KpKP13 Protein target profile

Virulence factor mviN

Accession: KP13_04929

Gene: AHE45292.1 mviN 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GRG5

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Length 511

Pocket druggability (P2Rank · AlphaFold DB model) 0.949

Direct ligand evidence 0 52 total records

Functional annotation 0 EC 6 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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 0.95, FPocket 0.79). 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. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.79. This is a computational pocket signal, not binding validation. Review the complete evidence below

Risks to review

Evidence gaps

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

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 2.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 91.585 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 91.85 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) 0.949

Structure A0A0H3GRG5

Pocket Pocket 1

Druggability (FPocket) 0.789

Structure A0A0H3GRG5

Pocket Pocket 26

ColabFold model

P2Rank 0.932 · Pocket 1

FPocket 0.845 · Pocket 27

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 137 / 4744 genomes with a hit

Prevalence 2.9%

Sequence

Primary amino-acid sequence viewer.

MNLLKSLAAVSSMTMFSRVLGFARDAIVARIFGAGMATDAFFVAFKLPNLLRRIFAEGAFSQAFVPILAEYKSKQGEDATRVFVSYVSGLLTLALAIVTVIGMLAAPWVITITAPGFADTADKFALTTQLLRITFPYILLISLASLVGAILNTWNRFSVPAFAPTFLNVSMIGFALFAAPYFHPPVLALAWAVTVGGVLQLAYQLPHLKKIGMLVLPRINLKDAGAMRVVKQMGPAILGVSVSQISLIINTIFASFLVSGSVSWMYYADRLMEFPSGVLGVALGTILLPSLSKSFASGNHDEYCRLMDWGLRLCFLLALPSAVALGILAKPLTVALFQYGKFSAFDAAMTQRALVAYSVGLMGLIVVKVLAPGFYSRQDIKTPVKIAIITLIMTQVMNLAFIGPLKHAGLSLSIGLAACLNAALLYWQLRKQKIFTPQPGWLAFLLRLIIAVLVMAAALLGVMHLMPEWSLGTMPFRLMRLLAVVIAGVVAYFATLLVLGFRVKEFVRRTA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Subcellular localization

Localization: CytoplasmicMembrane

Gene Ontology (GO)

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:0015648 Enables the directed movement of lipid-linked peptidoglycans into, out of or within a cell, or between cells.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0034204 The translocation, or flipping, of lipid molecules from one monolayer of a membrane bilayer to the opposite monolayer.
GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
GO:0008360 Any process that modulates the surface configuration of a cell.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

65 records

Show feature table

Start	End	DB	Term	Name
130	152	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
186	203	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
407	429	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
349	371	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
274	296	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
82	110	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
348	370	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	511	PIRSF	PIRSF002869	MviN
1	511	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
130	154	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
237	259	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
408	429	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
236	259	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
441	466	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
383	402	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
330	348	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
159	181	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
183	187	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
3	467	Hamap	MF_02078	Probable lipid II flippase MurJ [murJ].
3	467	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
260	270	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	26	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
502	511	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
383	402	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
111	129	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
289	308	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
430	440	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
28	478	Pfam	PF03023	Lipid II flippase MurJ
28	478	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
46	81	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
26	45	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	509	PANTHER	PTHR47019	LIPID II FLIPPASE MURJ
403	407	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
478	501	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
161	182	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
155	160	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
11	431	CDD	cd13123	MATE_MurJ_like
11	431	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
372	382	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
441	463	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
206	235	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
271	288	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
309	328	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
309	329	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
33	52	PRINTS	PR01806	Virulence factor MviN signature
33	52	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
357	376	PRINTS	PR01806	Virulence factor MviN signature
357	376	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
409	426	PRINTS	PR01806	Virulence factor MviN signature
409	426	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
52	68	PRINTS	PR01806	Virulence factor MviN signature
52	68	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
259	285	PRINTS	PR01806	Virulence factor MviN signature
259	285	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
133	157	PRINTS	PR01806	Virulence factor MviN signature
133	157	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
157	178	PRINTS	PR01806	Virulence factor MviN signature
157	178	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
2	508	NCBIfam	TIGR01695	murein biosynthesis integral membrane protein MurJ
2	508	InterPro	IPR004268	Peptidoglycan biosynthesis protein MurJ
188	205	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
467	477	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
88	110	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
27	45	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
478	500	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.

