Amino acids
231
Annotations
7
Features
20
PDB binders
16
Druggability
0.494
Overview
Basic information about this protein and its source genome.
- Accession
- PA0750
- Gene
- ung PA0750
- Status
- annotated
- Amino acids
- 231
- Structure source
- AlphaFold
EC
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004844 Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine.
GO:0097510 A base-excision repair, AP site formation process occurring via excision of a deaminated base.
GO:0016799 Catalysis of the hydrolysis of any N-glycosyl bond.
GO:0006284 In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 52.727
- Human E-value
- 5.06e-76
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- Localization
- Cytoplasmic
Selected Druggability evidence
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
0.494
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
6 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
6- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0004844 Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine.
- GO:0097510 A base-excision repair, AP site formation process occurring via excision of a deaminated base.
- GO:0016799 Catalysis of the hydrolysis of any N-glycosyl bond.
- GO:0006284 In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
- GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
Sequence Features
Domain/signature hits from InterPro and related databases.
20 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 60 | 215 | Pfam | PF03167 | Uracil DNA glycosylase superfamily |
| 60 | 215 | InterPro | IPR005122 | Uracil-DNA glycosylase-like |
| 11 | 227 | Hamap | MF_00148 | Uracil-DNA glycosylase [ung]. |
| 11 | 227 | InterPro | IPR002043 | Uracil-DNA glycosylase family 1 |
| 7 | 229 | PANTHER | PTHR11264 | URACIL-DNA GLYCOSYLASE |
| 7 | 229 | InterPro | IPR002043 | Uracil-DNA glycosylase family 1 |
| 9 | 228 | SUPERFAMILY | SSF52141 | Uracil-DNA glycosylase-like |
| 9 | 228 | InterPro | IPR036895 | Uracil-DNA glycosylase-like domain superfamily |
| 64 | 73 | ProSitePatterns | PS00130 | Uracil-DNA glycosylase signature. |
| 64 | 73 | InterPro | IPR018085 | Uracil-DNA glycosylase, active site |
| 26 | 226 | CDD | cd10027 | UDG-F1-like |
| 26 | 226 | InterPro | IPR002043 | Uracil-DNA glycosylase family 1 |
| 4 | 229 | FunFam | G3DSA:3.40.470.10:FF:000001 | Uracil-DNA glycosylase |
| 2 | 231 | Gene3D | G3DSA:3.40.470.10 | - |
| 2 | 231 | InterPro | IPR036895 | Uracil-DNA glycosylase-like domain superfamily |
| 56 | 216 | SMART | SM00987 | UDG_2_a |
| 56 | 216 | SMART | SM00986 | UDG_2 |
| 56 | 216 | InterPro | IPR005122 | Uracil-DNA glycosylase-like |
| 12 | 220 | NCBIfam | TIGR00628 | uracil-DNA glycosylase |
| 12 | 220 | InterPro | IPR002043 | Uracil-DNA glycosylase family 1 |
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
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA0750
|
AlphaFold | — | — | full sequence | — | Viewing |
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.494 |
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.
67 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 |
|---|---|---|---|---|---|---|
| 302 | P13051 | 346.3 Da LogP 0.16 TPSA 146.2 | ✓ Ro5 | ✓ Clean |
c1cc(ccc1\C=N\OCCO/N=C/C2=CC(=O)NC(=O)N2)C(=O)O
|
|
| 3FI | P13051 | 346.3 Da LogP 0.29 TPSA 136.6 | ✓ Ro5 | ✓ Clean |
c1cc(cc(c1)C(=O)O)\C=N\OCCCNCC2=CC(=O)NC(=O)N2
|
|
| 3FL | P13051 | 346.4 Da LogP 0.42 TPSA 127.1 | ✓ Ro5 | ✓ Clean |
c1cc(cc(c1)C(=O)O)CNCCCCNCC2=CC(=O)NC(=O)N2
|
|
| 5NU | P9WFQ9 | 157.1 Da LogP -1.03 TPSA 108.9 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1)[N+](=O)[O-]
|
|
| 5UC | P9WFQ9 | 146.5 Da LogP -0.28 TPSA 65.7 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1)Cl
|
|
