Protein target profile

KP13_03796

dTDP-4-dehydrorhamnose reductase in cps region

Genome: KpKP13 Gene: AHE43666.1 rmlD 3D evidence: Experimental + ColabFold model UniProt C9K1F1

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Length 296

Pocket druggability 0.895

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 5 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 0.90, P2Rank 0.92). Use the 3D pocket comparison to verify whether they identify the same site. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Strong predicted binding pocket FPocket selected-pocket score 0.90. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.92. 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 (%): 34.188 Lower values reduce human off-target concern.
Human E-value: 7.45e-15
Gut microbiome similarity: 1.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 61.905 Higher values support similarity to known essential genes.
DEG E-value: 1.8e-132 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 98.35 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

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 0.895

Structure 8CTR

Pocket Pocket 1

P2Rank 0.917

Structure 8CTR

Pocket Pocket 1

ColabFold model

FPocket 0.262 · Pocket 7

P2Rank 0.935 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 53 / 4744 genomes with a hit

Prevalence 1.1%

Cross-references

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

Sequence

Primary amino-acid sequence viewer.

MKILLIGKNGQVGWELQRSLSTLGDVVAVDYFDKLLCGDLTNLEGIAQTVRTVRPDVVVNAAAHTAVDKAESERELSDLLNDKGVAVLAAESAKLGALMVHYSTDYVFDGAGSHYRREDEATGPLNVYGETKRAGELALEQGNPRHLIFRTSWVYATRGANFAKTMLRLAGEKETLSIIDDQHGAPTGAELLADCTATAIRETLRNPALAGTYHLVASGETSWCDYARYVFEVARAHGAELAVQEVKGIPTTAYPTPAKRPLNSRLSNEKFQQAFGVTLPDWRQGVARVVTEVLGK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1.1.1.133

Gene Ontology (GO)

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0008831 Catalysis of the reaction: dTDP-6-deoxy-L-mannose + NADP+ = dTDP-4-dehydro-6-deoxy-L-mannose + H+ + NADPH.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0019305 The chemical reactions and pathways resulting in the formation of dTDP-rhamnose, a substance composed of rhamnose in glycosidic linkage with deoxyribosylthymine diphosphate.
GO:0009243 The chemical reactions and pathways resulting in the formation of the O side chain of a lipopolysaccharide, which determines the antigenic specificity of the organism. It is made up of about 50 repeating units of a branched tetrasaccharide.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

11 records

Show feature table

Start	End	DB	Term	Name
3	280	Gene3D	G3DSA:3.40.50.720	-
162	287	Gene3D	G3DSA:3.90.25.10	-
2	293	PANTHER	PTHR10491	DTDP-4-DEHYDRORHAMNOSE REDUCTASE
2	293	InterPro	IPR005913	dTDP-4-dehydrorhamnose reductase family
2	292	NCBIfam	TIGR01214	dTDP-4-dehydrorhamnose reductase
2	292	InterPro	IPR005913	dTDP-4-dehydrorhamnose reductase family
1	293	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1	293	InterPro	IPR036291	NAD(P)-binding domain superfamily
1	293	Pfam	PF04321	RmlD substrate binding domain
1	293	InterPro	IPR029903	RmlD-like substrate binding domain
2	287	CDD	cd05254	dTDP_HR_like_SDR_e

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

0.895

Likely same site as P2Rank 1 6.8 Å 23 shared residues 72% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #9

0.47

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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

0.917

Likely same site as FPocket 1 6.8 Å 23 shared residues 72% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.099

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Surrounding area

Site 3 P2Rank #3

0.029

Likely same site as FPocket 1 7.6 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.016

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Surrounding area

Site 5 P2Rank #5

0.002

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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

0.935

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Surrounding area

Site 2 P2Rank #2

0.091

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Surrounding area

Site 3 P2Rank #3

0.009

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Surrounding area

All structural evidence 1 experimental · 1 predicted

Structural evidence

1 + 1

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
PDB 8CTR	X-ray	1.65 Å	A,B,C,D	100.0% 1-296	PDBe RCSB PDBj File	Viewing
ColabFold KP13_03796	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.

55 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

STL PDB via homolog 228.2 Da · LogP 2.97 · TPSA 60.7 Open detail RCSB PDB

TRH PDB via homolog Detail RCSB PDB

TXP PDB via homolog Detail RCSB PDB

DWT ChEMBL via homolog · pchembl 7.28 (~52.5 nM) Detail ChEMBL

CHEMBL375328 ChEMBL via homolog · pchembl 6.05 (~891.3 nM) Detail ChEMBL

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
STL RCSB PDB	2YDX	Q9NZL9	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`c1cc(ccc1\C=C\c2cc(cc(c2)O)O)O`
TRH RCSB PDB	1KC3	P26392	548.3 Da LogP -2.43 TPSA 256.5	3 viol.	✓ Clean	`C[C@H]1[C@@H]([C@H]([C@H]([C@H](O1)O[P@](=O)(O)…`
TXP RCSB PDB	2YDX	Q9NZL9	747.4 Da LogP -3.18 TPSA 364.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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
DWT ChEMBL	Q9NZL9	7.28 ~52.5 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
CHEMBL375328 ChEMBL	P9WH09	6.05 ~891.3 nM	320.3 Da LogP 3.68 TPSA 90.9	✓ Ro5	Alert	`O=c1cc2oc3cc(O)c(O)cc3c(-c3ccccc3)c-2cc1O`

