Protein target profile

VK055_3518

gpsA

Genome: KpATCC43816 Gene: AIK82074.1 gpsA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GUQ5

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Length 330

Pocket druggability 0.971

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 62 total records

Functional annotation 1 EC 13 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: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.97, P2Rank 0.92). Use the 3D pocket comparison to verify whether they identify the same site. Central metabolic position More central than 99.4% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. 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: Hit
Human identity (%): 32.967 Lower values reduce human off-target concern.
Human E-value: 1.47e-06
Gut microbiome similarity: 3.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 93.03 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: 95.4 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 0.971

Structure A0A0H3GUQ5

Pocket Pocket 1

P2Rank 0.92

Structure A0A0H3GUQ5

Pocket Pocket 1

ColabFold model

FPocket 0.976 · Pocket 1

P2Rank 0.953 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 164 / 4744 genomes with a hit

Prevalence 3.5%

Cross-references

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

Sequence

UniProt A0A0H3GUQ5

Pathways

BioCyc GLYC3PDEHYDROGBIOSYN-RXN-GLYCEROL-3P/NADP//DIHYDROXY-ACETONE-PHOSPHATE/NADPH/PROTON.59. KEGG R00842 BioCyc 1.1.1.8-RXN

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: more central than 99.4% of genes in this genome.

Relative network centrality 99.4% more central than 99.4% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MIGAGSYGTALAITLARNGHHVVLWGHDPKHIATLQHDRCNAAFLPDVPFPDTLHLESDLATALAASRDILVVVPSHVFGQVLRQIKPLMRSDARLVWATKGLEAETGRLLQDVAREALGDDIPLAVISGPTFAKELAAGLPTAISLAATDPQFAEDLQRLLHCGKSFRVYINPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLVEMSRLGAALGADPETFMGMAGLGDLVLTCTDNQSRNRRFGMMLGQGMDVQSAQDKIGQVVEGYRNTKEVRVLAQRLGVEMPITEEIYQVLYCGKIAREAALTLLGRARKDERSSN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Enzyme Commission (EC)

1.1.1.94

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:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0046168 The chemical reactions and pathways resulting in the breakdown of glycerol-3-phosphate, a phosphoric monoester of glycerol.
GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0009331 An enzyme complex that catalyzes the oxidation of sn-glycerol 3-phosphate to dihydroxyacetone phosphate, with concurrent reduction of flavin adenine dinucleotide (FAD) to FADH2. In E. coli, the complex is either a GlpA-GlpB-GlpC heterotrimer that functions in anaerobic conditions, or a GlpD homodimer that functions in aerobic conditions.
GO:0006072 The chemical reactions and pathways involving glycerol-3-phosphate, a phosphoric monoester of glycerol.
GO:0047952 Catalysis of the reaction: sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+.
GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0141152 Catalysis of the reaction: NAD+ + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H+ + NADH.
GO:0141153 NADP+ + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H+ + NADPH.
GO:0046167 The chemical reactions and pathways resulting in the formation of glycerol-3-phosphate, a phosphoric monoester of glycerol.
GO:0046474 The chemical reactions and pathways resulting in the formation of glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
184	330	Gene3D	G3DSA:1.10.1040.10	-
184	330	InterPro	IPR013328	6-phosphogluconate dehydrogenase, domain 2
175	313	Pfam	PF07479	NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus
175	313	InterPro	IPR006109	Glycerol-3-phosphate dehydrogenase, NAD-dependent, C-terminal
1	327	PIRSF	PIRSF000114	Glycerol-3-P_dh
1	327	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent
1	182	FunFam	G3DSA:3.40.50.720:FF:000019	Glycerol-3-phosphate dehydrogenase [NAD(P)+]
1	182	Gene3D	G3DSA:3.40.50.720	-
1	314	PANTHER	PTHR11728	GLYCEROL-3-PHOSPHATE DEHYDROGENASE
175	326	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
175	326	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
184	328	FunFam	G3DSA:1.10.1040.10:FF:000001	Glycerol-3-phosphate dehydrogenase [NAD(P)+]
127	147	PRINTS	PR00077	NAD-dependent glycerol-3-phosphate dehydrogenase signature
127	147	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent
168	192	PRINTS	PR00077	NAD-dependent glycerol-3-phosphate dehydrogenase signature
168	192	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent
233	250	PRINTS	PR00077	NAD-dependent glycerol-3-phosphate dehydrogenase signature
233	250	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent
193	217	PRINTS	PR00077	NAD-dependent glycerol-3-phosphate dehydrogenase signature
193	217	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent
1	18	PRINTS	PR00077	NAD-dependent glycerol-3-phosphate dehydrogenase signature
1	18	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent
51	78	PRINTS	PR00077	NAD-dependent glycerol-3-phosphate dehydrogenase signature
51	78	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent
2	173	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
2	173	InterPro	IPR036291	NAD(P)-binding domain superfamily
183	204	ProSitePatterns	PS00957	NAD-dependent glycerol-3-phosphate dehydrogenase signature.
183	204	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent
1	154	Pfam	PF01210	NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus
1	154	InterPro	IPR011128	Glycerol-3-phosphate dehydrogenase, NAD-dependent, N-terminal
1	317	Hamap	MF_00394	Glycerol-3-phosphate dehydrogenase [NAD(P)+] [gpsA].
1	317	InterPro	IPR006168	Glycerol-3-phosphate dehydrogenase, NAD-dependent