| 6UA | P9WFQ9 | 127.1 Da LogP -1.02 TPSA 84.5 | ✓ Ro5 | ✓ Clean |
C1C(=NC(=O)NC1=O)N
|
|
| DUR | P10186 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
C1[C@@H]([C@H](O[C@H]1N2C=CC(=O)NC2=O)CO)O
|
|
| FCF | P13051 | 346.3 Da LogP 0.16 TPSA 146.2 | ✓ Ro5 | ✓ Clean |
c1cc(cc(c1)C(=O)O)\C=N\OCCO/N=C/C2=CC(=O)NC(=O)…
|
|
| FCK | P13051 | 346.3 Da LogP 0.29 TPSA 136.6 | ✓ Ro5 | ✓ Clean |
c1cc(cc(c1)C(=O)O)CNCCCON=CC2=CC(=O)NC(=O)N2
|
|
| FLC | P9WFQ9 | 189.1 Da LogP -5.25 TPSA 140.6 | ✓ Ro5 | ✓ Clean |
C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
|
|
| QU4 | P13051 | 422.3 Da LogP 2.45 TPSA 169.4 | ✓ Ro5 | ✓ Clean |
c1cc(c(cc1C(=C2C=CC(=O)C(=C2)C(=O)O)c3ccc(c(c3)…
|
|
| TUL | P9WFQ9 | 128.2 Da LogP 0.43 TPSA 48.6 | ✓ Ro5 | ✓ Clean |
C1=CNC(=S)NC1=O
|
|
| URA | D0VWU0 | 112.1 Da LogP -0.94 TPSA 65.7 | ✓ Ro5 | ✓ Clean |
C1=CNC(=O)NC1=O
|
|
| URB | D0VWU0 | 191.0 Da LogP -0.17 TPSA 65.7 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1)Br
|
|
| URF | P9WFQ9 | 130.1 Da LogP -0.80 TPSA 65.7 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1)F
|
|
| WBU | P9WFQ9 | 127.1 Da LogP -1.35 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
C1=C(C(=O)NC(=O)N1)N
|
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 |
|---|---|---|---|---|---|---|
| CHEMBL4129274 | P13051 | — | 851.5 Da LogP 4.76 TPSA 183.3 | 3 viol. | Alert |
C=CC(=O)Nc1ccccc1Nc1nc(Nc2ccc(N3CCN(CCOCCOCCOCC…
|
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 |
|---|---|---|---|---|---|
| ZINC105325 | 1.000 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]1
|
| ZINC155696 | 1.000 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]1
|
| ZINC2556389 | 1.000 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]1
|
| ZINC3635934 | 1.000 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]1
|
| ZINC3833863 | 1.000 | 422.3 Da LogP 2.45 TPSA 169.4 | ✓ Ro5 | ✓ Clean |
O=C(O)C1=CC(=C(c2ccc(O)c(C(=O)O)c2)c2ccc(O)c(C(…
|
| ZINC3869842 | 1.000 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]1
|
| ZINC4124398 | 1.000 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]1
|
| ZINC56350 | 1.000 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]1
|
| ZINC8613701 | 1.000 | 228.2 Da LogP -1.82 TPSA 104.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]1
|
| ZINC4918789 | 0.850 | 258.2 Da LogP -2.46 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=…
|
| ZINC4918794 | 0.850 | 258.2 Da LogP -2.46 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O…
|
| ZINC4918798 | 0.850 | 258.2 Da LogP -2.46 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(…
|
| ZINC4918802 | 0.850 | 258.2 Da LogP -2.46 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=…
|
| ZINC103421486 | 0.762 | 244.3 Da LogP -0.45 TPSA 87.5 | ✓ Ro5 | ✓ Clean |
O=c1[nH]c(=S)ccn1[C@H]1C[C@@H](O)[C@@H](CO)O1
|
| ZINC1081178 | 0.762 | 230.2 Da LogP -0.85 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@H](F)[C@@H](CO)O2)c(=O)[nH]1
|
| ZINC17173289 | 0.762 | 244.3 Da LogP -0.45 TPSA 87.5 | ✓ Ro5 | ✓ Clean |
O=c1[nH]c(=S)ccn1[C@H]1C[C@H](O)[C@@H](CO)O1
|
| ZINC2556998 | 0.762 | 230.2 Da LogP -0.85 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@@H](F)[C@H](CO)O2)c(=O)[nH]1
|
| ZINC29544850 | 0.762 | 230.2 Da LogP -0.85 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@@H](F)[C@@H](CO)O2)c(=O)[nH]1
|
| ZINC33505015 | 0.762 | 244.3 Da LogP -0.45 TPSA 87.5 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=S)[nH]1
|
| ZINC3792179 | 0.762 | 230.2 Da LogP -0.85 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@H](F)[C@@H](CO)O2)c(=O)[nH]1
|
| ZINC4975368 | 0.762 | 230.2 Da LogP -0.85 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@H](F)[C@H](CO)O2)c(=O)[nH]1
|
| ZINC2054344316 | 0.756 | 300.3 Da LogP 2.01 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
