Protein profile

PA4829

dihydrolipoamide dehydrogenase

Genome: NC_002516.2

Gene: PA4829 lpd3 Structure source: AlphaFold UniProt Q9HUY1

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Amino acids 467

Annotations 7

Features 36

PDB binders 9

Druggability 0.716

Overview

Basic information about this protein and its source genome.

Accession: PA4829
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4829 lpd3
Status: annotated
Amino acids: 467
Structure source: AlphaFold

1.8.1.4

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. 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: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: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. GO:0016668 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces NAD or NADP.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 66.667
Human E-value: 7.729999999999999e-24
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 0.716

Structure –

Pocket –

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)

1.8.1.4

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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: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: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.
GO:0016668 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces NAD or NADP.

Sequence Features

Domain/signature hits from InterPro and related databases.

36 records

Show feature table

Start	End	DB	Term	Name
1	463	PIRSF	PIRSF000350	Hg-II_reductase_MerA
1	463	InterPro	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I
40	50	ProSitePatterns	PS00076	Pyridine nucleotide-disulphide oxidoreductases class-I active site.
40	50	InterPro	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site
6	28	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
409	424	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
431	451	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
39	54	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
344	365	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
141	150	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
267	281	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
177	202	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
309	316	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
347	467	Gene3D	G3DSA:3.30.390.30	-
347	467	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
348	456	Pfam	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
348	456	InterPro	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
347	467	FunFam	G3DSA:3.30.390.30:FF:000001	Dihydrolipoyl dehydrogenase
1	375	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
1	375	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
150	273	Gene3D	G3DSA:3.50.50.60	-
150	273	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
138	156	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
7	26	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
266	282	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
294	316	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
177	195	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
344	465	SUPERFAMILY	SSF55424	FAD/NAD-linked reductases, dimerisation (C-terminal) domain
344	465	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
6	331	Gene3D	G3DSA:3.50.50.60	-
6	331	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
4	465	NCBIfam	TIGR01350	dihydrolipoyl dehydrogenase
4	465	InterPro	IPR006258	Dihydrolipoamide dehydrogenase
3	459	PANTHER	PTHR22912	DISULFIDE OXIDOREDUCTASE
5	329	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
5	329	InterPro	IPR023753	FAD/NAD(P)-binding domain

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 PA4829	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				0.716

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.

69 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
3II	3II4	P9WHH9	625.6 Da LogP 4.65 TPSA 91.4	1 viol.	✓ Clean	`COc1ccc(c(c1)OC)C(=O)N2CCC3(CC2)C(=O)N(CN3c4ccc…`
BTB	6N7F	Q9A0E2	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
GCG	1BZL	P28593	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…`
M52	4M52	P9WHH9	429.3 Da LogP 1.69 TPSA 114.6	✓ Ro5	✓ Clean	`C[N@@](CC(=O)Nc1ccc(cc1)OC)S(=O)(=O)c2cc(cnc2N)…`
MAE	1AOG	P28593	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)/C(=O)O`
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`
QUM	1GXF	P28593	468.9 Da LogP 5.83 TPSA 40.6	1 viol.	✓ Clean	`C[C@@H](CCCN(CCCl)CCCl)/N=C\1/c2ccc(cc2Nc3c1cc(…`
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@…`

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
CHEMBL1451931	P9WHH9	7.00	263.3 Da LogP 2.58 TPSA 46.2	✓ Ro5	Alert	`O=C1C=C(NCc2ccccc2)c2ccccc2C1=O`
CHEMBL160637	P28593	6.52	456.6 Da LogP 5.06 TPSA 86.7	1 viol.	Alert	`CCCCN(CCCC)CCCNC(=O)CCCCC1=C(C)C(=O)c2cccc(O)c2…`
CHEMBL76523	P28593	6.46	530.7 Da LogP 3.80 TPSA 113.8	2 viol.	✓ Clean	`O=C(CCc1c[nH]c2ccccc12)NCCCNCCCCNCCCNC(=O)Cc1c[…`
CHEMBL76582	P28593	6.41	516.7 Da LogP 3.41 TPSA 113.8	2 viol.	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)NCCCNCCCCNCCCNC(=O)Cc1c[n…`
CHEMBL358636	P28593	6.35	671.8 Da LogP 4.91 TPSA 179.0	1 viol.	Alert	`CC1=C(CCCCC(=O)NCCCNCCCNC(=O)CCCCC2=C(C)C(=O)c3…`
CHEMBL159006	P28593	6.22	711.0 Da LogP 8.01 TPSA 119.1	2 viol.	Alert	`CCCCN(CCCC)CCCNC(=O)CCCCC1=C(CCCCC(=O)NCCCN(CCC…`
CHEMBL3949128	P9WHH9	6.16	463.7 Da LogP 2.35 TPSA 114.6	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1Cl`
CHEMBL152787	P28593	6.10	680.9 Da LogP 3.48 TPSA 125.5	1 viol.	Alert	`CN1CCN(CCCNC(=O)CCCCCC2=C(CCCCCC(=O)NCCCN3CCN(C…`
CHEMBL3935059	P9WHH9	6.08	441.4 Da LogP 2.81 TPSA 105.4	✓ Ro5	✓ Clean	`CC(C)c1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1`
CHEMBL3983097	P9WHH9	6.08	459.3 Da LogP 1.70 TPSA 123.9	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1OC`

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…`
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)…`
ZINC12297063	0.814	388.5 Da LogP 3.06 TPSA 89.8	✓ Ro5	✓ Clean	`O=C(CCc1c[nH]c2ccccc12)NCCNC(=O)Cc1c[nH]c2ccccc…`
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)[…`
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`
ZINC4262829	0.781	263.3 Da LogP 2.74 TPSA 46.2	✓ Ro5	Alert	`O=C1C=C(NCc2ccccc2)C(=O)c2ccccc21`
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)…`
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)[…`
ZINC3831425	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)[…`
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)[…`
ZINC7782849	0.745	258.4 Da LogP 3.41 TPSA 44.9	✓ Ro5	✓ Clean	`CCCCCNC(=O)CCc1c[nH]c2ccccc12`
ZINC12296361	0.744	402.5 Da LogP 3.45 TPSA 89.8	✓ Ro5	✓ Clean	`O=C(CCc1c[nH]c2ccccc12)NCCNC(=O)CCc1c[nH]c2cccc…`
ZINC9689998	0.727	331.4 Da LogP 3.94 TPSA 60.7	✓ Ro5	✓ Clean	`O=C(CCc1c[nH]c2ccccc12)NCCc1c[nH]c2ccccc12`
ZINC7735055	0.723	244.3 Da LogP 3.02 TPSA 44.9	✓ Ro5	✓ Clean	`CCCCNC(=O)CCc1c[nH]c2ccccc12`
ZINC12296653	0.717	416.5 Da LogP 3.84 TPSA 89.8	✓ Ro5	✓ Clean	`O=C(CCCc1c[nH]c2ccccc12)NCCNC(=O)CCc1c[nH]c2ccc…`
ZINC4430761	0.717	412.8 Da LogP -2.33 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO)c3…`
ZINC4430762	0.717	412.8 Da LogP -2.33 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO)c…`
ZINC4430763	0.717	412.8 Da LogP -2.33 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO)c…`
ZINC4430764	0.717	412.8 Da LogP -2.33 TPSA 181.8	1 viol.	✓ Clean	`O=c1nc2n(C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO)…`

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.