KpATCC43816 Protein target profile

4-amino-4-deoxy-L-arabinose (L-Ara4N) transferase

Accession: VK055_3627

Gene: arnT AIK82182.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GZQ8

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Length 551

Pocket druggability (P2Rank · AlphaFold DB model) 0.933

Direct ligand evidence 0 55 total records

Functional annotation 1 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

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.93. Structure available AlphaFold DB model + ColabFold model 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: 1.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 62.795 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 92.78 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) 0.933

Structure A0A0H3GZQ8

Pocket Pocket 1

Druggability (FPocket) 0.915

Structure A0A0H3GZQ8

Pocket Pocket 1

ColabFold model

P2Rank 0.904 · Pocket 1

FPocket 0.925 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 73 / 4744 genomes with a hit

Prevalence 1.5%

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.

MKSIRYGVSLIALFALYYLLPLNFRLLWQPDETRYAEISREMLATGDWVVPHFLGLRYFEKPIAGYWINSIGQWLFGHNNFGVRFGSVFAITMTALLVAWLAWRIFRDKRVAILSPIIFLTAMLVYAIGTYAVLDPMITLWLALAMCSFWGAAQAHSRSGKILGYVLLGVACGMGVMTKGFLALAVPVVGVLPWVIARKRWREVLTYGWLAVIVCTLVVLPWGLAIAQREPDFWRYFFWVEHIQRFAEKDAQHKAPFWYYIPFLIAGSLPWLALLPGALKRGWLERDEARGALYLLGWVAMPFLFFSIAKGKLPTYILPCFAPLSILMARYALEAAKTGAKALRINGMINLGVGLLGLIAVLVVSPWGFMHKPVWTKIELYKCLLAAIAFAVWALMGWLAMKDSGRRWSLAALCPLGLALLVGFAIPDRVIDSKQPQFLVDIVSESLQPSRYVLTNNVGIAGGLAWELKRSDIIMFDKQGELKYGLDWPDAQGSFVSQAGFADWLAAHRQQGPVSLVLLMDKGESMLDLPLPKPDNAYELGRVVFLQYLPQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

2.4.2.43

Gene Ontology (GO)

GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0000030 Catalysis of the transfer of a mannosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
GO:0006493 A glycoprotein biosynthetic process starting with the covalent linkage of carbohydrate or carbohydrate derivative unit via a glycosidic bond to the oxygen atom of a serine, threonine, hydroxylysine, hydroxyproline or tyrosine side chain in a protein, which can be further elongated with the sequential addition of sugar units resulting in the formation of a protein O-linked glycan.
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:0103015 Catalysis of the reaction: (Kdo)2-lipid A + 2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate = (beta-L-Ara4N)2-(KDO)2-lipid A + 2 ditrans,polycis-undecaprenyl phosphate.
GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.
GO:0009103 The chemical reactions and pathways resulting in the formation of lipopolysaccharides, any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria.
GO:0010041 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an iron(III) ion stimulus.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

41 records

Show feature table

Start	End	DB	Term	Name
112	134	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
132	137	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
334	344	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
257	279	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
112	131	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
310	314	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
207	227	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
10	542	PANTHER	PTHR33908	MANNOSYLTRANSFERASE YKCB-RELATED
1	551	Hamap	MF_01165	Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase [arnT].
1	551	InterPro	IPR022839	Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
384	401	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
408	426	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
315	333	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
280	290	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
291	309	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
175	197	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
157	161	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
7	29	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
313	335	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
162	195	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
402	407	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
257	279	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
384	401	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
292	309	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
138	156	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
204	226	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
107	111	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
81	103	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	5	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
347	369	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
6	24	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
365	383	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
4	237	Pfam	PF02366	Dolichyl-phosphate-mannose-protein mannosyltransferase
4	237	InterPro	IPR003342	Glycosyl transferase family 39/83
345	364	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
228	256	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
427	551	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
408	427	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
85	106	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
25	84	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
196	206	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.

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 · P2Rank

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

Pocket 1 P2Rank #1

0.933

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Surrounding area

Pocket 2 P2Rank #2

0.753

Likely same site as FPocket 4 1.8 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.289

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Surrounding area

Pocket 4 P2Rank #4

0.177

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Surrounding area

Pocket 5 P2Rank #5

0.128

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.915 Unusual size

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Surrounding area

Pocket 2 FPocket #4

0.854

Likely same site as P2Rank 2 1.8 Å 15 shared residues 94% of smaller site

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.904

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Surrounding area

Pocket 2 P2Rank #2

0.717

Likely same site as FPocket 2 1.4 Å 14 shared residues 88% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.3

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Surrounding area

Pocket 4 P2Rank #4

0.218

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Surrounding area

Pocket 5 P2Rank #5

0.18

Likely same site as FPocket 32 1.6 Å 10 shared residues 100% of smaller site

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #2

0.925

Likely same site as P2Rank 2 1.4 Å 14 shared residues 88% of smaller site

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Surrounding area

Pocket 2 FPocket #15

0.4

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Surrounding area

Pocket 3 FPocket #32

0.203

Likely same site as P2Rank 5 1.6 Å 10 shared residues 100% of smaller site

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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_A0A0H3GZQ8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3627	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.

