Protein profile

PA2991

soluble pyridine nucleotide transhydrogenase

Genome: NC_002516.2

Gene: PA2991 sthA sth Structure source: AlphaFold UniProt P57112

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Amino acids 464

Annotations 8

Features 35

PDB binders 17

Druggability 0.273

Overview

Basic information about this protein and its source genome.

Accession: PA2991
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2991 sthA sth
Status: annotated
Amino acids: 464
Structure source: AlphaFold

1.6.1.1

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004148 Catalysis of the reaction: N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ = N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+. GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0003957 Catalysis of the reaction: NADPH + NAD+ = NADP+ + NADH. GO:0006103 The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism. GO:0006739 The chemical reactions and pathways involving nicotinamide adenine dinucleotide phosphate (NADP+), a coenzyme that interconverts with its reduced form, NADPH, in many redox and biosynthetic reactions.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 42.857
Human E-value: 6.46e-07
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 0.273

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1.6.1.1

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:0004148 Catalysis of the reaction: N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ = N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0003957 Catalysis of the reaction: NADPH + NAD+ = NADP+ + NADH.
GO:0006103 The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
GO:0006739 The chemical reactions and pathways involving nicotinamide adenine dinucleotide phosphate (NADP+), a coenzyme that interconverts with its reduced form, NADPH, in many redox and biosynthetic reactions.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

35 records

Show feature table

Start	End	DB	Term	Name
262	276	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
340	361	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
305	312	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
141	150	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
177	202	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
40	55	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
405	420	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
7	29	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
430	450	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
6	325	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
6	325	InterPro	IPR023753	FAD/NAD(P)-binding domain
8	27	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
138	156	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
261	277	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
290	312	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
177	195	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
1	464	Hamap	MF_00247	Soluble pyridine nucleotide transhydrogenase [sthA].
1	464	InterPro	IPR022962	Soluble pyridine nucleotide transhydrogenase, gammaproteobacteria
157	275	FunFam	G3DSA:3.50.50.60:FF:000008	Soluble pyridine nucleotide transhydrogenase
157	275	Gene3D	G3DSA:3.50.50.60	-
157	275	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
343	463	FunFam	G3DSA:3.30.390.30:FF:000002	Soluble pyridine nucleotide transhydrogenase
4	318	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
4	318	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
2	459	PIRSF	PIRSF000350	Hg-II_reductase_MerA
2	459	InterPro	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I
343	461	SUPERFAMILY	SSF55424	FAD/NAD-linked reductases, dimerisation (C-terminal) domain
343	461	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
344	455	Pfam	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
344	455	InterPro	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
343	463	Gene3D	G3DSA:3.30.390.30	-
343	463	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
6	332	Gene3D	G3DSA:3.50.50.60	-
6	332	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
5	456	PANTHER	PTHR22912	DISULFIDE OXIDOREDUCTASE

3D Structure

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

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Structural evidence

0 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA2991	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
2				0.273
4				0.233

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
2JR	4NEV	Q389T8	351.5 Da LogP 5.55 TPSA 31.9	1 viol.	✓ Clean	`c1cc2c(cc[nH]2)cc1c3ncc(s3)C4(CCCCC4)N5CCCC5`
BTB	6N7F	Q9A0E2	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
GCG	2WOW	Q389T8	723.9 Da LogP -4.58 TPSA 313.3	3 viol.	✓ Clean	`C(CCNC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@@H](C(=O)O…`
JWZ	6RB5	Q389T8	607.9 Da LogP 3.63 TPSA 103.4	1 viol.	✓ Clean	`[H]/N=C(/N)\N1CCC(CC1)(CN(C)CCCN2CN(C3(C2=O)CCN…`
M9J	6OEZ	Q389T8	555.8 Da LogP 6.51 TPSA 45.1	2 viol.	✓ Clean	`c1cc2c(ccn2CC3CCCN3)cc1c4nc(c(s4)C5(CCCCC5)N6CC…`
M9S	6OEY	Q389T8	434.7 Da LogP 5.77 TPSA 33.1	1 viol.	✓ Clean	`c1cc2c(ccn2C[C@@H]3CCCN3)cc1c4ncc(s4)C5(CCCCC5)…`
M9Y	6OEX	Q389T8	597.8 Da LogP 6.91 TPSA 45.1	2 viol.	✓ Clean	`c1cc2c(ccn2CCC3CCNCC3)cc1c4nc(c(s4)C5(CCCCC5)N6…`
MLT	6CMZ	B4EEF2	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
NHE	3RNM	P09622-2	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
RBF	6N7F	Q9A0E2	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@…`
RD0	6BU7	Q389T8	462.7 Da LogP 6.41 TPSA 33.1	1 viol.	✓ Clean	`c1cc2c(ccn2CCC3CCNCC3)cc1c4ncc(s4)C5(CCCCC5)N6C…`
RD7	6BTL	Q389T8	463.7 Da LogP 4.93 TPSA 36.3	✓ Ro5	✓ Clean	`c1cc2c(ccn2CCN3CCNCC3)cc1c4ncc(s4)C5(CCCCC5)N6C…`
WP5	2WP5	Q389T8	373.2 Da LogP 4.08 TPSA 41.9	✓ Ro5	✓ Clean	`CC1=Nc2ccc(cc2[C@@H](N1CC(=O)OC)c3ccccc3)Br`
WP6	2WP6	Q389T8	346.9 Da LogP 6.00 TPSA 15.6	1 viol.	✓ Clean	`CC1=Nc2ccc(cc2[C@@H](N1Cc3ccccc3)c4ccccc4)Cl`
WP7	2WPC	Q389T8	463.0 Da LogP 4.85 TPSA 52.3	✓ Ro5	✓ Clean	`CC1=Nc2ccc(cc2[C@@H](N1CCN3CCN(CC3)C(=O)c4ccco4…`
WPE	2WPE	Q389T8	393.9 Da LogP 4.82 TPSA 57.8	✓ Ro5	✓ Clean	`CC1=Nc2ccc(cc2[C@@H](N1CCNC(=O)c3ccco3)c4ccccc4…`
WPF	2WPF	Q389T8	355.9 Da LogP 5.06 TPSA 18.8	1 viol.	✓ Clean	`Cc1ccc(cc1)[C@H]2c3cc(ccc3N=C(N2CCCN(C)C)C)Cl`

