Protein target profile

KP13_03430

Choline dehydrogenase

Genome: KpKP13 Gene: AHE45805.1 betA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GL29

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Length 554

Pocket druggability 0.877

Direct ligand evidence 0 57 total records

Functional annotation 2 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 0.88, P2Rank 0.98). 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 0.88. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.98. 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 (%): 47.849 Lower values reduce human off-target concern.
Human E-value: 4.62e-171
Gut microbiome similarity: 1.9% 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.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 96.02 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 0.877

Structure A0A0H3GL29

Pocket Pocket 1

P2Rank 0.983

Structure A0A0H3GL29

Pocket Pocket 1

ColabFold model

FPocket 0.992 · Pocket 1

P2Rank 0.991 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 91 / 4744 genomes with a hit

Prevalence 1.9%

Cross-references

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

Sequence

UniProt A0A0H3GL29

Sequence

Primary amino-acid sequence viewer.

MQFDYIIIGAGSAGNVLATRLTEDPNTTVLLLEAGGPDYRFDFRTQMPAALAYPLQGKRYNWAYETEPEPYMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLDNWAKEPGLEHWSYLDCLPYYRKAETRDIGPNDYHGGDGPVSVTTPKPGNNPLFEAMVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPQGRRTSTARGYLDQARGRPNLTIRTHALTDHIIFAGKRAVGVEWLEGESTIPSKATANKEVLLCAGAIASPQILQRSGVGNPELLRQFDIPVVHDLPGVGENLQDHLEMYLQYECKEPVSLYPALQWWNQPKIGAEWLFGGTGIGASNQFEAGGFIRSRAEFAWPNIQYHFLPVAINYNGSNAVKEHGFQCHVGSMRSPSRGHVRLKSRDPHAHPAILFNYMSHEQDWQEFRDAIRITREIMNQPALDKYRGREISPGIECQSDAELDEFVRNHAETAFHPCGTCKMGYDEMAVVDGEGRVHGLEGLRVVDASIMPQIITGNLNATTIMIGEKMADAIRGRQPLPRSTATYYVAGDAPVRR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 6 GO

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0019285 The chemical reactions and pathways resulting in the formation of betaine (N-trimethylglycine) from the oxidation of choline.
GO:0016614 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0008812 Catalysis of the reaction: A + choline = AH(2) + betaine aldehyde.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0008802 Catalysis of the reaction: betaine aldehyde + NAD+ + H2O = betaine + NADH + H+.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
82	105	ProSitePatterns	PS00623	GMC oxidoreductases signature 1.
82	105	InterPro	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
259	273	ProSitePatterns	PS00624	GMC oxidoreductases signature 2.
259	273	InterPro	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
1	535	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
1	535	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	538	PIRSF	PIRSF000137	Alcohol_oxidase
1	538	InterPro	IPR012132	Glucose-methanol-choline oxidoreductase
3	539	PANTHER	PTHR11552	GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE
3	539	InterPro	IPR012132	Glucose-methanol-choline oxidoreductase
1	554	Hamap	MF_00750	Oxygen-dependent choline dehydrogenase [betA].
1	554	InterPro	IPR011533	Oxygen-dependent choline dehydrogenase
295	477	SUPERFAMILY	SSF54373	FAD-linked reductases, C-terminal domain
3	300	Pfam	PF00732	GMC oxidoreductase
3	300	InterPro	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
393	527	Pfam	PF05199	GMC oxidoreductase
393	527	InterPro	IPR007867	Glucose-methanol-choline oxidoreductase, C-terminal
4	537	NCBIfam	TIGR01810	choline dehydrogenase
4	537	InterPro	IPR011533	Oxygen-dependent choline dehydrogenase
43	472	Gene3D	G3DSA:3.30.560.10	Glucose Oxidase, domain 3
4	525	Gene3D	G3DSA:3.50.50.60	-
4	525	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily

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 #1

0.877

Likely same site as P2Rank 1 0.8 Å 44 shared residues 96% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #2

0.777

Likely same site as P2Rank 2 2.2 Å 24 shared residues 100% 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

0.983

Likely same site as FPocket 1 0.8 Å 44 shared residues 96% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.77

Likely same site as FPocket 2 2.2 Å 24 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.098

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Surrounding area

Site 4 P2Rank #4

0.05

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Surrounding area

Site 5 P2Rank #5

0.047

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Surrounding area

Residue sets

UniProt: Active site:473-473 Proton acceptor

UniProt: Binding site:4-33

Binding pockets · FPocket

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

Site 1 FPocket #1

0.992

Likely same site as P2Rank 1 0.9 Å 52 shared residues 96% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #17

0.868

Likely same site as P2Rank 2 2.8 Å 19 shared residues 95% 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

0.991

Likely same site as FPocket 1 0.9 Å 52 shared residues 96% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.564

Likely same site as FPocket 17 2.8 Å 19 shared residues 95% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.143

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Surrounding area

Site 4 P2Rank #4

0.077

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Surrounding area

Site 5 P2Rank #5

0.054

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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_A0A0H3GL29	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03430	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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ANN PDB via homolog 152.1 Da · LogP 1.39 · TPSA 46.5 Open detail RCSB PDB

