Protein target profile

VK055_1110

short chain dehydrogenase family protein

Genome: KpATCC43816 Gene: AIK79733.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GS90

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Length 253

Pocket druggability 0.974

Direct ligand evidence 0 60 total records

Functional annotation 0 EC 1 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

Second pocket predictor agrees P2Rank predicted binding-site probability 0.95. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 9 structural and 1 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 (%): 39.796 Lower values reduce human off-target concern.
Human E-value: 6.47e-11
Gut microbiome similarity: 1.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 38.153 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.04 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 0.974

Structure A0A0H3GS90

Pocket Pocket 1

P2Rank 0.955

Structure A0A0H3GS90

Pocket Pocket 1

ColabFold model

FPocket 0.649 · Pocket 4

P2Rank 0.916 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

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 A0A0H3GS90

Chemistry

ChEMBL CHEMBL361197

Sequence

Primary amino-acid sequence viewer.

MNNSAKIALVTGGSRGLGRATVEALAQRGVNVVLTYKTRLAEANEVVTRVEALGARAIALPFSAGEIDTFDAFVSAFQGALTELGADKFDYLVNNAGNASGMGFLNATEAEFDALYRTHVKSVFFLSQKLLPLLADGGRIVNVSSGLTRIVMANRAPYAIMKSAVETLTRYMAFELGSRGITVNCVAPVAIATDFSGGVVRDNPQVAQAVANMTALGRPGLPEDIGPMIASLLSDDHRWVNAQRIEVSGGMRI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
14	251	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
138	146	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
138	146	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
158	177	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
158	177	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
87	98	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
87	98	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
6	252	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
6	252	InterPro	IPR036291	NAD(P)-binding domain superfamily
2	252	Gene3D	G3DSA:3.40.50.720	-
3	251	PANTHER	PTHR43639	OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870)
215	235	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
215	235	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
158	177	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
7	24	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
7	24	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
87	98	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
132	148	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
132	148	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
179	196	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
179	196	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR

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

0.974

Likely same site as P2Rank 1 0.8 Å 39 shared residues 95% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.955

Likely same site as FPocket 1 0.8 Å 39 shared residues 95% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.037

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #4

0.649

Likely same site as P2Rank 1 1.1 Å 37 shared residues 95% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #5

0.317

Show in viewer

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_A0A0H3GS90	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1110	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 and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1TJ PDB via homolog 320.3 Da · LogP 2.36 · TPSA 91.7 Open detail RCSB PDB

2V4 PDB via homolog Detail RCSB PDB

CUE PDB via homolog Detail RCSB PDB

GEN PDB via homolog Detail RCSB PDB

HHF 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
1TJ RCSB PDB	4KWI	Q9ZGC1	320.3 Da LogP 2.36 TPSA 91.7	✓ Ro5	Alert	`Cc1cc2c(c(c1)O)C3=C(C(=O)C2)C(=O)c4c(cccc4O)C3=O`
2V4 RCSB PDB	4OSP	K0IB23	338.3 Da LogP 1.75 TPSA 111.9	✓ Ro5	Alert	`C[C@]1(Cc2cc(c3c(c2C(=O)C1)C(=O)c4cccc(c4C3=O)O…`
CUE RCSB PDB	3QWI	O93874	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`c1cc2c(cc1O)oc-3c2C(=O)Oc4c3ccc(c4)O`
GEN RCSB PDB	4FJ1	O93874	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`c1cc(ccc1C2=COc3cc(cc(c3C2=O)O)O)O`
HHF RCSB PDB	4FJ0	O93874	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`c1ccc(cc1)C2=C(C(=O)c3ccc(cc3O2)O)O`
KMP RCSB PDB	3QWH	O93874	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`c1cc(ccc1C2=C(C(=O)c3c(cc(cc3O2)O)O)O)O`
MLH RCSB PDB	6T65	V5VHN7	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c2cc(c(cc2n(c1CN(C)C)c3ccccc3)Br)O`
PYQ RCSB PDB	1JA9	Q9HFV6	173.2 Da LogP 1.52 TPSA 20.3	✓ Ro5	✓ Clean	`c1cc2c3c(c1)CCN3C(=O)CC2`
QSO RCSB PDB	4FJ2	O93874	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(cc1)C2=COc3cc(cc(c3C2=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL361197 ChEMBL	O93874	6.16 ~691.8 nM	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccccc1`

