Protein target profile

KP13_05459

L-Ala-D/L-Glu epimerase

Genome: KpKP13 Gene: AHE44951.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GNH7

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Length 342

Pocket druggability 0.931

Direct ligand evidence 0 54 total records

Functional annotation 1 EC 3 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 0.93, P2Rank 0.86). 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. Strong predicted binding pocket FPocket selected-pocket score 0.93. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.86. 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: No hit
Gut microbiome similarity: 2.0% 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: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.27 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 0.931

Structure A0A0H3GNH7

Pocket Pocket 1

P2Rank 0.865

Structure A0A0H3GNH7

Pocket Pocket 1

ColabFold model

FPocket 0.887 · Pocket 1

P2Rank 0.684 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 93 / 4744 genomes with a hit

Prevalence 2.0%

Cross-references

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

Sequence

UniProt A0A0H3GNH7

Sequence

Primary amino-acid sequence viewer.

MYDIRQLHGKPYLTFTREDKGMRNVRVYEEAWPLHTPFVIARGSRSEAKVVVVELEEDGVKGVGECTPYPRYGESIASVMAQVMAIGEQLEAGLTREQLQRLLPAGAARNAIDCALWDLQARREGKTLAQLLGVALPNRVITAQTVVIGTPDQMAASAAALWQAGAQLLKVKLDDRLISERLIAIRQAAPEATLIVDANESWHSEGLAARCQLLADLGVAMLEQPLPADDDSALENFVHPLPICADESCHTRESLPRLRGRYEMINIKLDKTGGLTEALALAGEAERQGFERMLGCMLCTSRGIAAALPLAPLARFADLDGPTWLAVDVEPALRFSTGVLHL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

5.1.1.-

Gene Ontology (GO)

GO:0016855 Catalysis of a reaction that alters the configuration of one or more chiral centers in an amino acid.
GO:0009063 The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
20	125	Gene3D	G3DSA:3.30.390.10	-
20	125	InterPro	IPR029017	Enolase-like, N-terminal
24	325	CDD	cd03319	L-Ala-DL-Glu_epimerase
24	325	InterPro	IPR034603	Dipeptide epimerase
23	133	SUPERFAMILY	SSF54826	Enolase N-terminal domain-like
23	133	InterPro	IPR029017	Enolase-like, N-terminal
22	124	FunFam	G3DSA:3.30.390.10:FF:000010	Dipeptide epimerase
151	244	SMART	SM00922	MR_MLE_2
151	244	InterPro	IPR013342	Mandelate racemase/muconate lactonizing enzyme, C-terminal
137	339	SUPERFAMILY	SSF51604	Enolase C-terminal domain-like
137	339	InterPro	IPR036849	Enolase-like, C-terminal domain superfamily
31	342	SFLD	SFLDF00010	dipeptide epimerase
31	342	InterPro	IPR034603	Dipeptide epimerase
31	342	SFLD	SFLDS00001	Enolase
194	225	ProSitePatterns	PS00909	Mandelate racemase / muconate lactonizing enzyme family signature 2.
194	225	InterPro	IPR018110	Mandelate racemase/muconate lactonizing enzyme, conserved site
40	338	PANTHER	PTHR48080	D-GALACTONATE DEHYDRATASE-RELATED
40	338	InterPro	IPR034593	D-galactonate dehydratase DgoD-like
154	340	Pfam	PF13378	Enolase C-terminal domain-like
154	340	InterPro	IPR029065	Enolase C-terminal domain-like
136	342	Gene3D	G3DSA:3.20.20.120	-
136	342	InterPro	IPR036849	Enolase-like, C-terminal domain superfamily
23	133	Pfam	PF02746	Mandelate racemase / muconate lactonizing enzyme, N-terminal domain
23	133	InterPro	IPR013341	Mandelate racemase/muconate lactonizing enzyme, N-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 · FPocket

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

Site 1 FPocket #1

0.931

Likely same site as P2Rank 1 2.4 Å 17 shared residues 89% 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

0.865

Likely same site as FPocket 1 2.4 Å 17 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.185

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Surrounding area

Site 3 P2Rank #3

0.052

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Surrounding area

Residue sets

UniProt: Active site:151-151 Proton acceptor; specific for (R)-substrate epimerization

UniProt: Active site:247-247 Proton acceptor; specific for (S)-substrate epimerization

