Genome KpATCC43816

Protein target profile

putative 2Fe-2S cluster-containing protein

Accession: VK055_1464

Gene: AIK80085.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GV80

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Length 374

Pocket druggability (P2Rank) 0.906

Direct ligand evidence 0 58 total records

Functional annotation 1 EC 5 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 0.91, FPocket 0.98). 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 0.98. This is a computational pocket signal, not binding validation. 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: 0.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 26.794 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.33 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) 0.906

Structure A0A0H3GV80

Pocket Pocket 1

Druggability (FPocket) 0.979

Structure A0A0H3GV80

Pocket Pocket 1

ColabFold model

P2Rank 0.907 · Pocket 1

FPocket 0.982 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 25 / 4744 genomes with a hit

Prevalence 0.5%

Cross-references

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

Sequence

UniProt A0A0H3GV80

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.

MSNLSPDFTLPINFCDNPQDAWTIPARFYTDSQAFEHEKERIFANSWICVAHGSEVARPNDYITREIIGENIVIVRGRDNILRAFYNVCPHRGHQLLSGEGKAKNVITCPYHAWAFKLDGNLAHARNCENVANFDSEKATLVPVRLEEYAGFVFINMNPEAESVETQLPGLQDKVLEACPDVHDLKLAARFTTLTPANWKNIVDNYLECYHCGPAHPGFSDSVQVDRYWHTMHGKWTLQYGFAKPSEQSFKFEEGTDAAFHGFWLWPCTMFNVTPIKGMMTVIYEFPVDEETTLQNYDIYFTNEELTDDQKALIEWYRDVFRPEDLRLVESVQKGLKSRGYRGQGRIMADNSGSGISEHGIAHFHNLVAQVFQP

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.14.13.239

Gene Ontology (GO)

GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.
GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0005506 Binding to an iron (Fe) ion.
GO:0009437 The chemical reactions and pathways involving carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
GO:0016709 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

31 records

Show feature table

Start	End	DB	Term	Name
248	373	Gene3D	G3DSA:3.90.380.10	-
166	247	Gene3D	G3DSA:3.90.380.10	-
15	160	SUPERFAMILY	SSF50022	ISP domain
15	160	InterPro	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily
46	134	Pfam	PF00355	Rieske [2Fe-2S] domain
46	134	InterPro	IPR017941	Rieske [2Fe-2S] iron-sulphur domain
188	371	CDD	cd08886	RHO_alpha_C_2
44	165	Gene3D	G3DSA:2.102.10.10	-
44	165	InterPro	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily
61	76	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
61	76	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
103	123	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
103	123	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
31	56	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
31	56	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
144	170	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
144	170	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
82	102	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
82	102	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
47	163	CDD	cd03469	Rieske_RO_Alpha_N
89	112	ProSitePatterns	PS00570	Bacterial ring hydroxylating dioxygenases alpha-subunit signature.
89	112	InterPro	IPR015881	Aromatic-ring-hydroxylating dioxygenase, 2Fe-2S-binding site
47	155	ProSiteProfiles	PS51296	Rieske [2Fe-2S] iron-sulfur domain profile.
47	155	InterPro	IPR017941	Rieske [2Fe-2S] iron-sulphur domain
1	373	Hamap	MF_02097	Carnitine monooxygenase oxygenase subunit.
1	373	InterPro	IPR039004	Carnitine monooxygenase oxygenase subunit
14	372	PANTHER	PTHR43756	CHOLINE MONOOXYGENASE, CHLOROPLASTIC
14	372	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
160	371	SUPERFAMILY	SSF55961	Bet v1-like
184	371	Pfam	PF00848	Ring hydroxylating alpha subunit (catalytic domain)
184	371	InterPro	IPR015879	Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain

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

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

Pocket 1 P2Rank #1

0.906

Likely same site as FPocket 1 1.3 Å 22 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.472

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Surrounding area

Pocket 3 P2Rank #3

0.029

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Surrounding area

Pocket 4 P2Rank #4

0.012

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Surrounding area

Pocket 5 P2Rank #5

0.012

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.979

Likely same site as P2Rank 1 1.3 Å 22 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:109-109

