Protein profile

KP13_01236

Bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase

Genome: KpKP13

Gene: AHE46699.1 cpdB Structure source: Experimental + ColabFold UniProt A6THC4

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Amino acids 647

Annotations 7

Features 43

PDB binders 9

Druggability 0.579

Overview

Basic information about this protein and its source genome.

Accession: KP13_01236
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE46699.1 cpdB
Status: annotated
Amino acids: 647
Structure source: Experimental + ColabFold

GO:0009166 The chemical reactions and pathways resulting in the breakdown of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates). GO:0009117 The chemical reactions and pathways involving a nucleotide, a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic nucleotides (nucleoside cyclic phosphates). GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0008663 Catalysis of the reaction: nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate. GO:0046872 Binding to a metal ion. GO:0016788 Catalysis of the hydrolysis of any ester bond.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 26.778
Human E-value: 3.01e-08
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 62.366
DEG E-value: 0.0
Localization: Periplasmic
ColabFold pLDDT: 93.96

Selected Druggability evidence

PDB experimental structure

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.579

Structure 3JYF

Pocket Pocket 1

P2Rank 0.434

Structure 3JYF

Pocket Pocket 1

ColabFold model

FPocket 0.975 · Pocket 25

P2Rank 0.994 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 145 / 4744 genomes with a hit

Normalized 0.031

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0009166 The chemical reactions and pathways resulting in the breakdown of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates).
GO:0009117 The chemical reactions and pathways involving a nucleotide, a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic nucleotides (nucleoside cyclic phosphates).
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0008663 Catalysis of the reaction: nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate.
GO:0046872 Binding to a metal ion.
GO:0016788 Catalysis of the hydrolysis of any ester bond.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
1	19	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
20	647	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
4	14	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
19	353	SUPERFAMILY	SSF56300	Metallo-dependent phosphatases
19	353	InterPro	IPR029052	Metallo-dependent phosphatase-like
22	647	NCBIfam	TIGR01390	2',3'-cyclic-nucleotide 2'-phosphodiesterase
22	647	InterPro	IPR006294	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
363	594	FunFam	G3DSA:3.90.780.10:FF:000002	Bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
355	597	SUPERFAMILY	SSF55816	5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain
355	597	InterPro	IPR036907	5'-Nucleotidase, C-terminal domain superfamily
14	595	PANTHER	PTHR11575	5'-NUCLEOTIDASE-RELATED
14	595	InterPro	IPR006179	5'-Nucleotidase/apyrase
356	550	Pfam	PF02872	5'-nucleotidase, C-terminal domain
356	550	InterPro	IPR008334	5'-Nucleotidase, C-terminal
1	19	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
365	594	Gene3D	G3DSA:3.90.780.10	-
365	594	InterPro	IPR036907	5'-Nucleotidase, C-terminal domain superfamily
24	259	Pfam	PF00149	Calcineurin-like phosphoesterase
24	259	InterPro	IPR004843	Calcineurin-like phosphoesterase domain, ApaH type
530	549	PRINTS	PR01607	Apyrase family signature
530	549	InterPro	IPR006179	5'-Nucleotidase/apyrase
243	266	PRINTS	PR01607	Apyrase family signature
243	266	InterPro	IPR006179	5'-Nucleotidase/apyrase
283	303	PRINTS	PR01607	Apyrase family signature
283	303	InterPro	IPR006179	5'-Nucleotidase/apyrase
22	40	PRINTS	PR01607	Apyrase family signature
22	40	InterPro	IPR006179	5'-Nucleotidase/apyrase
215	232	PRINTS	PR01607	Apyrase family signature
215	232	InterPro	IPR006179	5'-Nucleotidase/apyrase
428	451	PRINTS	PR01607	Apyrase family signature
428	451	InterPro	IPR006179	5'-Nucleotidase/apyrase
1	19	Phobius	SIGNAL_PEPTIDE	Signal peptide region
24	36	ProSitePatterns	PS00785	5'-nucleotidase signature 1.
24	36	InterPro	IPR006146	5'-Nucleotidase, conserved site
109	120	ProSitePatterns	PS00786	5'-nucleotidase signature 2.
109	120	InterPro	IPR006146	5'-Nucleotidase, conserved site
15	19	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
16	354	Gene3D	G3DSA:3.60.21.10	-
16	354	InterPro	IPR029052	Metallo-dependent phosphatase-like
16	354	FunFam	G3DSA:3.60.21.10:FF:000037	Bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
24	321	CDD	cd07410	MPP_CpdB_N
24	321	InterPro	IPR041827	CpdB, N-terminal metallophosphatase domain

