Protein profile

KP13_02775

Cystathionine beta-lyase metC

Genome: KpKP13

Gene: AHE42656.1 Structure source: Experimental + ColabFold UniProt A0A0H3GVN6

Export view

Amino acids 395

Annotations 10

Features 20

PDB binders 17

Druggability 0.673

Overview

Basic information about this protein and its source genome.

Accession: KP13_02775
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42656.1
Status: annotated
Amino acids: 395
Structure source: Experimental + ColabFold

4.4.1.13

GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0004121 OBSOLETE. Catalysis of the reaction: cystathionine + H2O = L-homocysteine + NH3 + pyruvate. GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0019346 The interconversion of homocysteine and cysteine via cystathionine. In contrast with enteric bacteria and mammals, Saccharomyces cerevisiae has two transsulfuration pathways employing two separate sets of enzymes. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 31.902
Human E-value: 4.89e-47
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 65.296
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 97.13

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 0.673

Structure 8DUY

Pocket Pocket 2

P2Rank 0.637

Structure 8DUY

Pocket Pocket 1

ColabFold model

FPocket 0.197 · Pocket 16

P2Rank 0.526 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 132 / 4744 genomes with a hit

Normalized 0.028

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

4.4.1.13

Gene Ontology (GO)

GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
GO:0004121 OBSOLETE. Catalysis of the reaction: cystathionine + H2O = L-homocysteine + NH3 + pyruvate.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0019346 The interconversion of homocysteine and cysteine via cystathionine. In contrast with enteric bacteria and mammals, Saccharomyces cerevisiae has two transsulfuration pathways employing two separate sets of enzymes.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0047804 Catalysis of the reaction: S-substituted L-cysteine + H2O = a thiol + NH4+ + pyruvate.
GO:0019450 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-cysteine into other compounds, including pyruvate.
GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
1	258	Gene3D	G3DSA:3.40.640.10	-
1	258	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
8	394	NCBIfam	TIGR01324	cystathionine beta-lyase
8	394	InterPro	IPR006233	Cystathionine beta-lyase, bacterial
202	216	ProSitePatterns	PS00868	Cys/Met metabolism enzymes pyridoxal-phosphate attachment site.
202	216	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
259	395	FunFam	G3DSA:3.90.1150.10:FF:000058	Cystathionine beta-lyase
1	258	FunFam	G3DSA:3.40.640.10:FF:000062	Cystathionine beta-lyase
24	393	SUPERFAMILY	SSF53383	PLP-dependent transferases
24	393	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
22	392	CDD	cd00614	CGS_like
22	392	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
1	395	PIRSF	PIRSF001434	CGS
1	395	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
3	394	PANTHER	PTHR43500	CYSTATHIONINE BETA-LYASE-RELATED
3	394	InterPro	IPR006233	Cystathionine beta-lyase, bacterial
7	391	Pfam	PF01053	Cys/Met metabolism PLP-dependent enzyme
7	391	InterPro	IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
259	395	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
259	395	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small 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...

Legend High Medium Low

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 8DUY	X-ray	1.90 Å	A,B,C,D	100.0% 1-395	PDBe RCSB PDBj File	Viewing
ColabFold KP13_02775	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
3				0.942
4				0.853
2				0.588
5				0.264

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	31.37	0.939
2	30.07	0.933
3	29.81	0.933
4	27.13	0.919
5	27.06	0.918

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	7.35	0.384
2	4.64	0.202
3	2.48	0.068

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.

71 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.

