KpKP13 Protein target profile

Fumarate reductase flavoprotein subunit

Accession: KP13_01189

Gene: AHE44772.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A085DGZ5

Export view

Length 898

Pocket druggability (P2Rank · AlphaFold DB model) 0.97

Direct ligand evidence 0 62 total records

Functional annotation 1 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.97, FPocket 0.95). 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 0.95. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. Review the complete evidence below

Risks to review

Evidence 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 (%): 25.088 Lower values reduce human off-target concern.
Human E-value: 1.73e-13
Gut microbiome similarity: 0.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 92.27 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) 0.97

Structure A0A085DGZ5

Pocket Pocket 1

Druggability (FPocket) 0.949

Structure A0A085DGZ5

Pocket Pocket 41

ColabFold model

P2Rank 0.966 · Pocket 1

FPocket 0.907 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 41 / 4744 genomes with a hit

Prevalence 0.9%

Cross-references

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

Sequence

UniProt A0A085DGZ5

Chemistry

ChEMBL CHEMBL3903155 ChEMBL CHEMBL3931142 ChEMBL CHEMBL1908377 ChEMBL CHEMBL3894201 ChEMBL CHEMBL3921174 ChEMBL CHEMBL3931781

Sequence

Primary amino-acid sequence viewer.

MTTCTGYFDGTVTSELVEYYRARAGSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIAGLAKIAEAIKAEGSKAILQIYHGGRMVDPQLIGGRQPVAPSAIAAPREGAAMPRALSGEEVEGMIAKFGDGVRRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDITHKMARQYADDAFIIGYRFSPEEMEVPGIRFDDTMYLLEKLAARGVDYLHFSVGATLRPSIVDTSDPTPLIEKYCAMRSDTLAQVPVMGVGGVVNAADAEQGLDHGYDLIAVGRACIAYPDWASRIAAGEELELFIDSTQREALHIPEPLWRFSLVEAMIRDMSMGDAKFKPGMFVETVHDDANELVINVSLENDHIADIELAASPVQTVEFTTSFEEIRERILTANTPHVDAISGATSQSEAVKKAVAKAMLKSSKALAAEEGGNDAAPKSYDVVVVGSGGAGLAAAIQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLNDITTTGGMSIDRTHRPRDGSAVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEVQTKSIVVATGGFSANSAMVVKYRPDLEGFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFFNEMETRDKVSAAIIALPEHYAYIVFDEHVRAKNKAADEYIAKGFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGRTTALRAPINEGPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAAKRARG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Unknown

Enzyme Commission (EC)

1.3.99.1

Gene Ontology (GO)

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:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
455	892	Gene3D	G3DSA:3.50.50.60	-
455	892	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
456	878	Pfam	PF00890	FAD binding domain
456	878	InterPro	IPR003953	FAD-dependent oxidoreductase 2, FAD binding domain
359	446	Gene3D	G3DSA:3.90.1010.20	-
370	434	Pfam	PF04205	FMN-binding domain
370	434	InterPro	IPR007329	FMN-binding
360	437	SMART	SM00900	FMN_bind_2
360	437	InterPro	IPR007329	FMN-binding
1	322	SUPERFAMILY	SSF51395	FMN-linked oxidoreductases
689	834	FunFam	G3DSA:3.90.700.10:FF:000007	NADH-dependent fumarate reductase
1	333	CDD	cd04735	OYE_like_4_FMN
451	895	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
451	895	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
692	838	SUPERFAMILY	SSF56425	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
692	838	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
1	314	Pfam	PF00724	NADH:flavin oxidoreductase / NADH oxidase family
1	314	InterPro	IPR001155	NADH:flavin oxidoreductase/NADH oxidase, N-terminal
456	889	NCBIfam	TIGR01813	flavocytochrome c
456	889	InterPro	IPR010960	Flavocytochrome c
1	348	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	348	InterPro	IPR013785	Aldolase-type TIM barrel
689	834	Gene3D	G3DSA:3.90.700.10	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
689	834	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
436	896	PANTHER	PTHR43400	FUMARATE REDUCTASE

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

Download VMD script Full viewer

Loading 3D structure...

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

Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.97

Likely same site as FPocket 1 7.3 Å 21 shared residues 78% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.656

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.547

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.072

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.033

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #41

0.949 Unusual size

Likely same site as P2Rank 1 7.4 Å 22 shared residues 73% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #1

0.761

Likely same site as P2Rank 1 7.3 Å 21 shared residues 78% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.966

Likely same site as FPocket 2 5.3 Å 21 shared residues 68% of smaller site

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.89

Likely same site as FPocket 5 2.8 Å 23 shared residues 82% of smaller site

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.11

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.088

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.068

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #5

0.907 Unusual size

Likely same site as P2Rank 2 2.8 Å 23 shared residues 82% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #1

0.712

Show in viewer

Surrounding area

Pocket 3 FPocket #2

0.43 Unusual size

Likely same site as P2Rank 1 5.3 Å 21 shared residues 68% of smaller site

Show in viewer

Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A085DGZ5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01189	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.