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
ZINC12353732 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2cc(O)cc(O)c2)cc1`
ZINC1857524289 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2cc(O)cc(O)c2)cc1`
ZINC3860685 ZINC	1.000	320.3 Da LogP 3.68 TPSA 90.9	✓ Ro5	Alert	`O=c1cc2oc3cc(O)c(O)cc3c(-c3ccccc3)c-2cc1O`
ZINC6787 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2cc(O)cc(O)c2)cc1`
ZINC100037549 ZINC	0.775	336.3 Da LogP 3.39 TPSA 111.1	✓ Ro5	Alert	`O=c1cc2oc3cc(O)c(O)cc3c(-c3ccccc3O)c-2cc1O`
ZINC13507072 ZINC	0.742	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC33979251 ZINC	0.742	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC12503053 ZINC	0.738	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC33979243 ZINC	0.738	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC33979244 ZINC	0.738	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O)…`
ZINC33979245 ZINC	0.738	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=…`
ZINC33979246 ZINC	0.738	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC8215882 ZINC	0.738	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC13319959 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2ccc(O)cc2)cc1`
ZINC1510311 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2ccc(O)cc2)cc1`
ZINC1875408805 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2ccc(O)cc2)cc1`
ZINC4881528 ZINC	0.733	321.3 Da LogP 3.08 TPSA 103.8	✓ Ro5	Alert	`O=c1cc2oc3cc(O)c(O)cc3c(-c3cccnc3)c-2cc1O`
ZINC34544488 ZINC	0.720	230.2 Da LogP 3.41 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2cc(O)cc(F)c2)cc1`
ZINC4822213 ZINC	0.711	363.4 Da LogP 3.75 TPSA 94.1	✓ Ro5	Alert	`CN(C)c1ccc(-c2c3cc(O)c(=O)cc-3oc3cc(O)c(O)cc23)…`
ZINC2561223 ZINC	0.708	291.1 Da LogP 4.03 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C/c2ccc(Br)cc2)c1`
ZINC49588452 ZINC	0.708	246.7 Da LogP 3.92 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C/c2ccc(Cl)cc2)c1`
ZINC71622042 ZINC	0.708	246.7 Da LogP 3.92 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C\c2ccc(Cl)cc2)c1`
ZINC901115 ZINC	0.696	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C/c2ccccc2)c1`
ZINC9147134 ZINC	0.696	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1cc(O)cc(/C=C\c2ccccc2)c1`
ZINC32669136 ZINC	0.689	415.2 Da LogP 4.15 TPSA 111.1	✓ Ro5	Alert	`O=c1cc2oc3cc(O)c(O)cc3c(-c3ccc(O)c(Br)c3)c-2cc1O`
ZINC13523519 ZINC	0.672	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532628 ZINC	0.672	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC1678872 ZINC	0.672	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=O…`
ZINC2047010 ZINC	0.672	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870253 ZINC	0.672	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870254 ZINC	0.672	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O)…`
ZINC6523446 ZINC	0.672	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC13340993 ZINC	0.667	242.3 Da LogP 3.28 TPSA 49.7	✓ Ro5	✓ Clean	`COc1cc(O)cc(/C=C\c2ccc(O)cc2)c1`
ZINC14505445 ZINC	0.667	244.2 Da LogP 2.68 TPSA 80.9	✓ Ro5	Alert	`Oc1ccc(/C=C/c2cc(O)c(O)c(O)c2)cc1`
ZINC2053558586 ZINC	0.667	242.3 Da LogP 3.28 TPSA 49.7	✓ Ro5	✓ Clean	`COc1cc(O)cc(C=Cc2ccc(O)cc2)c1`
ZINC4894119 ZINC	0.667	364.4 Da LogP 4.08 TPSA 100.1	✓ Ro5	Alert	`CCOc1ccc(-c2c3cc(O)c(=O)cc-3oc3cc(O)c(O)cc23)cc1`
ZINC6483567 ZINC	0.667	242.3 Da LogP 3.28 TPSA 49.7	✓ Ro5	✓ Clean	`COc1cc(O)cc(/C=C/c2ccc(O)cc2)c1`
ZINC71614385 ZINC	0.667	244.2 Da LogP 2.68 TPSA 80.9	✓ Ro5	Alert	`Oc1ccc(/C=C\c2cc(O)c(O)c(O)c2)cc1`
ZINC1857776228 ZINC	0.654	242.3 Da LogP 3.28 TPSA 49.7	✓ Ro5	✓ Clean	`COc1ccc(C=Cc2cc(O)cc(O)c2)cc1`
ZINC3978779 ZINC	0.654	242.3 Da LogP 3.28 TPSA 49.7	✓ Ro5	✓ Clean	`COc1ccc(/C=C/c2cc(O)cc(O)c2)cc1`
ZINC3871401 ZINC	0.653	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871402 ZINC	0.653	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3871403 ZINC	0.653	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3871404 ZINC	0.653	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC4096223 ZINC	0.653	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC238950253 ZINC	0.652	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950256 ZINC	0.652	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950259 ZINC	0.652	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950261 ZINC	0.652	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC17107637 ZINC	0.651	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(N)(N)=O)O2)c(…`

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.