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
2LM	3AEL	Q86D28	378.3 Da LogP 1.48 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C(\CCSC)/C(=O)O)O`
3LM	3AEO	Q86D28	378.3 Da LogP 1.13 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN/C(=C/CSC)/C(=O)O)O`
4LM	3AEP	Q86D28	330.2 Da LogP 1.11 TPSA 149.5	✓ Ro5	✓ Clean	`C/C=C(\C(=O)O)/N=C/c1c(cnc(c1O)C)COP(=O)(O)O`
AA5	3AEJ	Q86D28	378.3 Da LogP 1.33 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C=N[C@@H](CCSC)C(=O)O)O`
BLP	2GQN	P06721	469.3 Da LogP 0.16 TPSA 213.2	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNNC(=O)CNC(=O)c2ccccc…`
ECX	3JW9	Q84AR1	149.2 Da LogP 0.15 TPSA 63.3	✓ Ro5	✓ Clean	`CCSC[C@@H](C(=O)O)N`
IN5	4ITX	P06721	356.2 Da LogP 0.32 TPSA 169.4	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](C)P(=O)(O)O)O`
LCS	4OMA	Q84AR1	331.2 Da LogP -0.29 TPSA 150.6	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C/2\CONC2=O)O`
MEE	3AEP	Q86D28	48.1 Da LogP 0.55 TPSA 0.0	✓ Ro5	✓ Clean	`CS`
MPJ	3JWA	Q84AR1	169.2 Da LogP 0.49 TPSA 63.3	✓ Ro5	✓ Clean	`CSCC[C@H](N)[P@H](=O)O`
NLE	5M3Z	A0A0A5P8W7	131.2 Da LogP 0.59 TPSA 63.3	✓ Ro5	✓ Clean	`CCCC[C@@H](C(=O)O)N`
P3F	2FQ6	P06721	490.3 Da LogP 1.60 TPSA 170.4	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\NC(=O)CNC(=O)c2cc…`
PLG	4HF8	Q84AR1	306.2 Da LogP -0.12 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNCC(=O)O)O`
PPG	1CL2	P06721	389.3 Da LogP 0.22 TPSA 184.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C(\C=C\OCCN)/C(=O)…`
PPJ	1E5E	A2FEV4	362.3 Da LogP 0.35 TPSA 169.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\[C@@H](C[C@H](C)O…`
PY6	5M3Z	A0A0A5P8W7	362.3 Da LogP 1.44 TPSA 149.2	✓ Ro5	✓ Clean	`CCCC[C@@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O`
PZP	3MKJ	Q84AR1	246.2 Da LogP 0.70 TPSA 123.7	✓ Ro5	✓ Clean	`[H]/N=C/c1c(cnc(c1O)C)COP(=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
CHEMBL219268	P06721	7.10	261.2 Da LogP 0.43 TPSA 84.2	✓ Ro5	✓ Clean	`NNC(=O)CNC(=O)c1ccccc1C(F)(F)F`
CHEMBL218090	P06721	6.55	285.2 Da LogP 3.67 TPSA 29.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)C(C(F)(F)F)C(F)(F)F`
CHEMBL220764	P06721	6.28	498.2 Da LogP 4.83 TPSA 145.2	✓ Ro5	✓ Clean	`O=C(OCc1ccccc1Br)c1cc([N+](=O)[O-])cc2c1-c1ccc(…`
CHEMBL221848	P06721	6.19	277.2 Da LogP -0.17 TPSA 93.4	✓ Ro5	✓ Clean	`COc1c(F)cc(C(=O)NCC(=O)NN)c(F)c1F`