62 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

FUM PDB via homolog 116.1 Da · LogP -0.29 · TPSA 74.6 Open detail RCSB PDB

MEZ PDB via homolog Detail RCSB PDB

MWQ PDB via homolog Detail RCSB PDB

SIN PDB via homolog Detail RCSB PDB

TEO 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
FUM RCSB PDB	1E39	P0C278	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
MEZ RCSB PDB	1Y0P	P0C278	130.1 Da LogP 0.10 TPSA 74.6	✓ Ro5	✓ Clean	`C/C(=C\C(=O)O)/C(=O)O`
MWQ RCSB PDB	6T88	Q8CVD0	140.1 Da LogP 0.43 TPSA 66.0	✓ Ro5	✓ Clean	`c1c([nH]cn1)CCC(=O)O`
SIN RCSB PDB	1D4D	P83223	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)O`
TEO RCSB PDB	1P2H	P0C278	132.1 Da LogP -3.14 TPSA 103.7	✓ Ro5	✓ Clean	`C(=C(\O)/[O-])\[C@H](C(=O)[O-])O`
URO RCSB PDB	6T87	Q8CVD0	138.1 Da LogP 0.51 TPSA 66.0	✓ Ro5	✓ Clean	`c1c(nc[nH]1)C=CC(=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
CHEMBL3903155 ChEMBL	F1KRD8	8.62 ~2.4 nM	466.6 Da LogP 5.19 TPSA 72.8	1 viol.	✓ Clean	`CC1=C[C@@](C)(O)[C@@H](C)O[C@H]1/C(C)=C/C=C/C=C…`
CHEMBL3931142 ChEMBL	F1KRD8	6.33 ~467.7 nM	466.6 Da LogP 5.19 TPSA 72.8	1 viol.	✓ Clean	`CC1=C[C@@](C)(O)[C@@H](C)O[C@@H]1/C(C)=C/C=C/C=…`
CHEMBL1908377 ChEMBL	F1KRD8	6.30 ~501.2 nM	1151.4 Da LogP 12.34 TPSA 144.8	2 viol.	Alert	`Cc1cc(/C=C/c2ccc3cc(N(C)C)ccc3[n+]2C)c(C)n1-c1c…`
CHEMBL3894201 ChEMBL	F1KRD8	6.08 ~831.8 nM	408.5 Da LogP 5.05 TPSA 52.6	1 viol.	✓ Clean	`C=C1C=C(C)[C@H](/C(C)=C/C=C/C=C/C=C/[C@]2(C)[C@…`
CHEMBL3921174 ChEMBL	F1KRD8	6.08 ~831.8 nM	440.6 Da LogP 4.90 TPSA 61.8	✓ Ro5	✓ Clean	`CO[C@@]1(C)C=C(C)[C@H](/C(C)=C/C=C/C=C/C=C/[C@]…`
CHEMBL3931781 ChEMBL	F1KRD8	6.07 ~851.1 nM	426.6 Da LogP 4.24 TPSA 72.8	✓ Ro5	✓ Clean	`CC1=C[C@](C)(O)[C@H](/C(C)=C/C=C/C=C/C=C/[C@]2(…`