UniProt: Binding site:112-112

UniProt: Binding site:211-211

UniProt: Binding site:216-216

UniProt: Binding site:325-325

UniProt: Binding site:89-89

UniProt: Binding site:91-91

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.907

Likely same site as FPocket 1 0.8 Å 25 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.52

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Surrounding area

Pocket 3 P2Rank #3

0.08

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Surrounding area

Pocket 4 P2Rank #4

0.009

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Surrounding area

Pocket 5 P2Rank #5

0.009

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Surrounding area

Residue sets

UniProt: Binding site:109-109

UniProt: Binding site:112-112

UniProt: Binding site:211-211

UniProt: Binding site:216-216

UniProt: Binding site:325-325

UniProt: Binding site:89-89

UniProt: Binding site:91-91

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_A0A0H3GV80	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1464	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.

58 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 8 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

152 PDB via homolog 162.2 Da · LogP -0.47 · TPSA 57.5 Open detail RCSB PDB

3BY PDB via homolog Detail RCSB PDB

AZI PDB via homolog Detail RCSB PDB

BNL PDB via homolog Detail RCSB PDB

FES 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
152 RCSB PDB	6Y9C	D0C9N6	162.2 Da LogP -0.47 TPSA 57.5	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@@H](CC(=O)O)O`
3BY RCSB PDB	4QUP	Q92ZP9	129.2 Da LogP 0.17 TPSA 40.5	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)O`
AZI RCSB PDB	4QUQ	Q92ZP9	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BNL RCSB PDB	2GBX	A2TC87	154.2 Da LogP 3.35 TPSA 0.0	✓ Ro5	✓ Clean	`c1ccc(cc1)c2ccccc2`
FES RCSB PDB	2GBW	A2TC87	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
MBN RCSB PDB	3EN1	A5W4F2	92.1 Da LogP 2.00 TPSA 0.0	✓ Ro5	✓ Clean	`Cc1ccccc1`
OXY RCSB PDB	2GBW	A2TC87	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`
PE3 RCSB PDB	3EN1	A5W4F2	634.8 Da LogP -0.81 TPSA 160.5	2 viol.	✓ Clean	`C(COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO)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
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`
ZINC881607888 ZINC	0.600	214.3 Da LogP 1.04 TPSA 23.6	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCC(F)CC1`
ZINC967435 ZINC	0.600	233.1 Da LogP 4.12 TPSA 0.0	✓ Ro5	✓ Clean	`Brc1ccc(-c2ccccc2)cc1`
ZINC1580159 ZINC	0.588	210.3 Da LogP -0.26 TPSA 58.9	✓ Ro5	✓ Clean	`OCCOCCSCCOCCO`
ZINC170877414 ZINC	0.581	279.4 Da LogP 0.55 TPSA 43.9	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCN(C(=O)C2CCC2)CC1`
ZINC195163670 ZINC	0.581	293.4 Da LogP 0.94 TPSA 43.9	✓ Ro5	✓ Clean	`CN1CCC[C@@H]1C(=O)N1CCN(C(=O)C2CCCC2)CC1`
ZINC195163684 ZINC	0.581	293.4 Da LogP 0.94 TPSA 43.9	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCN(C(=O)C2CCCC2)CC1`
ZINC334287038 ZINC	0.581	214.3 Da LogP 0.66 TPSA 23.6	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCSCC1`
ZINC2555269 ZINC	0.579	220.3 Da LogP 1.22 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCOCCOCCOCCO`
ZINC258828116 ZINC	0.579	452.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC33967025 ZINC	0.579	252.3 Da LogP -0.87 TPSA 94.5	✓ Ro5	✓ Clean	`O=C(O)COCCOCCOCCOCCO`
ZINC575408819 ZINC	0.579	383.5 Da LogP -1.00 TPSA 99.1	✓ Ro5	✓ Clean	`CN(CCOCCOCCOCCO)CCOCCOCCOCCO`
ZINC79016673 ZINC	0.579	232.3 Da LogP -0.32 TPSA 57.2	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCO`
ZINC96503366 ZINC	0.579	408.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`C#CCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC96503425 ZINC	0.579	222.2 Da LogP -0.50 TPSA 85.2	✓ Ro5	✓ Clean	`O=C(O)CCOCCOCCOCCO`
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.