BET PDB via homolog Detail RCSB PDB

FAO PDB via homolog Detail RCSB PDB

FDA PDB via homolog Detail RCSB PDB

PLM 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
ANN RCSB PDB	5OC1	O94219	152.1 Da LogP 1.39 TPSA 46.5	✓ Ro5	✓ Clean	`COc1ccc(cc1)C(=O)O`
BET RCSB PDB	4MJW	Q7X2H8	118.2 Da LogP -0.22 TPSA 37.3	✓ Ro5	✓ Clean	`C[N+](C)(C)CC(=O)O`
FAO RCSB PDB	2JBV	Q7X2H8	789.6 Da LogP -2.56 TPSA 355.8	3 viol.	✓ Clean	`Cc1cc2c(cc1C)[N@@]([C@@H]3[C@H](N2)C(=O)NC(=O)N…`
FDA RCSB PDB	4YNT	B8MX95	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
PLM RCSB PDB	5NCC	A0A248QE08	256.4 Da LogP 5.55 TPSA 37.3	1 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)O`
PXM RCSB PDB	4HA6	Q5NT46	168.2 Da LogP 0.05 TPSA 79.4	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)CO)CN)O`
STE RCSB PDB	6ZH7	A0A248QE08	284.5 Da LogP 6.33 TPSA 37.3	1 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=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).

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
ZINC1529498 ZINC	1.000	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
ZINC1530417 ZINC	1.000	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
ZINC1628119 ZINC	1.000	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
ZINC11802360 ZINC	0.870	244.2 Da LogP 3.19 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(Oc2ccc(C(=O)O)cc2)cc1`
ZINC1514433 ZINC	0.870	228.2 Da LogP 3.06 TPSA 46.5	✓ Ro5	✓ Clean	`COc1ccc(-c2ccc(C(=O)O)cc2)cc1`
ZINC138457918 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCC(=O)O`
ZINC138458029 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCC(=O)O`
ZINC144395054 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCC(=O)O`
ZINC14619628 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCCCC(=O)O`
ZINC196749828 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCC(=O)O`
ZINC2113934076 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCC(=O)O`
ZINC2113934082 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCC(=O)O`
ZINC2113934083 ZINC	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCC(=O)O`
ZINC2243670 ZINC	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCC(=O)O`
ZINC2569203 ZINC	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCC(=O)O`
ZINC4798470 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC5973005 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCC(=O)O`
ZINC71418182 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)CCCCC(=O)O`
ZINC79244776 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCCC(=O)O`
ZINC86037082 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC86037089 ZINC	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCCCC(=O)O`
ZINC86039283 ZINC	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCC(=O)O`
ZINC3160730 ZINC	0.810	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCC(=O)O`
ZINC4582907 ZINC	0.810	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCC(=O)O`
ZINC4727003 ZINC	0.810	312.4 Da LogP 4.69 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCC(=O)CCCCCCCC(=O)O`
ZINC86037074 ZINC	0.810	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)CCCC(=O)O`
ZINC2378801 ZINC	0.800	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCC(=O)O`
ZINC1556261 ZINC	0.769	242.3 Da LogP 2.98 TPSA 46.5	✓ Ro5	✓ Clean	`COc1ccc(Cc2ccc(C(=O)O)cc2)cc1`
ZINC39238945 ZINC	0.769	272.3 Da LogP 2.61 TPSA 72.8	✓ Ro5	✓ Clean	`COc1ccc(C(=O)Oc2ccc(C(=O)O)cc2)cc1`
ZINC9195331 ZINC	0.769	270.3 Da LogP 3.72 TPSA 46.5	✓ Ro5	✓ Clean	`COc1ccc(C(C)(C)c2ccc(C(=O)O)cc2)cc1`
ZINC2113934081 ZINC	0.762	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCCCCCC(=O)O`
ZINC2243668 ZINC	0.762	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCC(=O)O`
ZINC2378799 ZINC	0.762	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCC(=O)O`
ZINC33820423 ZINC	0.762	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCCCC(=O)O`
ZINC1675842 ZINC	0.741	292.3 Da LogP 2.23 TPSA 80.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)c2ccc(C(=O)O)cc2)cc1`
ZINC2387442 ZINC	0.739	246.4 Da LogP 4.34 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCSCCCCC(=O)O`
ZINC31778284 ZINC	0.739	310.4 Da LogP 4.47 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)/C=C\C(=O)CCCCCCCC(=O)O`
ZINC5540108 ZINC	0.739	310.4 Da LogP 4.47 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)/C=C/C(=O)CCCCCCCC(=O)O`
ZINC64633397 ZINC	0.739	226.4 Da LogP 4.55 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC(=O)O`
ZINC128920 ZINC	0.731	202.2 Da LogP 2.55 TPSA 46.5	✓ Ro5	✓ Clean	`COc1ccc2cc(C(=O)O)ccc2c1`
ZINC1566855 ZINC	0.727	270.3 Da LogP 2.77 TPSA 52.6	✓ Ro5	Alert	`COc1ccc(C(=O)C(=O)c2ccc(OC)cc2)cc1`
ZINC59545317 ZINC	0.727	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCC(=O)O`
ZINC59545320 ZINC	0.727	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)CCC(=O)O`
ZINC59545336 ZINC	0.727	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCC(=O)O`
ZINC397461 ZINC	0.714	286.3 Da LogP 3.04 TPSA 87.7	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)Nc2ccc(C(=O)O)cc2)cc1`
ZINC100292624 ZINC	0.708	344.4 Da LogP 2.63 TPSA 111.9	✓ Ro5	✓ Clean	`CCCCCCC(=O)[C@@H](O)[C@H](O)C(=O)CCCCCCCC(=O)O`
ZINC117423079 ZINC	0.708	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCC[C@H](O)CCCCC(=O)O`
ZINC59200967 ZINC	0.708	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCC[C@H](O)CCCCCCCC(=O)O`
ZINC85857782 ZINC	0.708	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCCCC[C@@H](O)CCCCCCC(=O)O`
ZINC85858219 ZINC	0.708	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@H](O)CCCCC(=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.