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
ZINC11565587	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC1532585	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC1615342	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC1710230	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC1769096	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC2036848	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC3650334	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831422	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC3831423	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831424	1.000	376.4 Da LogP -1.72 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC655343	1.000	373.3 Da LogP 4.08 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(Br)cc2[C@H]1c1ccccc1`
ZINC655345	1.000	373.3 Da LogP 4.08 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(Br)cc2[C@@H]1c1ccccc1`
ZINC4353342	0.957	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC4353343	0.957	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC4353344	0.957	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC4353345	0.957	406.4 Da LogP -2.36 TPSA 181.8	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC2004116	0.860	396.8 Da LogP -1.38 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2c(cc1Cl)nc1c(=O)[nH]c(=O)nc-1n2C[C@H](O)[…`
ZINC149168378	0.857	374.4 Da LogP -0.31 TPSA 141.3	✓ Ro5	✓ Clean	`CC[C@@H](O)[C@@H](O)[C@@H](O)Cn1c2nc(=O)[nH]c(=…`
ZINC3650235	0.843	377.4 Da LogP -2.45 TPSA 187.6	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC4430211	0.843	396.8 Da LogP -1.38 TPSA 161.6	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC5545623	0.843	377.4 Da LogP -2.45 TPSA 187.6	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC5545624	0.843	377.4 Da LogP -2.45 TPSA 187.6	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC5545628	0.843	377.4 Da LogP -2.45 TPSA 187.6	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC4430517	0.820	404.4 Da LogP -1.22 TPSA 161.6	✓ Ro5	✓ Clean	`CCc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)…`
ZINC170612491	0.811	407.7 Da LogP 4.73 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(Br)cc2[C@@H]1c1cccc(Cl)c1`
ZINC170612493	0.811	407.7 Da LogP 4.73 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(Br)cc2[C@H]1c1cccc(Cl)c1`
ZINC35653106	0.811	405.4 Da LogP -1.97 TPSA 164.8	✓ Ro5	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC179149	0.800	308.4 Da LogP 3.62 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(C)cc2[C@H]1c1ccccc1`
ZINC179151	0.800	308.4 Da LogP 3.62 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(C)cc2[C@@H]1c1ccccc1`
ZINC100058975	0.796	359.2 Da LogP 3.99 TPSA 52.9	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Br)cc2[C@H](c2ccccc2)N1CC(=O)O`
ZINC100058980	0.796	359.2 Da LogP 3.99 TPSA 52.9	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Br)cc2[C@@H](c2ccccc2)N1CC(=O)O`
ZINC2004372	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC2689651	0.769	328.8 Da LogP 3.97 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(Cl)cc2[C@H]1c1ccccc1`
ZINC69847	0.769	328.8 Da LogP 3.97 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(Cl)cc2[C@@H]1c1ccccc1`
ZINC4430765	0.765	447.2 Da LogP -1.67 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO)c3…`
ZINC4430766	0.765	447.2 Da LogP -1.67 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO)c…`
ZINC4430767	0.765	447.2 Da LogP -1.67 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO)c…`
ZINC4430768	0.765	447.2 Da LogP -1.67 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO)…`
ZINC43763773	0.759	410.8 Da LogP -1.12 TPSA 161.6	✓ Ro5	✓ Clean	`CCc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)…`
ZINC43763774	0.759	410.8 Da LogP -1.12 TPSA 161.6	✓ Ro5	✓ Clean	`CCc1cc2c(cc1Cl)nc1c(=O)[nH]c(=O)nc-1n2C[C@H](O)…`
ZINC831827	0.759	407.7 Da LogP 4.73 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(Br)cc2[C@H]1c1ccccc1Cl`
ZINC831828	0.759	407.7 Da LogP 4.73 TPSA 41.9	✓ Ro5	✓ Clean	`COC(=O)CN1C(C)=Nc2ccc(Br)cc2[C@@H]1c1ccccc1Cl`
ZINC13513101	0.750	456.4 Da LogP -1.90 TPSA 204.9	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](O)[…`
ZINC3831426	0.750	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@H](O)…`
ZINC3831427	0.750	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC3831428	0.750	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC8551105	0.750	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@@H](O)[C@@H](O…`
ZINC8551106	0.750	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@@H](O)…`
ZINC8551108	0.750	456.3 Da LogP -1.61 TPSA 208.1	1 viol.	✓ Clean	`Cc1cc2nc3c(=O)[nH]c(=O)nc-3n(C[C@H](O)[C@H](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.