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

0.971

Likely same site as P2Rank 2 3.3 Å 15 shared residues 100% of smaller site

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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

0.92

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Surrounding area

Site 2 P2Rank #2

0.426

Likely same site as FPocket 1 3.3 Å 15 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.118

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Surrounding area

Site 4 P2Rank #4

0.002

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Surrounding area

Residue sets

UniProt: Active site:195-195 Proton acceptor

UniProt: Binding site:110-110

UniProt: Binding site:12-17

UniProt: Binding site:139-139

UniProt: Binding site:141-141

UniProt: Binding site:143-143

UniProt: Binding site:15-15

UniProt: Binding site:16-16

UniProt: Binding site:195-195

UniProt: Binding site:248-248

UniProt: Binding site:258-258

UniProt: Binding site:259-259

UniProt: Binding site:259-260

UniProt: Binding site:260-260

UniProt: Binding site:283-283

UniProt: Binding site:285-285

UniProt: Binding site:36-36

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.953

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Surrounding area

Site 2 P2Rank #2

0.415

Likely same site as FPocket 1 2.2 Å 16 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.184

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Surrounding area

Site 4 P2Rank #4

0.038

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Surrounding area

Site 5 P2Rank #5

0.026

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Surrounding area

Residue sets

UniProt: Active site:195-195 Proton acceptor

UniProt: Binding site:110-110

UniProt: Binding site:12-17

UniProt: Binding site:139-139

UniProt: Binding site:141-141

UniProt: Binding site:143-143

UniProt: Binding site:15-15

UniProt: Binding site:16-16

UniProt: Binding site:195-195

UniProt: Binding site:248-248

UniProt: Binding site:258-258

UniProt: Binding site:259-259

UniProt: Binding site:259-260

UniProt: Binding site:260-260

UniProt: Binding site:283-283

UniProt: Binding site:285-285

UniProt: Binding site:36-36

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_A0A0H3GUQ5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3518	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 ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 12 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