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
ZINC1219 ZINC	1.000	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`O=c1oc2cc(O)ccc2c2oc3cc(O)ccc3c12`
ZINC1233995 ZINC	1.000	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(O)cc12`
ZINC12358883 ZINC	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccccc1`
ZINC1857742182 ZINC	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(C=Cc1ccccc1)OCc1ccccc1`
ZINC18825330 ZINC	1.000	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(O)cc2)coc2cc(O)cc(O)c12`
ZINC18847037 ZINC	1.000	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(O)c3c2=O)cc1`
ZINC3869768 ZINC	1.000	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2)oc2cc(O)cc(O)c12`
ZINC4654730 ZINC	1.000	338.3 Da LogP 1.75 TPSA 111.9	✓ Ro5	Alert	`C[C@]1(O)CC(=O)c2c(cc(O)c3c2C(=O)c2cccc(O)c2C3=…`
ZINC4803379 ZINC	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C\c1ccccc1)OCc1ccccc1`
ZINC6032158 ZINC	1.000	338.3 Da LogP 1.75 TPSA 111.9	✓ Ro5	Alert	`C[C@@]1(O)CC(=O)c2c(cc(O)c3c2C(=O)c2cccc(O)c2C3…`
ZINC6116596 ZINC	1.000	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)ccc12`
ZINC6018481 ZINC	0.875	298.3 Da LogP 3.18 TPSA 68.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(OC)cc(O)c3c2=O)cc1`
ZINC8453886 ZINC	0.849	431.3 Da LogP 4.65 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccc(C)cc2)c2cc(Br)c(O)c…`
ZINC14504998 ZINC	0.844	254.3 Da LogP 3.15 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(O)cc1)OCc1ccccc1`
ZINC39203780 ZINC	0.844	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`O=c1oc2cc(O)ccc2c2oc3ccc(O)cc3c12`
ZINC6093351 ZINC	0.824	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2)oc2cc(O)ccc12`
ZINC304562 ZINC	0.811	333.1 Da LogP 3.63 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(Br)cc2)coc2cc(O)cc(O)c12`
ZINC5731170 ZINC	0.811	288.7 Da LogP 3.52 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(Cl)cc2)coc2cc(O)cc(O)c12`
ZINC5997152 ZINC	0.811	272.2 Da LogP 3.01 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(F)cc2)coc2cc(O)cc(O)c12`
ZINC120273 ZINC	0.806	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)cc(O)c12`
ZINC2149675 ZINC	0.806	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccccc2)coc2cc(O)cc(O)c12`
ZINC57845 ZINC	0.806	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2cccc(O)c2)oc2cc(O)ccc12`
ZINC5222178 ZINC	0.800	431.3 Da LogP 4.64 TPSA 43.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(OC)cc12`
ZINC2888441 ZINC	0.794	272.7 Da LogP 4.10 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccc(Cl)cc1`
ZINC3103992 ZINC	0.794	272.7 Da LogP 4.10 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(Cl)cc1)OCc1ccccc1`
ZINC3228605 ZINC	0.794	256.3 Da LogP 3.58 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(F)cc1)OCc1ccccc1`
ZINC11865148 ZINC	0.791	282.3 Da LogP 3.48 TPSA 59.7	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(C)c3c2=O)cc1`
ZINC14811807 ZINC	0.791	298.3 Da LogP 3.18 TPSA 68.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(OC)c3c2=O)cc1`
ZINC18847044 ZINC	0.786	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1cc(O)c2c(=O)c(-c3ccc(O)cc3)coc2c1`
ZINC3869685 ZINC	0.784	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	Alert	`O=c1c(O)c(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC6092209 ZINC	0.784	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`O=c1c(-c2ccc(O)c(O)c2)coc2cc(O)cc(O)c12`
ZINC57648 ZINC	0.778	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2ccc(O)cc12`
ZINC103633384 ZINC	0.759	296.3 Da LogP 3.03 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(/C=C\C(=O)OCc1ccccc1)OCc1ccccc1`
ZINC4411156 ZINC	0.759	296.3 Da LogP 3.03 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(/C=C/C(=O)OCc1ccccc1)OCc1ccccc1`
ZINC2556384 ZINC	0.757	282.3 Da LogP 3.41 TPSA 72.8	✓ Ro5	✓ Clean	`COc1ccc2c(c1)oc1c3ccc(O)cc3oc(=O)c21`
ZINC1633891 ZINC	0.750	268.3 Da LogP 3.45 TPSA 35.5	✓ Ro5	✓ Clean	`COc1ccc(/C=C/C(=O)OCc2ccccc2)cc1`
ZINC3874317 ZINC	0.750	318.2 Da LogP 1.69 TPSA 151.6	1 viol.	Alert	`O=c1c(O)c(-c2cc(O)c(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC3881558 ZINC	0.750	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2O)oc2cc(O)cc(O)c12`
ZINC4537958 ZINC	0.750	268.3 Da LogP 3.45 TPSA 35.5	✓ Ro5	✓ Clean	`COc1ccc(/C=C\C(=O)OCc2ccccc2)cc1`
ZINC584641356 ZINC	0.750	338.2 Da LogP 3.60 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(C(F)(F)F)cc2)oc2cc(O)cc(O)c12`
ZINC6411540 ZINC	0.750	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	✓ Clean	`COc1ccc(-c2oc3cc(O)cc(O)c3c(=O)c2O)cc1`
ZINC6525249 ZINC	0.750	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(O)cc2O)coc2cc(O)cc(O)c12`
ZINC4654724 ZINC	0.738	322.3 Da LogP 2.05 TPSA 91.7	✓ Ro5	Alert	`C[C@@]1(O)CC(=O)c2c(ccc3c2C(=O)c2cccc(O)c2C3=O)…`
ZINC4654725 ZINC	0.738	322.3 Da LogP 2.05 TPSA 91.7	✓ Ro5	Alert	`C[C@]1(O)CC(=O)c2c(ccc3c2C(=O)c2cccc(O)c2C3=O)C1`
ZINC1678812 ZINC	0.737	288.7 Da LogP 3.52 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(Cl)cc2)oc2cc(O)ccc12`
ZINC6068882 ZINC	0.737	252.3 Da LogP 3.47 TPSA 50.4	✓ Ro5	✓ Clean	`Cc1c(-c2ccccc2)oc2cc(O)ccc2c1=O`
ZINC704414 ZINC	0.736	374.2 Da LogP 4.58 TPSA 51.5	✓ Ro5	✓ Clean	`CCOC(=O)c1c(C)n(-c2ccccc2)c2cc(Br)c(O)cc12`
ZINC2561259 ZINC	0.733	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	✓ Clean	`COc1cc(-c2coc3cc(O)cc(O)c3c2=O)ccc1O`
ZINC6484607 ZINC	0.733	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(O)c3c2=O)cc1O`
ZINC6556076 ZINC	0.733	314.3 Da LogP 2.89 TPSA 89.1	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(O)c3c2=O)cc1OC`

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.