UniProt: Binding site:176-176

UniProt: Binding site:202-202

UniProt: Binding site:225-225

Binding pockets · FPocket

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

Site 1 FPocket #1

0.887

Likely same site as P2Rank 1 2.8 Å 19 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #12

0.375

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Surrounding area

Site 3 FPocket #23

0.338

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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

0.684

Likely same site as FPocket 1 2.8 Å 19 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.157

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Surrounding area

Site 3 P2Rank #3

0.11

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Surrounding area

Site 4 P2Rank #4

0.002

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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_A0A0H3GNH7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_05459	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

FUM PDB via homolog 116.1 Da · LogP -0.29 · TPSA 74.6 Open detail RCSB PDB

NSK PDB via homolog Detail RCSB PDB

SUG PDB via homolog Detail RCSB PDB

TAR PDB via homolog Detail RCSB PDB

ZINC1866114950 ZINC proposed compound · Tanimoto 0.844 Detail ZINC

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
FUM RCSB PDB	3R11	B0TZW0	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
NSK RCSB PDB	2P8B	Q81IL5	246.3 Da LogP -0.45 TPSA 129.7	✓ Ro5	✓ Clean	`C(CCN)C[C@@H](C(=O)O)NC(=O)CCC(=O)O`
SUG RCSB PDB	2P8C	Q81IL5	274.3 Da LogP -1.32 TPSA 165.6	1 viol.	✓ Clean	`C(C[C@@H](C(=O)O)NC(=O)CCC(=O)O)CNC(=N)N`
TAR RCSB PDB	3R0U	B0TZW0	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@@H](C(=O)O)O)(C(=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
ZINC1866114950 ZINC	0.844	260.3 Da LogP -0.06 TPSA 129.7	✓ Ro5	✓ Clean	`NCCCC[C@H](NC(=O)CCCC(=O)O)C(=O)O`
ZINC1530138 ZINC	0.806	217.3 Da LogP -0.97 TPSA 118.4	✓ Ro5	✓ Clean	`NCCCC[C@H](NC(=O)CCN)C(=O)O`
ZINC403598 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC403599 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC15261332 ZINC	0.744	303.3 Da LogP -1.99 TPSA 191.6	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC39351856 ZINC	0.741	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC1576211 ZINC	0.730	231.3 Da LogP -2.22 TPSA 154.3	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CN)C(=O)O`
ZINC116981435 ZINC	0.706	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC116981437 ZINC	0.706	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@@H](NC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC116981440 ZINC	0.706	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@H](NC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC40860752 ZINC	0.706	319.3 Da LogP -0.81 TPSA 179.0	1 viol.	✓ Clean	`NCCCC[C@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1847640 ZINC	0.703	216.2 Da LogP -1.16 TPSA 128.3	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC2169795 ZINC	0.703	216.2 Da LogP -1.16 TPSA 128.3	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CCCNC(=N)N)C(=O)O`
ZINC1722125 ZINC	0.694	217.2 Da LogP -1.63 TPSA 154.3	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(N)=O)C(=O)O`
ZINC4537126 ZINC	0.694	217.2 Da LogP -1.63 TPSA 154.3	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](NC(N)=O)C(=O)O`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC32333 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC34319489 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC34319490 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC1529261 ZINC	0.684	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529262 ZINC	0.684	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@@H](N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529939 ZINC	0.684	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N[C@@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1529940 ZINC	0.684	304.3 Da LogP -1.39 TPSA 185.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC1530510 ZINC	0.684	246.3 Da LogP -1.23 TPSA 148.5	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NCCC(=O)O)C(=O)O`
ZINC1530296 ZINC	0.677	247.2 Da LogP -0.71 TPSA 141.0	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC2512061 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@H](N)C(=O)O)ccc2O)…`
ZINC6091882 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O…`
ZINC6091894 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O)…`
ZINC6783254 ZINC	0.676	231.2 Da LogP 0.61 TPSA 103.7	✓ Ro5	✓ Clean	`CCCC[C@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC6783285 ZINC	0.676	231.2 Da LogP 0.61 TPSA 103.7	✓ Ro5	✓ Clean	`CCCC[C@@H](NC(=O)CCC(=O)O)C(=O)O`
ZINC113625226 ZINC	0.676	272.4 Da LogP 2.05 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)N[C@@H](CCCCN)C(=O)O`
ZINC28539131 ZINC	0.676	328.5 Da LogP 3.61 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)N[C@@H](CCCCN)C(=O)O`
ZINC14982778 ZINC	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC14982780 ZINC	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC2575618 ZINC	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`

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.