CC(=C1C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1
|
| ZINC28092924 | 0.756 | 300.3 Da LogP 2.01 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
C/C(=C1/C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1
|
| ZINC36748824 | 0.756 | 300.3 Da LogP 2.01 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
C/C(=C1\C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1
|
| ZINC1532902 | 0.700 | 206.2 Da LogP -0.86 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC2018106 | 0.700 | 206.2 Da LogP -0.86 TPSA 132.1 | ✓ Ro5 | ✓ Clean |
O=C(O)CC[C@](O)(CC(=O)O)C(=O)O
|
| ZINC13514392 | 0.696 | 308.2 Da LogP -1.71 TPSA 151.1 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)…
|
| ZINC1532629 | 0.696 | 308.2 Da LogP -1.71 TPSA 151.1 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c…
|
| ZINC3869888 | 0.696 | 308.2 Da LogP -1.71 TPSA 151.1 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(…
|
| ZINC3869889 | 0.696 | 308.2 Da LogP -1.71 TPSA 151.1 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…
|
| ZINC3869890 | 0.696 | 308.2 Da LogP -1.71 TPSA 151.1 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…
|
| ZINC4228260 | 0.696 | 308.2 Da LogP -1.71 TPSA 151.1 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…
|
| ZINC6524723 | 0.696 | 308.2 Da LogP -1.71 TPSA 151.1 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c…
|
| ZINC3787626 | 0.681 | 253.2 Da LogP -0.50 TPSA 133.1 | ✓ Ro5 | Alert |
[N-]=[N+]=N[C@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@@…
|
| ZINC5663432 | 0.681 | 253.2 Da LogP -0.50 TPSA 133.1 | ✓ Ro5 | Alert |
[N-]=[N+]=N[C@H]1C[C@@H](n2ccc(=O)[nH]c2=O)O[C@…
|
| ZINC5663433 | 0.681 | 253.2 Da LogP -0.50 TPSA 133.1 | ✓ Ro5 | Alert |
[N-]=[N+]=N[C@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@H…
|
| ZINC5663434 | 0.681 | 253.2 Da LogP -0.50 TPSA 133.1 | ✓ Ro5 | Alert |
[N-]=[N+]=N[C@@H]1C[C@@H](n2ccc(=O)[nH]c2=O)O[C…
|
| ZINC5663435 | 0.681 | 253.2 Da LogP -0.50 TPSA 133.1 | ✓ Ro5 | Alert |
[N-]=[N+]=N[C@@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@…
|
| ZINC6524816 | 0.681 | 253.2 Da LogP -0.50 TPSA 133.1 | ✓ Ro5 | Alert |
[N-]=[N+]=N[C@@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@…
|
| ZINC38322194 | 0.667 | 254.2 Da LogP -1.26 TPSA 134.6 | ✓ Ro5 | Alert |
N=[N+]=N[C@@H]1C[C@@H](n2ccc(=O)[nH]c2=O)O[C@H]…
|
| ZINC38322195 | 0.667 | 254.2 Da LogP -1.26 TPSA 134.6 | ✓ Ro5 | Alert |
N=[N+]=N[C@@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@H]1…
|
| ZINC3870698 | 0.667 | 212.2 Da LogP -0.80 TPSA 84.3 | ✓ Ro5 | ✓ Clean |
C[C@H]1O[C@@H](n2ccc(=O)[nH]c2=O)C[C@@H]1O
|
| ZINC3593496 | 0.652 | 206.2 Da LogP -1.16 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
COC(=O)C[C@@](O)(CC(=O)O)C(=O)O
|
| ZINC3593497 | 0.652 | 206.2 Da LogP -1.16 TPSA 121.1 | ✓ Ro5 | ✓ Clean |
COC(=O)C[C@](O)(CC(=O)O)C(=O)O
|
| ZINC13519035 | 0.651 | 229.2 Da LogP -2.43 TPSA 117.4 | ✓ Ro5 | ✓ Clean |
O=c1ncn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]1
|
| ZINC64708385 | 0.644 | 467.4 Da LogP 0.44 TPSA 214.5 | 1 viol. | ✓ Clean |
NOC(=O)C1=CC(=C(c2ccc(O)c(C(=O)ON)c2)c2ccc(O)c(…
|
| ZINC8217150 | 0.640 | 388.2 Da LogP -1.59 TPSA 197.6 | ✓ Ro5 | ✓ Clean |
O=c1ccn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(…
|
| ZINC44608151 | 0.636 | 244.2 Da LogP -2.12 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1[nH]c(=O)n([C@H]2C[C@@H](O)[C@@H](CO)O2)cc1O
|
| ZINC4897037 | 0.636 | 244.2 Da LogP -2.12 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1[nH]c(=O)n([C@@H]2C[C@H](O)[C@H](CO)O2)cc1O
|
| ZINC6090954 | 0.636 | 244.2 Da LogP -2.12 TPSA 124.8 | ✓ Ro5 | ✓ Clean |
O=c1[nH]c(=O)n([C@H]2C[C@H](O)[C@@H](CO)O2)cc1O
|
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.