Protein target profile

KP13_03277

2-oxoglutarate dehydrogenase E1 component

Genome: KpKP13 Gene: sucA AHE45656.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GQ15

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Length 935

Pocket druggability 0.729

Direct ligand evidence 0 60 total records

Functional annotation 1 EC 6 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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

Main supporting evidence

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.73, P2Rank 0.83). 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 0.73. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.83. 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 (%): 47.101 Lower values reduce human off-target concern.
Human E-value: 1.94e-39
Gut microbiome similarity: 4.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 93.797 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 93.66 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.729

Structure A0A0H3GQ15

Pocket Pocket 49

P2Rank 0.835

Structure A0A0H3GQ15

Pocket Pocket 1

ColabFold model

FPocket 0.606 · Pocket 59

P2Rank 0.876 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 195 / 4744 genomes with a hit

Prevalence 4.1%

Cross-references

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

Sequence

UniProt A0A0H3GQ15

Sequence

Primary amino-acid sequence viewer.

MQNGAMKAWLDSSYLSGSNQSWIEQLYEDFLTDPDSVDANWRSMFQQLPGTGVKPDQFHSKTRDYFRRLAKDASRYTSSISDPDTNVKQVKVLQLINAYRFRGHQHANLDPLGLWKQERVADLDPAYHDLTEADFQESYNVGSFAIGKDTMKLGELIAALKQTYCGSIGAEYMHITSTEEKRWIQQRIESVAGKASFTAEEKKRFLSELTAAEGLERYLGAKFPGAKRFSLEGGDALIPMLKEMIRHAGKSGTREVVLGMAHRGRLNVLVNVLGKKPQDLFDEFAGKHKEHLGTGDVKYHMGFSSDMETEGGLVHLALAFNPSHLEIVSPVVIGSVRARLDRLDEPSSNKVLPITIHGDAAVTGQGVVQETLNMSKARGYEVGGTVRIVINNQVGFTTSNPLDARSTPYCTDIGKMVQAPIFHVNADDPEAVAFVTRLALDFRNTFKRDVFIDLVCYRRHGHNEADEPSATQPLMYQKIKKHPTPRKIYADKLEQEKVATLEDATEQVNLYRDALDAGECVVQEWRPMNMHSFTWSPYLNHEWDESYPDKVEPKRLQELAKRISTVPEGIEMQSRVAKIYADRQAMAAGEKLFDWGGAENLAYATLVDEGIPVRLSGEDSGRGTFFHRHAVIHNQTNGSTYTPLQHVHNGQGQFRVWDSVLSEEAVLAFEYGYATAEPRTLTIWEAQFGDFANGAQVVIDQFISSGEQKWGRMCGLVMLLPHGYEGQGPEHSSARLERYLQLCAEQNMQVCVPSTPAQVYHMLRRQALRGMRRPLVVMSPKSLLRHPLAVSSMDELANGTFLPAIGEIDQLDPQAVKRVVLCSGKVYYDLLEQRRKNEQKDVAIVRIEQLYPFPHQAVQEALKAYAHVHDFVWCQEEPLNQGAWYCSQHHFREVIPFGASLRYAGRPASASPAVGYMSVHQKQQQDLVNDALNVD

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1.2.4.2

Gene Ontology (GO)

GO:0016624 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces a disulfide.
GO:0004591 Catalysis of the reaction: N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H+ = N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2.
GO:0030976 Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0045252 A multi-enzyme complex that catalyzes the oxidative decarboxylation of alpha-ketoglutarate (also known as 2-oxoglutarate) to form succinyl-CoA. The complex comprises multiple copies of three enzymes referred to as E1, E2 and E3: oxoglutarate dehydrogenase (lipoamide) (E1), dihydrolipoamide S-succinyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). Additional proteins may also be present.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

