KpKP13 Protein target profile

L-aspartate oxidase

Accession: KP13_00805

Gene: AHE43170.1 nadB 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H1L7

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Length 539

Pocket druggability (P2Rank · AlphaFold DB model) 0.97

Direct ligand evidence 0 76 total records

Functional annotation 1 EC 6 GO

Target summary

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

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

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.97. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 26 structural and 0 bioactivity records.

Risks to review

Evidence gaps

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

Terms and data sources used on this page

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Prioritization evidence

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

Off-target risk

Human off-target: Hit
Human identity (%): 33.459 Lower values reduce human off-target concern.
Human E-value: 1.22e-23
Gut microbiome similarity: 4.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 59.925 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 94.14 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 A0A0H3H1L7

Pocket Pocket 1

Druggability (FPocket) 0.347

Structure A0A0H3H1L7

Pocket Pocket 1

ColabFold model

P2Rank 0.986 · Pocket 1

FPocket 0.889 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 188 / 4744 genomes with a hit

Prevalence 4.0%

Cross-references

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

Sequence

UniProt A0A0H3H1L7

Sequence

Primary amino-acid sequence viewer.

MNTTPDFSCDVLIIGSGAAGLSLALRLAEHSSVTVLSKGPISEGSTFYAQGGIAAVFDETDSIESHVEDTLIAGAGLCDRHAVTFVASNARSCVQWLIDQGVLFDTQVQANGEESYHLTREGGHSHRRILHAADATGKAVETTLVDKALAHPNIRILERSNAVDLIVSDKIGLPGTRRVVGAWIWNRNKERVETCSAKAVVLATGGAAKVYQYTTNPDVSSGDGIAMAWRAGCRVANLEFNQFHPTALYHPQARNFLLTEALRGEGAHLKRPDGTRFMPDFDERGELAPRDIVARAIDHEMKRLGVDCMFLDISHKPEAFVRQHFPMIYEKLLGLGIDLTKDPVPVVPAAHYTCGGVMVDDNGRTDVDGLYAIGEVSYTGLHGANRMASNSLLECLVYGWSAAEDITRRLPLAQKVATLPAWDESQVEIPDELVVIQHNWHELRLLMWDYVGIVRTTRRLERALRRITMLQQELDEYYARFRVSNNLLELRNLVQVAELIVRCAMLRKESRGLHYTLDYPQPLPDSGPSILSPLAHIKR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.4.3.16

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:0008734 Catalysis of the reaction: L-aspartate + O2 = iminosuccinate + H2O2. Can also use fumatate as electron acceptor under anaerobic conditions, yielding succinate.
GO:0009435 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions. NAD+ is derived from various sources including vitamin B3.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0034628 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), beginning with the catabolism of L-aspartate into the precursor quinolinate. NAD+ is a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

29 records

Show feature table

Start	End	DB	Term	Name
425	539	Gene3D	G3DSA:1.20.58.100	-
10	392	Pfam	PF00890	FAD binding domain
10	392	InterPro	IPR003953	FAD-dependent oxidoreductase 2, FAD binding domain
355	377	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
11	30	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
8	522	PANTHER	PTHR42716	L-ASPARTATE OXIDASE
8	522	InterPro	IPR005288	L-aspartate oxidase
10	259	FunFam	G3DSA:3.50.50.60:FF:000060	L-aspartate oxidase
441	521	Pfam	PF02910	Fumarate reductase flavoprotein C-term
441	521	InterPro	IPR015939	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal
238	353	SUPERFAMILY	SSF56425	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
238	353	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
453	480	Coils	Coil	Coil
426	536	FunFam	G3DSA:1.20.58.100:FF:000002	L-aspartate oxidase
4	445	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
4	445	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	257	PIRSF	PIRSF000171	SDHA_APRA_LASPO
341	527	PIRSF	PIRSF000171	SDHA_APRA_LASPO
426	525	SUPERFAMILY	SSF46977	Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain
426	525	InterPro	IPR037099	Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily
248	361	Gene3D	G3DSA:3.90.700.10	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
248	361	InterPro	IPR027477	Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
10	404	Gene3D	G3DSA:3.50.50.60	-
10	404	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
248	361	FunFam	G3DSA:3.90.700.10:FF:000002	L-aspartate oxidase
370	377	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
10	32	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
8	520	NCBIfam	TIGR00551	L-aspartate oxidase
8	520	InterPro	IPR005288	L-aspartate oxidase

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

0.97

Likely same site as FPocket 1 3.4 Å 41 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.391

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Surrounding area

Pocket 3 P2Rank #3

0.268

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Surrounding area

Pocket 4 P2Rank #4

0.109

Likely same site as FPocket 1 7.8 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.08

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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

0.347 Unusual size

Likely same site as P2Rank 1 3.4 Å 41 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:290-290 Proton acceptor

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.986

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Surrounding area

Pocket 2 P2Rank #2

0.08

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Surrounding area

Pocket 3 P2Rank #3

0.059

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Surrounding area

Pocket 4 P2Rank #4

0.016

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Surrounding area

Pocket 5 P2Rank #5

0.015

Likely same site as FPocket 4 1.9 Å 9 shared residues 90% 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 #1

0.889

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Surrounding area

Pocket 2 FPocket #21

0.327

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Surrounding area

Pocket 3 FPocket #4

0.224

Likely same site as P2Rank 5 1.9 Å 9 shared residues 90% 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_A0A0H3H1L7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00805	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.