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
ZINC2035155	0.826	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](N)C(=O)O`
ZINC22148777	0.703	247.2 Da LogP 1.52 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)c1ccccc1C(F)(F)F`
ZINC2590069	0.694	322.3 Da LogP 4.28 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@H](Nc1ccccc1C)C(F)(F)F`
ZINC2590070	0.694	322.3 Da LogP 4.28 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@@H](Nc1ccccc1C)C(F)(F)F`
ZINC1532514	0.681	247.1 Da LogP 0.52 TPSA 117.0	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C=O)c1O`
ZINC3138368	0.676	299.2 Da LogP 3.98 TPSA 29.1	✓ Ro5	✓ Clean	`Cc1cccc(C)c1NC(=O)C(C(F)(F)F)C(F)(F)F`
ZINC3188764	0.676	339.2 Da LogP 4.38 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1C(F)(F)F)C(C(F)(F)F)C(F)(F)F`
ZINC2962475	0.667	404.3 Da LogP 3.88 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(NCCNC(=O)c1ccccc1C(F)(F)F)c1ccccc1C(F)(F)F`
ZINC2185058	0.657	397.1 Da LogP 3.97 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1I)C(C(F)(F)F)C(F)(F)F`
ZINC3188827	0.657	350.1 Da LogP 4.13 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1Br)C(C(F)(F)F)C(F)(F)F`
ZINC2114966	0.643	332.2 Da LogP 0.99 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(/C=N/CCCC(=O)O)c1O`
ZINC19261983	0.641	232.2 Da LogP 1.39 TPSA 55.1	✓ Ro5	✓ Clean	`NCCNC(=O)c1ccccc1C(F)(F)F`
ZINC5978748	0.641	231.2 Da LogP 2.85 TPSA 29.1	✓ Ro5	✓ Clean	`CCCNC(=O)c1ccccc1C(F)(F)F`
ZINC1674993	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSCCSCC[C@H](N)C(=O)O)C(=O)O`
ZINC1674994	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSCCSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1674996	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCSCCSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC100177544	0.639	385.3 Da LogP 3.67 TPSA 145.2	✓ Ro5	✓ Clean	`CCCCOC(=O)c1cc([N+](=O)[O-])cc2c1-c1ccc([N+](=O…`
ZINC2317717	0.639	315.2 Da LogP 3.06 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1NC(=O)C(C(F)(F)F)C(F)(F)F`
ZINC4837861	0.632	343.3 Da LogP 2.50 TPSA 145.2	✓ Ro5	✓ Clean	`COC(=O)c1cc([N+](=O)[O-])cc2c1-c1ccc([N+](=O)[O…`
ZINC57160064	0.632	271.2 Da LogP 3.00 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(NCC(F)(F)F)c1ccccc1C(F)(F)F`
ZINC103767685	0.629	399.4 Da LogP 3.91 TPSA 145.2	✓ Ro5	✓ Clean	`CC(C)CCOC(=O)c1cc([N+](=O)[O-])cc2c1-c1ccc([N+]…`
ZINC25436796	0.628	337.3 Da LogP 3.18 TPSA 55.4	✓ Ro5	✓ Clean	`O=C(CNC(=O)c1ccccc1C(F)(F)F)OCc1ccccc1`
ZINC9455654	0.622	350.3 Da LogP 3.64 TPSA 58.2	✓ Ro5	✓ Clean	`CCc1ccccc1NC(=O)CNC(=O)c1ccccc1C(F)(F)F`
ZINC3150756	0.622	321.2 Da LogP 4.52 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(Nc1cccc2ccccc12)C(C(F)(F)F)C(F)(F)F`
ZINC178267905	0.619	343.4 Da LogP 2.89 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@@H](C)N1CCN([C@@H](C)C(F)(F)F…`
ZINC178267918	0.619	343.4 Da LogP 2.89 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@H](C)N1CCN([C@@H](C)C(F)(F)F)…`
ZINC178267933	0.619	343.4 Da LogP 2.89 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@@H](C)N1CCN([C@H](C)C(F)(F)F)…`
ZINC178267948	0.619	343.4 Da LogP 2.89 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)[C@H](C)N1CCN([C@H](C)C(F)(F)F)C…`
ZINC126350	0.618	203.2 Da LogP 2.50 TPSA 29.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)C(F)(F)F`
ZINC2754661	0.618	368.3 Da LogP 4.15 TPSA 58.2	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)C(F)(F)C(F)(F)C(=O)Nc1ccccc1C`
ZINC1529407	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSC[C@@H](N)C(=O)O)C(=O)O`
ZINC1532680	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSC[C@H](N)C(=O)O)C(=O)O`
ZINC1708207	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCSC[C@H](N)C(=O)O)C(=O)O`
ZINC1708208	0.615	222.3 Da LogP -1.07 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC28210975	0.615	233.2 Da LogP 1.43 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(NCCO)c1ccccc1C(F)(F)F`
ZINC1605257	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](CCSC)C(=O)O`
ZINC1605258	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](NC(=O)[C@H](N)CCSC)C(=O)O`
ZINC1605259	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](CCSC)C(=O)O`
ZINC1605260	0.613	280.4 Da LogP 0.39 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@H](CCSC)C(=O)O`
ZINC2384801	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC242824	0.613	240.3 Da LogP 3.95 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)Nc1ccccc1C`
ZINC4556875	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC4556876	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC4556877	0.613	220.3 Da LogP -0.34 TPSA 92.4	✓ Ro5	✓ Clean	`CSCC[C@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC6218328	0.611	294.3 Da LogP 4.66 TPSA 41.1	✓ Ro5	✓ Clean	`Cc1ccccc1NC(=O)Nc1ccccc1C(F)(F)F`
ZINC3339684	0.609	350.3 Da LogP 3.69 TPSA 58.2	✓ Ro5	✓ Clean	`Cc1cccc(NC(=O)CNC(=O)c2ccccc2C(F)(F)F)c1C`
ZINC6993964	0.609	376.3 Da LogP 3.49 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CNC(=O)c1ccccc1C(F)(F)F)Nc1ccc(F)c(F)c1F`
ZINC41636241	0.600	227.2 Da LogP 2.07 TPSA 29.1	✓ Ro5	✓ Clean	`C#CCNC(=O)c1ccccc1C(F)(F)F`
ZINC450254	0.600	279.3 Da LogP 3.64 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)c1ccccc1C(F)(F)F`
ZINC4761004	0.600	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCC[C@H](N)C(=O)N[C@@H](C)C(=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.