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

0.949

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Surrounding area

Pocket 2 P2Rank #2

0.784

Likely same site as FPocket 28 4.3 Å 8 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.417

Likely same site as FPocket 26 1.3 Å 11 shared residues 92% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.378

Likely same site as FPocket 16 2.7 Å 9 shared residues 82% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.235

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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 #26

0.789

Likely same site as P2Rank 3 1.3 Å 11 shared residues 92% of smaller site

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Surrounding area

Pocket 2 FPocket #8

0.436

Likely same site as P2Rank 2 6.9 Å 13 shared residues 76% of smaller site

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Surrounding area

Pocket 3 FPocket #16

0.337

Likely same site as P2Rank 4 2.7 Å 9 shared residues 82% of smaller site

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Surrounding area

Pocket 4 FPocket #28

0.281

Likely same site as P2Rank 2 4.3 Å 8 shared residues 100% 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

0.932

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Surrounding area

Pocket 2 P2Rank #2

0.472

Likely same site as FPocket 11 0.8 Å 11 shared residues 92% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.458

Likely same site as FPocket 27 4.8 Å 13 shared residues 93% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.353

Likely same site as FPocket 8 1.1 Å 10 shared residues 91% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.238

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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 #27

0.845

Likely same site as P2Rank 3 4.8 Å 13 shared residues 93% of smaller site

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Surrounding area

Pocket 2 FPocket #8

0.776

Likely same site as P2Rank 4 1.1 Å 10 shared residues 91% of smaller site

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Surrounding area

Pocket 3 FPocket #11

0.638

Likely same site as P2Rank 2 0.8 Å 11 shared residues 92% of smaller site

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Surrounding area

Pocket 4 FPocket #18

0.241

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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_A0A0H3GRG5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04929	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

OLB PDB via homolog 356.5 Da · LogP 4.92 · TPSA 66.8 Open detail RCSB PDB

OLC PDB via homolog Detail RCSB PDB

ZINC1501016272 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1501016273 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1501016315 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
OLB RCSB PDB	5T77	B7IE18	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](CO)O`
OLC RCSB PDB	5T77	B7IE18	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](CO)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).

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
ZINC1501016272 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC1501016273 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC1501016315 ZINC	1.000	314.5 Da LogP 3.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC1501016316 ZINC	1.000	314.5 Da LogP 3.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC2038077522 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2038077523 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC221534416 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@@H](O)CO`
ZINC32840893 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840894 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840895 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840896 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840901 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840902 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840903 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840904 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC725433050 ZINC	1.000	342.5 Da LogP 4.53 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC725433052 ZINC	1.000	342.5 Da LogP 4.53 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC98208566 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@H](O)CO`
ZINC32840885 ZINC	0.943	300.4 Da LogP 3.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2053467566 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC=CCC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2053467567 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC=CCC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC29045599 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4557100 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4557101 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC5819989 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC5819990 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC85425978 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC29045446 ZINC	0.892	352.5 Da LogP 4.47 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\C/C=C\CCCCC(=O)OC[C@@H](O)CO`
ZINC13532428 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC13532431 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)C/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC13532435 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC13546140 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC13546141 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC2296552808 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)CC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC2296552809 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC33832849 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC35052109 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4411072 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)CC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC4411074 ZINC	0.829	372.5 Da LogP 3.89 TPSA 87.0	✓ Ro5	✓ Clean	`CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2516269 ZINC	0.824	246.3 Da LogP 2.02 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840883 ZINC	0.824	302.5 Da LogP 3.58 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840884 ZINC	0.824	302.5 Da LogP 3.58 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840889 ZINC	0.824	316.5 Da LogP 3.97 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840890 ZINC	0.824	316.5 Da LogP 3.97 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840891 ZINC	0.824	330.5 Da LogP 4.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840892 ZINC	0.824	330.5 Da LogP 4.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC72400435 ZINC	0.824	344.5 Da LogP 4.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC77313111 ZINC	0.824	344.5 Da LogP 4.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC8437476 ZINC	0.824	274.4 Da LogP 2.80 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@H](O)CO`
ZINC8437478 ZINC	0.824	274.4 Da LogP 2.80 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@@H](O)CO`

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 A0A0H3GRG5