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
ZINC38951971 ZINC	0.647	211.2 Da LogP -0.07 TPSA 95.1	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)NCCc1cnc[nH]1`
ZINC1529497 ZINC	0.615	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	0.615	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115 ZINC	0.615	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	0.615	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	0.615	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	0.615	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	0.615	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC13283631 ZINC	0.564	224.3 Da LogP 0.67 TPSA 55.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCOC(=O)/C=C/c1c[nH]cn1`
ZINC1572706 ZINC	0.563	260.2 Da LogP -1.05 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)NCCNC(=O)CCC(=O)O`
ZINC1703342 ZINC	0.533	202.2 Da LogP 1.07 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCCC(=O)O`
ZINC1728397 ZINC	0.533	233.2 Da LogP -0.29 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)CCN(CCC(=O)O)CCC(=O)O`
ZINC2508031 ZINC	0.533	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCC(=O)O`
ZINC2517013 ZINC	0.533	250.2 Da LogP 0.89 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCP(CCC(=O)O)CCC(=O)O`
ZINC1697439 ZINC	0.529	219.5 Da LogP 1.79 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)C(Cl)(Cl)Cl`
ZINC35465466 ZINC	0.529	244.3 Da LogP 2.24 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCC(=O)CCC(=O)O`
ZINC39208104 ZINC	0.529	262.2 Da LogP -0.20 TPSA 127.2	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)OCCOC(=O)CCC(=O)O`
ZINC329464921 ZINC	0.512	235.3 Da LogP 0.73 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CCc1cnc[nH]1)N1C[C@@H]2CC[C@H](C1)O2`
ZINC655315554 ZINC	0.512	277.3 Da LogP 2.16 TPSA 49.0	✓ Ro5	✓ Clean	`O=C(CCc1cnc[nH]1)N1Cc2cc(F)c(F)cc2C1`
ZINC100473925 ZINC	0.500	256.2 Da LogP -1.50 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)/C=C\C(=O)NCCNC(=O)/C=C\C(=O)O`
ZINC137001224 ZINC	0.500	212.0 Da LogP 1.41 TPSA 37.3	✓ Ro5	✓ Clean	`C/C(I)=C\C(=O)O`
ZINC145743383 ZINC	0.500	266.2 Da LogP 0.77 TPSA 129.0	✓ Ro5	✓ Clean	`O=C(O)CCP(=O)(CCC(=O)O)CCC(=O)O`
ZINC1542984448 ZINC	0.500	470.5 Da LogP 0.07 TPSA 148.4	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCOCCOCCC(=O)O`
ZINC1586444 ZINC	0.500	210.2 Da LogP -0.65 TPSA 108.7	✓ Ro5	✓ Clean	`O=C(O)CCS(=O)(=O)CCC(=O)O`
ZINC1679042 ZINC	0.500	256.2 Da LogP -1.50 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)/C=C/C(=O)NCCNC(=O)/C=C/C(=O)O`
ZINC1753095 ZINC	0.500	238.3 Da LogP 1.40 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCSCCSCCC(=O)O`
ZINC1911530830 ZINC	0.500	212.0 Da LogP 1.41 TPSA 37.3	✓ Ro5	✓ Clean	`CC(I)=CC(=O)O`
ZINC19255983 ZINC	0.500	205.2 Da LogP 1.08 TPSA 70.9	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Cc1cnc[nH]1)n1cccc1`
ZINC19255986 ZINC	0.500	205.2 Da LogP 1.08 TPSA 70.9	✓ Ro5	✓ Clean	`O=C(O)[C@H](Cc1cnc[nH]1)n1cccc1`
ZINC22028383 ZINC	0.500	204.2 Da LogP -0.88 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(O)CCNCCNCCC(=O)O`
ZINC22576322 ZINC	0.500	348.4 Da LogP -0.51 TPSA 155.7	✓ Ro5	✓ Clean	`O=C(O)CCN(CCC(=O)O)CCN(CCC(=O)O)CCC(=O)O`
ZINC26897400 ZINC	0.500	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC29405823 ZINC	0.500	200.3 Da LogP 2.98 TPSA 28.7	✓ Ro5	✓ Clean	`c1ccc(CCCCc2cnc[nH]2)cc1`
ZINC3074813 ZINC	0.500	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC329358154 ZINC	0.500	223.3 Da LogP 1.29 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CCc1cnc[nH]1)N1CCCCCO1`
ZINC33943644 ZINC	0.500	212.0 Da LogP 1.41 TPSA 37.3	✓ Ro5	✓ Clean	`C/C(I)=C/C(=O)O`
ZINC34423725 ZINC	0.500	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC35977596 ZINC	0.500	294.3 Da LogP 0.00 TPSA 111.5	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCC(=O)O`
ZINC38682833 ZINC	0.500	286.3 Da LogP -0.61 TPSA 115.2	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)N1CCN(C(=O)CCC(=O)O)CC1`
ZINC39383060 ZINC	0.500	206.2 Da LogP -0.03 TPSA 93.1	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCC(=O)O`
ZINC39427081 ZINC	0.500	250.2 Da LogP -0.01 TPSA 102.3	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCC(=O)O`
ZINC4181831 ZINC	0.500	232.2 Da LogP -0.01 TPSA 129.0	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)C(CC(=O)O)CC(=O)O`
ZINC4822898 ZINC	0.500	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900 ZINC	0.500	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC4866352 ZINC	0.500	282.3 Da LogP -1.06 TPSA 115.2	✓ Ro5	✓ Clean	`O=C(O)/C=C/C(=O)N1CCN(C(=O)/C=C/C(=O)O)CC1`
ZINC71257127 ZINC	0.500	426.5 Da LogP 0.05 TPSA 139.2	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCOCCC(=O)O`
ZINC71257128 ZINC	0.500	338.4 Da LogP 0.02 TPSA 120.8	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCC(=O)O`
ZINC79016464 ZINC	0.500	382.4 Da LogP 0.04 TPSA 130.0	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCC(=O)O`
ZINC8616656 ZINC	0.500	256.2 Da LogP -1.50 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)C=CC(=O)NCCNC(=O)C=CC(=O)O`
ZINC90623560 ZINC	0.500	256.2 Da LogP -1.50 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)/C=C\C(=O)NCCNC(=O)/C=C/C(=O)O`

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.