13P PDB via homolog 170.1 Da · LogP -1.34 · TPSA 104.1 Open detail RCSB PDB

3SY PDB via homolog Detail RCSB PDB

BCP PDB via homolog Detail RCSB PDB

BOA PDB via homolog Detail RCSB PDB

CFP 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
13P RCSB PDB	1WPQ	P21695	170.1 Da LogP -1.34 TPSA 104.1	✓ Ro5	✓ Clean	`C(C(=O)COP(=O)(O)O)O`
3SY RCSB PDB	6E8Y	P21695	136.1 Da LogP -2.06 TPSA 80.9	✓ Ro5	✓ Clean	`C(C(CO)(CO)CO)O`
BCP RCSB PDB	1M66	P90551	233.5 Da LogP 1.77 TPSA 54.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)nc(nc2Cl)Br`
BOA RCSB PDB	1M67	P90551	215.0 Da LogP 0.82 TPSA 74.7	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)nc(nc2O)Br`
CFP RCSB PDB	1JDJ	P90551	172.6 Da LogP 1.15 TPSA 54.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(nc(n2)F)Cl`
G3H RCSB PDB	1Z82	A0A0F6AK91	170.1 Da LogP -1.34 TPSA 104.1	✓ Ro5	✓ Clean	`C([C@H](C=O)O)OP(=O)(O)O`
G3P RCSB PDB	1Z82	A0A0F6AK91	172.1 Da LogP -1.55 TPSA 107.2	✓ Ro5	✓ Clean	`C([C@H](COP(=O)(O)O)O)O`
MYS RCSB PDB	1JDJ	P90551	212.4 Da LogP 6.10 TPSA 0.0	1 viol.	✓ Clean	`CCCCCCCCCCCCCCC`
NDE RCSB PDB	1N1E	P90551	831.5 Da LogP -4.94 TPSA 425.2	3 viol.	✓ Clean	`c1c[n+](cc(c1[C@H](C(=O)COP(=O)(O)O)O)C(=O)N)[C…`
NH4 RCSB PDB	1TXG	O29390	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
PLM RCSB PDB	1M66	P90551	256.4 Da LogP 5.55 TPSA 37.3	1 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)O`
POP RCSB PDB	6PYP	P21695	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(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`
ZINC15752737 ZINC	1.000	233.5 Da LogP 1.77 TPSA 54.5	✓ Ro5	✓ Clean	`Clc1nc(Br)nc2nc[nH]c12`
ZINC1628119 ZINC	1.000	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
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`
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`
ZINC1529620 ZINC	0.739	246.2 Da LogP -2.17 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(OC[C@@H](O)CO)OC[C@@H](O)CO`
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`
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`
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`
ZINC136729993 ZINC	0.708	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCC[C@@H](O)CCCCCCCC(=O)O`
ZINC14502373 ZINC	0.708	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCC[C@H](O)CCCCCCCC(=O)O`
ZINC1600678 ZINC	0.708	264.4 Da LogP 2.63 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCCS(=O)(=O)CCCCC(=O)O`
ZINC30726317 ZINC	0.708	316.5 Da LogP 4.27 TPSA 77.8	✓ Ro5	✓ Clean	`CCCCCCCC[C@@H](O)[C@H](O)CCCCCCCC(=O)O`
ZINC30730192 ZINC	0.708	316.5 Da LogP 4.27 TPSA 77.8	✓ Ro5	✓ Clean	`CCCCCCCC[C@H](O)[C@@H](O)CCCCCCCC(=O)O`
ZINC33820346 ZINC	0.708	316.5 Da LogP 4.27 TPSA 77.8	✓ Ro5	✓ Clean	`CCCCC[C@H](O)[C@@H](O)CCCCCCCCCCC(=O)O`
ZINC59200967 ZINC	0.708	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCC[C@H](O)CCCCCCCC(=O)O`
ZINC59206873 ZINC	0.708	316.5 Da LogP 4.27 TPSA 77.8	✓ Ro5	✓ Clean	`CCCCCCCC[C@H](O)[C@H](O)CCCCCCCC(=O)O`
ZINC59724711 ZINC	0.708	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`CCCCCCC[C@H](O)CCCCCC(=O)O`
ZINC8220964 ZINC	0.708	316.5 Da LogP 4.27 TPSA 77.8	✓ Ro5	✓ Clean	`CCCCCCCC[C@@H](O)[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`

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.