55 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5TR PDB via homolog 847.3 Da · LogP 18.33 · TPSA 66.8 Open detail RCSB PDB

DSL PDB via homolog Detail RCSB PDB

MPG PDB via homolog Detail RCSB PDB

PC PDB via homolog Detail RCSB PDB

CHEMBL255766 ChEMBL via homolog Detail ChEMBL

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
5TR RCSB PDB	5F15	Q1LDT6	847.3 Da LogP 18.33 TPSA 66.8	2 viol.	✓ Clean	`CC(=CCC/C(=C/CC/C(=C/CC/C(=C/CC/C(=C\CC/C(=C/CC…`
DSL RCSB PDB	5EZM	Q1LDT6	779.2 Da LogP 16.60 TPSA 66.8	2 viol.	✓ Clean	`CC(=CCC/C(=C/CC/C(=C\CC/C(=C\CC/C(=C\CC/C(=C\CC…`
MPG RCSB PDB	5EZM	Q1LDT6	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCCOC(=O)[C@@H](CO)O`
PC RCSB PDB	5EZM	Q1LDT6	184.2 Da LogP -0.20 TPSA 66.8	✓ Ro5	✓ Clean	`C[N+](C)(C)CCOP(=O)(O)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL255766 ChEMBL	O52327	—	301.3 Da LogP 0.45 TPSA 136.9	✓ Ro5	Alert	`CC(=O)OC1OC[C@H](N=[N+]=[N-])[C@H](OC(C)=O)[C@H…`