76 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 26 records from similar proteins

Structural ligands 26 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

12J PDB via homolog 381.2 Da · LogP 4.33 · TPSA 38.3 Open detail RCSB PDB

3NP PDB via homolog Detail RCSB PDB

4YP PDB via homolog Detail RCSB PDB

AT5 PDB via homolog Detail RCSB PDB

BRS 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
12J RCSB PDB	4YSZ	Q33862	381.2 Da LogP 4.33 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(c1)NC(=O)c2ccccc2I`
3NP RCSB PDB	3P4S	P00363	119.1 Da LogP -0.26 TPSA 80.4	✓ Ro5	✓ Clean	`C(C[N+](=O)[O-])C(=O)O`
4YP RCSB PDB	5C2T	Q33862	303.4 Da LogP 3.35 TPSA 69.4	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)N)OC)C/C=C(\C)/CCC=C(C)C`
AT5 RCSB PDB	3VRA	Q33862	366.2 Da LogP 2.79 TPSA 88.6	✓ Ro5	✓ Clean	`C[C@@H](C[C@H](C)C(=O)C1=C(C(=C(NC1=O)OC)OC)O)[…`
BRS RCSB PDB	1KFY	P00363	322.7 Da LogP 4.01 TPSA 106.5	✓ Ro5	✓ Clean	`C[C@H](c1ccc(cc1)Cl)c2cc(cc(c2O)[N+](=O)[O-])[N…`
CE1 RCSB PDB	1KF6	P00363	538.8 Da LogP 4.03 TPSA 94.1	1 viol.	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCO`
E23 RCSB PDB	4YSX	Q33862	335.4 Da LogP 4.93 TPSA 29.1	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(cc1)CNC(=O)c2ccccc2C(F)(F)F`
E24 RCSB PDB	4YSY	Q33862	348.2 Da LogP 4.94 TPSA 29.1	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)NCc2ccc(cc2Cl)Cl)C(F)(F)F`
EPH RCSB PDB	3VRA	Q33862	709.9 Da LogP 10.16 TPSA 134.4	2 viol.	✓ Clean	`CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…`
F3S RCSB PDB	3VRA	Q33862	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
F6A RCSB PDB	4YTM	Q33862	341.3 Da LogP 5.62 TPSA 29.1	1 viol.	✓ Clean	`c1ccc(cc1)c2cccc(c2)NC(=O)c3ccccc3C(F)(F)F`
FD8 RCSB PDB	4YTN	Q33862	447.3 Da LogP 6.45 TPSA 38.3	1 viol.	✓ Clean	`c1ccc(c(c1)C(=O)Nc2cccc(c2)Oc3c(c(c(c(c3F)F)F)F…`
FES RCSB PDB	3VRA	Q33862	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
FLC RCSB PDB	2B76	P00363	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
FTN RCSB PDB	3VRB	Q33862	323.3 Da LogP 4.74 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F`
FUM RCSB PDB	3VRB	Q33862	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
GUA RCSB PDB	3P4R	P00363	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
HQO RCSB PDB	1KF6	P00363	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(c2ccccc2[n+]1[O-])O`
MLI RCSB PDB	3VRA	Q33862	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MQ7 RCSB PDB	1L0V	P00363	649.0 Da LogP 14.10 TPSA 34.1	2 viol.	Alert	`CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CC\C=C(/C)\CC…`
MRN RCSB PDB	4YT0	Q33862	269.3 Da LogP 4.03 TPSA 38.3	✓ Ro5	✓ Clean	`Cc1ccccc1C(=O)Nc2cccc(c2)OC(C)C`
OAA RCSB PDB	1KF6	P00363	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
PBF RCSB PDB	6B58	P00363	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)c2ccc(cc2)C[C@@H](C(=O)O)N`
RQX RCSB PDB	3VR8	Q33862	263.3 Da LogP 2.41 TPSA 69.4	✓ Ro5	Alert	`CCC/C(=C/CC1=C(C(=O)C(=C(C1=O)OC)N)C)/C`
SIN RCSB PDB	1KNP	P10902	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)O`
UQ1 RCSB PDB	5C3J	Q33862	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C`

