=C(C)/C=C/C1=C(C)CCCC1(C)C`
ZINC8613746 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C\C(=O)O)C(C)(C)CCC1`
ZINC36079847 ZINC	0.636	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCC`
ZINC8214428 ZINC	0.636	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCC`
ZINC263614238 ZINC	0.627	470.5 Da LogP 3.32 TPSA 142.8	✓ Ro5	✓ Clean	`CC[C@H](C)CCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(…`
ZINC38564715 ZINC	0.627	470.5 Da LogP 3.32 TPSA 142.8	✓ Ro5	✓ Clean	`CC[C@H](C)CCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(…`
ZINC102190945 ZINC	0.620	411.5 Da LogP 3.29 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCCN`
ZINC32840692 ZINC	0.620	425.5 Da LogP 3.68 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCCN`
ZINC32840693 ZINC	0.620	425.5 Da LogP 3.68 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCCN`
ZINC32840704 ZINC	0.620	453.6 Da LogP 4.46 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OCCN`
ZINC32840705 ZINC	0.620	453.6 Da LogP 4.46 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OCCN`
ZINC95635984 ZINC	0.620	397.4 Da LogP 2.90 TPSA 128.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OCCN`
ZINC4521879 ZINC	0.619	386.5 Da LogP 4.73 TPSA 78.9	✓ Ro5	✓ Clean	`CCCCCC(=O)OCC(COC(=O)CCCCC)OC(=O)CCCCC`
ZINC33822387 ZINC	0.615	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC33822389 ZINC	0.615	426.5 Da LogP 2.66 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCC[N+](C)(C)C)…`
ZINC5820130 ZINC	0.614	288.4 Da LogP 2.59 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCC`
ZINC5820133 ZINC	0.614	288.4 Da LogP 2.59 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO)OC(=O)CCCCC`
ZINC257373224 ZINC	0.609	411.4 Da LogP -4.06 TPSA 227.3	2 viol.	Alert	`[N-]=[N+]=NCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O…`
ZINC257373226 ZINC	0.609	411.4 Da LogP -4.06 TPSA 227.3	2 viol.	Alert	`[N-]=[N+]=NCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O…`
ZINC257373227 ZINC	0.609	411.4 Da LogP -4.06 TPSA 227.3	2 viol.	Alert	`[N-]=[N+]=NCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O…`

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.