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
ZINC2556391 ZINC	1.000	302.4 Da LogP 4.51 TPSA 66.8	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CC/C(C)=C/COP(=O)(O)O`
ZINC1532829 ZINC	0.964	234.2 Da LogP 2.79 TPSA 66.8	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/COP(=O)(O)O`
ZINC12494625 ZINC	0.765	382.3 Da LogP 4.63 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CC/C(C)=C/CO[P@@](=O)(O)OP(=O)…`
ZINC2356589248 ZINC	0.765	382.3 Da LogP 4.63 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)=CCCC(C)=CCCC(C)=CCO[P@](=O)(O)OP(=O)(O)O`
ZINC8215849 ZINC	0.735	314.2 Da LogP 2.91 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CO[P@@](=O)(O)OP(=O)(O)O`
ZINC8218174 ZINC	0.722	462.3 Da LogP 4.75 TPSA 159.8	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CC/C(C)=C/CO[P@@](=O)(O)O[P@@]…`
ZINC71404870 ZINC	0.719	230.3 Da LogP 4.23 TPSA 26.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/COP(C)(C)=O`
ZINC34661063 ZINC	0.694	394.2 Da LogP 3.02 TPSA 159.8	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CO[P@@](=O)(O)O[P@@](=O)(O)OP(…`
ZINC59725075 ZINC	0.629	226.4 Da LogP 4.25 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCOC(C)=O`
ZINC59725096 ZINC	0.629	226.4 Da LogP 4.25 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCOC(C)=O`
ZINC103619636 ZINC	0.611	340.3 Da LogP 1.54 TPSA 176.4	✓ Ro5	Alert	`CC(=O)O[C@H]1[C@H](N=[N+]=[N-])C[C@H](N=[N+]=[N…`
ZINC102279436 ZINC	0.600	358.5 Da LogP 4.54 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)C[C@H](O)C(=O)OCCCCCCCC`
ZINC102279441 ZINC	0.600	358.5 Da LogP 4.54 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)C[C@@H](O)C(=O)OCCCCCCCC`
ZINC1719908 ZINC	0.588	264.4 Da LogP 4.97 TPSA 26.3	✓ Ro5	✓ Clean	`CC(=O)OC/C=C(\C)CC/C=C(\C)CCC=C(C)C`
ZINC1857777740 ZINC	0.588	264.4 Da LogP 4.97 TPSA 26.3	✓ Ro5	✓ Clean	`CC(=O)OCC=C(C)CCC=C(C)CCC=C(C)C`
ZINC4480023 ZINC	0.588	264.4 Da LogP 4.97 TPSA 26.3	✓ Ro5	✓ Clean	`CC(=O)OC/C=C(/C)CC/C=C(/C)CCC=C(C)C`
ZINC5829138 ZINC	0.588	264.4 Da LogP 4.97 TPSA 26.3	✓ Ro5	✓ Clean	`CC(=O)OC/C=C(/C)CC/C=C(\C)CCC=C(C)C`
ZINC5829142 ZINC	0.588	264.4 Da LogP 4.97 TPSA 26.3	✓ Ro5	✓ Clean	`CC(=O)OC/C=C(\C)CC/C=C(/C)CCC=C(C)C`
ZINC1850172 ZINC	0.583	240.4 Da LogP 4.64 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCOC(C)=O`
ZINC2018958 ZINC	0.583	226.4 Da LogP 4.25 TPSA 26.3	✓ Ro5	✓ Clean	`CCCC/C=C/CCCCCCOC(C)=O`
ZINC43068418 ZINC	0.583	240.4 Da LogP 4.64 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCOC(C)=O`
ZINC4543853 ZINC	0.583	226.4 Da LogP 4.25 TPSA 26.3	✓ Ro5	✓ Clean	`CCCC/C=C\CCCCCCOC(C)=O`
ZINC100503505 ZINC	0.581	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OCCC[C@H](O)CO`
ZINC100503506 ZINC	0.581	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OCCC[C@@H](O)CO`
ZINC17000749 ZINC	0.571	265.4 Da LogP 4.50 TPSA 52.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C\CC/C(C)=C\COC(N)=O`
ZINC17000752 ZINC	0.571	265.4 Da LogP 4.50 TPSA 52.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CC/C(C)=C\COC(N)=O`
ZINC17000755 ZINC	0.571	265.4 Da LogP 4.50 TPSA 52.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C\CC/C(C)=C/COC(N)=O`
ZINC17000758 ZINC	0.571	265.4 Da LogP 4.50 TPSA 52.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CC/C(C)=C/COC(N)=O`
ZINC5291871 ZINC	0.561	301.3 Da LogP 0.45 TPSA 136.9	✓ Ro5	Alert	`CC(=O)O[C@H]1[C@H](OC(C)=O)CO[C@@H](N=[N+]=[N-]…`
ZINC101342141 ZINC	0.559	374.5 Da LogP 3.52 TPSA 93.1	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)[C@@H](O)[C@@H](O)C(=O)OCCCCCCCC`
ZINC101342142 ZINC	0.559	374.5 Da LogP 3.52 TPSA 93.1	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)[C@@H](O)[C@H](O)C(=O)OCCCCCCCC`
ZINC101342143 ZINC	0.559	374.5 Da LogP 3.52 TPSA 93.1	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)[C@H](O)[C@@H](O)C(=O)OCCCCCCCC`
ZINC1319000 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1OC[C@@H](OC(C)=O)[C@H](OC(C)=O)[C…`
ZINC14584247 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CO[C@H](OC(C)=O)[C@@H](OC(C)=O)[C@…`
ZINC2003180 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CO[C@H](OC(C)=O)[C@H](OC(C)=O)[C@H…`
ZINC212206827 ZINC	0.556	273.4 Da LogP 2.77 TPSA 72.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOC(=O)[C@@H](N)CO`
ZINC25628116 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1[C@H](OC(C)=O)CO[C@H](OC(C)=O)[C@@…`
ZINC39336225 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1[C@H](OC(C)=O)[C@@H](OC(C)=O)OC[C…`
ZINC4557393 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1CO[C@H](OC(C)=O)[C@H](OC(C)=O)[C@…`
ZINC4557394 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CO[C@H](OC(C)=O)[C@H](OC(C)=O)[C@@…`
ZINC4557395 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1OC[C@@H](OC(C)=O)[C@@H](OC(C)=O)[…`
ZINC4557396 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CO[C@@H](OC(C)=O)[C@H](OC(C)=O)[C@…`
ZINC5438146 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1OC[C@@H](OC(C)=O)[C@@H](OC(C)=O)[…`
ZINC5495606 ZINC	0.556	318.3 Da LogP -0.30 TPSA 114.4	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1[C@@H](OC(C)=O)OC[C@@H](OC(C)=O)[…`
ZINC77300481 ZINC	0.553	260.3 Da LogP 2.12 TPSA 83.8	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)[C@H](O)CCC(=O)O`
ZINC77300485 ZINC	0.553	260.3 Da LogP 2.12 TPSA 83.8	✓ Ro5	✓ Clean	`CCCCCCCCOC(=O)[C@@H](O)CCC(=O)O`
ZINC113027531 ZINC	0.548	310.4 Da LogP 3.58 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCO[P@](=O)(O)OCC[N+](C)(C)C`
ZINC1560408744 ZINC	0.548	257.2 Da LogP -0.28 TPSA 96.2	✓ Ro5	✓ Clean	`C[N+](C)(C)CCO[P@](=O)(O)OC[C](O)CO`
ZINC217410460 ZINC	0.548	338.4 Da LogP 4.36 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCO[P@@](=O)(O)OCC[N+](C)(C)C`
ZINC43562168 ZINC	0.548	352.5 Da LogP 4.75 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCO[P@@](=O)(O)OCC[N+](C)(C)C`

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.

Cross-references

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

Sequence

UniProt A0A0H3GZQ8

Chemistry

ChEMBL CHEMBL255766