31 records

Show feature table

Start	End	DB	Term	Name
593	787	Pfam	PF02779	Transketolase, pyrimidine binding domain
593	787	InterPro	IPR005475	Transketolase-like, pyrimidine-binding domain
12	50	Pfam	PF16078	2-oxoglutarate dehydrogenase N-terminus
12	50	InterPro	IPR032106	2-oxoglutarate dehydrogenase E1 component, N-terminal domain
1	934	PIRSF	PIRSF000157	Oxoglu_dh_E1
1	934	InterPro	IPR011603	2-oxoglutarate dehydrogenase E1 component
84	166	Gene3D	G3DSA:1.10.287.1150	TPP helical domain
576	793	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
576	793	InterPro	IPR029061	Thiamin diphosphate-binding fold
215	476	CDD	cd02016	TPP_E1_OGDC_like
828	848	Coils	Coil	Coil
790	932	Pfam	PF16870	2-oxoglutarate dehydrogenase C-terminal
790	932	InterPro	IPR031717	Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal
14	932	NCBIfam	TIGR00239	2-oxoglutarate dehydrogenase E1 component
14	932	InterPro	IPR011603	2-oxoglutarate dehydrogenase E1 component
555	802	Gene3D	G3DSA:3.40.50.12470	-
791	931	FunFam	G3DSA:3.40.50.11610:FF:000001	2-oxoglutarate dehydrogenase E1 component
167	533	FunFam	G3DSA:3.40.50.970:FF:000014	2-oxoglutarate dehydrogenase E1 component
167	533	Gene3D	G3DSA:3.40.50.970	-
12	932	PANTHER	PTHR23152	2-OXOGLUTARATE DEHYDROGENASE
12	932	InterPro	IPR011603	2-oxoglutarate dehydrogenase E1 component
723	931	Gene3D	G3DSA:3.40.50.11610	-
723	931	InterPro	IPR042179	Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain superfamily
221	506	Pfam	PF00676	Dehydrogenase E1 component
221	506	InterPro	IPR001017	Dehydrogenase, E1 component
593	786	SMART	SM00861	Transket_pyr_3
593	786	InterPro	IPR005475	Transketolase-like, pyrimidine-binding domain
84	166	FunFam	G3DSA:1.10.287.1150:FF:000004	2-oxoglutarate dehydrogenase E1 component
555	726	FunFam	G3DSA:3.40.50.12470:FF:000002	2-oxoglutarate dehydrogenase E1 component
120	548	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
120	548	InterPro	IPR029061	Thiamin diphosphate-binding fold

3D structure

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

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Pocket score High Medium Low

How colors and pocket overlays are used

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

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

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

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

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

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

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

Binding pockets · FPocket

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

Site 1 FPocket #49

0.729

Likely same site as P2Rank 5 2.4 Å 10 shared residues 91% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #50

0.673

Likely same site as P2Rank 1 2.0 Å 19 shared residues 90% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.835

Likely same site as FPocket 50 2.0 Å 19 shared residues 90% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.815

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Surrounding area

Site 3 P2Rank #3

0.44

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Surrounding area

Site 4 P2Rank #4

0.393

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Surrounding area

Site 5 P2Rank #5

0.278

Likely same site as FPocket 49 2.4 Å 10 shared residues 91% of smaller site

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #59

0.606

Likely same site as P2Rank 5 5.2 Å 10 shared residues 71% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #42

0.535

Likely same site as P2Rank 1 2.1 Å 19 shared residues 86% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #14

0.517

Likely same site as P2Rank 4 2.6 Å 13 shared residues 87% of smaller site

Unusual size

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Surrounding area

Site 4 FPocket #58

0.493

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.876

Likely same site as FPocket 42 2.1 Å 19 shared residues 86% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.847

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Surrounding area

Site 3 P2Rank #3

0.366

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Surrounding area

Site 4 P2Rank #4

0.223

Likely same site as FPocket 14 2.6 Å 13 shared residues 87% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.196

Likely same site as FPocket 59 5.2 Å 10 shared residues 71% 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_A0A0H3GQ15	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03277	ColabFold	—	—	full sequence	—	Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

60 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 10 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