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
ZINC100014200 ZINC	1.000	494.7 Da LogP 4.02 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC100070166 ZINC	1.000	290.4 Da LogP 3.17 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCO`
ZINC100310628 ZINC	1.000	478.7 Da LogP 4.78 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC100365196 ZINC	1.000	302.5 Da LogP 4.71 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCO`
ZINC101772322 ZINC	1.000	434.7 Da LogP 4.76 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC103600921 ZINC	1.000	466.7 Da LogP 3.24 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC105794 ZINC	1.000	269.3 Da LogP 4.03 TPSA 38.3	✓ Ro5	✓ Clean	`Cc1ccccc1C(=O)Nc1cccc(OC(C)C)c1`
ZINC1479 ZINC	1.000	323.3 Da LogP 4.74 TPSA 38.3	✓ Ro5	✓ Clean	`CC(C)Oc1cccc(NC(=O)c2ccccc2C(F)(F)F)c1`
ZINC14880431 ZINC	1.000	378.6 Da LogP 3.20 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC14881140 ZINC	1.000	306.4 Da LogP 2.41 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCO`
ZINC1529909 ZINC	1.000	259.3 Da LogP 3.69 TPSA 47.2	✓ Ro5	Alert	`CCCCCCCc1cc(O)c2ccccc2[n+]1[O-]`
ZINC16051619 ZINC	1.000	350.5 Da LogP 2.42 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCOCCO`
ZINC2561081 ZINC	1.000	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2561082 ZINC	1.000	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2584424 ZINC	1.000	218.3 Da LogP 2.37 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCO`
ZINC4521877 ZINC	1.000	234.3 Da LogP 1.61 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCO`
ZINC5273610 ZINC	1.000	322.4 Da LogP 1.64 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCOCCOCCO`
ZINC58538366 ZINC	1.000	392.6 Da LogP 3.59 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC58631420 ZINC	1.000	422.6 Da LogP 3.22 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC59441819 ZINC	1.000	318.5 Da LogP 3.95 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCO`
ZINC59622400 ZINC	1.000	274.4 Da LogP 3.93 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCO`
ZINC6284606 ZINC	1.000	348.2 Da LogP 4.94 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(NCc1ccc(Cl)cc1Cl)c1ccccc1C(F)(F)F`
ZINC71788551 ZINC	1.000	334.5 Da LogP 3.19 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCO`
ZINC71788564 ZINC	1.000	262.4 Da LogP 2.39 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCO`
ZINC71788567 ZINC	1.000	406.6 Da LogP 3.98 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC8214594 ZINC	1.000	362.6 Da LogP 3.97 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCO`
ZINC88260008 ZINC	1.000	390.6 Da LogP 4.75 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCO`
ZINC95784968 ZINC	1.000	450.7 Da LogP 4.00 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC95863931 ZINC	1.000	464.7 Da LogP 4.39 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC1849711 ZINC	0.950	202.3 Da LogP 3.14 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCO`
ZINC1850542 ZINC	0.950	216.4 Da LogP 3.53 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCOCCO`
ZINC2555269 ZINC	0.950	220.3 Da LogP 1.22 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCOCCOCCOCCO`
ZINC59660505 ZINC	0.950	244.4 Da LogP 4.31 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCO`
ZINC8437287 ZINC	0.950	230.4 Da LogP 3.92 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCO`
ZINC85733754 ZINC	0.950	258.4 Da LogP 4.70 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCO`
ZINC1644613 ZINC	0.810	206.3 Da LogP 0.83 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCO`
ZINC379537 ZINC	0.791	295.3 Da LogP 3.97 TPSA 38.3	✓ Ro5	✓ Clean	`COc1cccc(NC(=O)c2ccccc2C(F)(F)F)c1`
ZINC1703342 ZINC	0.786	202.2 Da LogP 1.07 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCCC(=O)O`
ZINC9269892 ZINC	0.786	283.4 Da LogP 4.42 TPSA 38.3	✓ Ro5	✓ Clean	`CC[C@@H](C)Oc1cccc(NC(=O)c2ccccc2C)c1`
ZINC9269893 ZINC	0.786	283.4 Da LogP 4.42 TPSA 38.3	✓ Ro5	✓ Clean	`CC[C@H](C)Oc1cccc(NC(=O)c2ccccc2C)c1`
ZINC9512529 ZINC	0.778	362.2 Da LogP 4.98 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(NCCc1ccc(Cl)cc1Cl)c1ccccc1C(F)(F)F`
ZINC3554461 ZINC	0.775	293.3 Da LogP 3.94 TPSA 29.1	✓ Ro5	✓ Clean	`Cc1ccc(CNC(=O)c2ccccc2C(F)(F)F)cc1`
ZINC725613 ZINC	0.775	353.2 Da LogP 3.55 TPSA 38.3	✓ Ro5	✓ Clean	`COc1cccc(NC(=O)c2ccccc2I)c1`
ZINC59545536 ZINC	0.773	258.4 Da LogP 4.70 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCCO`
ZINC95831576 ZINC	0.773	230.4 Da LogP 3.92 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCCCO`
ZINC1529497 ZINC	0.769	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	0.769	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115 ZINC	0.769	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	0.769	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	0.769	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=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.