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

1 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 3JYF	X-ray	20.00 Å	-	—	PDBe RCSB PDBj File	Viewing
ColabFold KP13_01236	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
27				0.506
1				0.273
4				0.222

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	15.55	0.756
2	5.44	0.259
3	4.95	0.224
4	1.46	0.02

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
25				0.975

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	57.91	0.986
2	3.33	0.118
3	1.24	0.012
4	0.63	0.001

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.

59 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
TAM	3JYF Open crystal	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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
3D1	4Q7F	Q2G1L5	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO)O)N`
A12	1HPU	P07024	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ADN	1HO5	P07024	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
AKG	3QFK	Q2G1L5	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
MLT	5EQV	A0A5P8YBY3	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
MTN	4WWL	P07024	264.4 Da LogP 1.82 TPSA 57.3	✓ Ro5	✓ Clean	`CC1(C=C(C(N1[O])(C)C)CSS(=O)(=O)C)C`
THM	2Z1A	Q5SIP1	242.2 Da LogP -1.51 TPSA 104.6	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)O`
WO4	2USH	P07024	247.8 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][W](=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
ZINC2047403	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC2047673	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC2169830	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC3201876	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC3201878	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC3830178	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3830179	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3978047	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC3978048	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC3978049	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC4048240	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC8580514	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC895113	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC896706	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC970363	1.000	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC4188096	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188103	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4188112	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188116	0.974	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4804742	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)…`
ZINC4804743	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)[…`
ZINC4804744	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O…`
ZINC4804745	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O)…`
ZINC4809089	0.833	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](S)[C@H]1O`
ZINC4809090	0.833	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](S)[C@H]1O`
ZINC4809091	0.833	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](S)[C@@H]1O`
ZINC4809092	0.833	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](S)[C@@H]…`
ZINC13470207	0.814	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](N)[C@H]1O`
ZINC14418140	0.814	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](N)[C@H]1O`
ZINC79682926	0.814	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](N)[C@@H]1O`
ZINC16928956	0.810	258.3 Da LogP -0.14 TPSA 87.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=S`
ZINC5085194	0.805	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CF)O2)c(=O)[nH]c1=O`
ZINC5085195	0.805	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CF)O2)c(=O)[nH]c1=O`
ZINC5085196	0.805	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CF)O2)c(=O)[nH]c1=O`
ZINC5085197	0.805	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CF)O2)c(=O)[nH]c1=O`
ZINC12618466	0.795	269.2 Da LogP -1.00 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](F)[C@@H]1O`
ZINC11677083	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](F)[C@@H](CO)O2)c(=O)[nH]c1…`
ZINC11677088	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](F)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC17187169	0.791	241.2 Da LogP -1.55 TPSA 110.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](N)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC1725270	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](F)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC2130970	0.791	241.2 Da LogP -1.55 TPSA 110.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](N)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC25054	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](F)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC3785451	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](F)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC4537463	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](F)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC4537467	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](F)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC56790	0.791	244.2 Da LogP -0.54 TPSA 84.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](F)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC5833725	0.791	255.3 Da LogP -1.29 TPSA 96.4	✓ Ro5	✓ Clean	`CN[C@H]1C[C@@H](n2cc(C)c(=O)[nH]c2=O)O[C@H]1CO`
ZINC5833727	0.791	255.3 Da LogP -1.29 TPSA 96.4	✓ Ro5	✓ Clean	`CN[C@H]1C[C@H](n2cc(C)c(=O)[nH]c2=O)O[C@H]1CO`
ZINC5833731	0.791	255.3 Da LogP -1.29 TPSA 96.4	✓ Ro5	✓ Clean	`CN[C@@H]1C[C@@H](n2cc(C)c(=O)[nH]c2=O)O[C@H]1CO`
ZINC6667024	0.791	256.3 Da LogP -0.86 TPSA 93.5	✓ Ro5	✓ Clean	`COC[C@H]1O[C@@H](n2cc(C)c(=O)[nH]c2=O)C[C@@H]1O`

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.