DW3 PDB via homolog 60.1 Da · LogP -0.82 · TPSA 37.3 Open detail RCSB PDB

JQ5 PDB via homolog Detail RCSB PDB

OAA PDB via homolog Detail RCSB PDB

QSP PDB via homolog Detail RCSB PDB

TD6 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
DW3 RCSB PDB	6KMA	A0A3Q0L1E1	60.1 Da LogP -0.82 TPSA 37.3	✓ Ro5	✓ Clean	`C(C=O)O`
JQ5 RCSB PDB	6R2C	A0R2B1	210.1 Da LogP 0.60 TPSA 100.9	✓ Ro5	✓ Clean	`CCOP(=O)(C(=O)CCC(=O)O)O`
OAA RCSB PDB	6VEF	P0AFG3	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
QSP RCSB PDB	6R29	A0R2B1	608.4 Da LogP 0.82 TPSA 283.4	3 viol.	✓ Clean	`Cc1ncc(c(n1)N)CN2[C@H](SC(=C2C)CCOP(=O)(O)OP(=O…`
TD6 RCSB PDB	3ZHS	A0R2B1	527.4 Da LogP 0.74 TPSA 226.5	2 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@H](CCC(=O)O)O)CCO…`
TD7 RCSB PDB	2Y0P	A0R2B1	526.4 Da LogP 2.36 TPSA 225.9	3 viol.	✓ Clean	`Cc1ncc(c(n1)N)CN2C(=C(SC2=C(CCC(=O)O)O)CCO[P@](…`
TD8 RCSB PDB	3ZHU	A0R2B1	541.4 Da LogP 1.13 TPSA 226.5	2 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@@H](CCCC(=O)O)O)C…`
TD9 RCSB PDB	3ZHT	A0R2B1	541.4 Da LogP 1.13 TPSA 226.5	2 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@H](CCCC(=O)O)O)CC…`
TDW RCSB PDB	3ZHV	A0R2B1	469.4 Da LogP 0.90 TPSA 189.2	✓ Ro5	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@H](C)O)CCOP(=O)(O…`
ZP1 RCSB PDB	6R2A	A0R2B1	636.5 Da LogP 1.87 TPSA 272.4	3 viol.	✓ Clean	`CCOP(=O)([C@@](CCC(=O)O)([C@@H]1N(C(=C(S1)CCOP(…`

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
ZINC12501520 ZINC	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716 ZINC	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC115086873 ZINC	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264 ZINC	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823 ZINC	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1542984442 ZINC	0.688	413.5 Da LogP -0.93 TPSA 120.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1565503710 ZINC	0.688	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792028 ZINC	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057 ZINC	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC230494776 ZINC	0.688	325.4 Da LogP -0.96 TPSA 101.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38917157 ZINC	0.688	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5650743 ZINC	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182 ZINC	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC83253921 ZINC	0.688	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC90741446 ZINC	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447 ZINC	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`
ZINC144169243 ZINC	0.647	281.3 Da LogP -1.37 TPSA 89.4	✓ Ro5	✓ Clean	`OCCOCCOCCNCCOCCOCCO`
ZINC205758716 ZINC	0.647	457.6 Da LogP -1.31 TPSA 126.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCNCCOCCOCCOCCOCCO`
ZINC575441396 ZINC	0.647	369.5 Da LogP -1.34 TPSA 107.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCNCCOCCOCCOCCO`
ZINC1644613 ZINC	0.611	206.3 Da LogP 0.83 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCO`
ZINC258839852 ZINC	0.611	276.3 Da LogP 0.61 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCC(F)(F)F`
ZINC167715346 ZINC	0.600	266.3 Da LogP -0.18 TPSA 77.4	✓ Ro5	✓ Clean	`OCCCOCCOCCOCCOCCCO`
ZINC34160867 ZINC	0.600	222.3 Da LogP -0.20 TPSA 68.2	✓ Ro5	✓ Clean	`OCCCOCCOCCOCCCO`
ZINC8215517 ZINC	0.592	425.3 Da LogP 0.84 TPSA 169.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…`
ZINC1580159 ZINC	0.588	210.3 Da LogP -0.26 TPSA 58.9	✓ Ro5	✓ Clean	`OCCOCCSCCOCCO`
ZINC1542984432 ZINC	0.579	398.4 Da LogP -0.43 TPSA 122.1	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC207588231 ZINC	0.579	207.3 Da LogP -0.75 TPSA 60.0	✓ Ro5	✓ Clean	`CNCCOCCOCCOCCO`
ZINC2555269 ZINC	0.579	220.3 Da LogP 1.22 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCOCCOCCOCCO`
ZINC33967025 ZINC	0.579	252.3 Da LogP -0.87 TPSA 94.5	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCO`
ZINC39267847 ZINC	0.579	208.2 Da LogP -0.89 TPSA 85.2	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCO`
ZINC575408819 ZINC	0.579	383.5 Da LogP -1.00 TPSA 99.1	✓ Ro5	✓ Clean	`CN(CCOCCOCCOCCO)CCOCCOCCOCCO`
ZINC575440725 ZINC	0.579	295.4 Da LogP -1.03 TPSA 80.6	✓ Ro5	✓ Clean	`CN(CCOCCOCCO)CCOCCOCCO`
ZINC83254085 ZINC	0.579	354.4 Da LogP -0.45 TPSA 112.9	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCO`
ZINC83254087 ZINC	0.579	266.3 Da LogP -0.48 TPSA 94.5	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCO`
ZINC95920522 ZINC	0.579	296.3 Da LogP -0.85 TPSA 103.7	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCOCCO`
ZINC96503366 ZINC	0.579	408.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC96503406 ZINC	0.579	276.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCOCCO`
ZINC96503526 ZINC	0.579	442.5 Da LogP -0.41 TPSA 131.4	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCOCCOCCOCCOCCOCCO`

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.