Protein profile

PA2025

glutathione reductase

Genome: NC_002516.2

Gene: gor PA2025 Structure source: AlphaFold UniProt P23189

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Amino acids 451

Annotations 8

Features 35

PDB binders 23

Druggability 0.268

Overview

Basic information about this protein and its source genome.

Accession: PA2025
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: gor PA2025
Status: annotated
Amino acids: 451
Structure source: AlphaFold

1.8.1.7

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. 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:0004362 Catalysis of the reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+. GO:0004791 Catalysis of the reaction: thioredoxin-dithiol + NADP+ = thioredoxin-disulfide + H+ + NADPH. GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell. 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 48.98
Human E-value: 4.49e-19
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 0.268

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)

1.8.1.7

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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:0004362 Catalysis of the reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+.
GO:0004791 Catalysis of the reaction: thioredoxin-dithiol + NADP+ = thioredoxin-disulfide + H+ + NADPH.
GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell.
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.

35 records

Show feature table

Start	End	DB	Term	Name
151	270	FunFam	G3DSA:3.50.50.60:FF:000051	Glutathione reductase
143	260	Gene3D	G3DSA:3.50.50.60	-
143	260	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
337	451	Gene3D	G3DSA:3.30.390.30	-
337	451	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
6	317	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
6	317	InterPro	IPR023753	FAD/NAD(P)-binding domain
4	448	PANTHER	PTHR42737	GLUTATHIONE REDUCTASE
4	448	InterPro	IPR046952	Glutathione reductase/thioredoxin reductase-like
1	444	PIRSF	PIRSF000350	Hg-II_reductase_MerA
1	444	InterPro	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I
39	49	ProSitePatterns	PS00076	Pyridine nucleotide-disulphide oxidoreductases class-I active site.
39	49	InterPro	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site
5	319	Gene3D	G3DSA:3.50.50.60	-
5	319	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
335	447	SUPERFAMILY	SSF55424	FAD/NAD-linked reductases, dimerisation (C-terminal) domain
335	447	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
338	446	Pfam	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
338	446	InterPro	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
399	414	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
134	143	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
297	304	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
6	28	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
38	53	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
168	193	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
254	268	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
334	355	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
421	441	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
1	358	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
1	358	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
168	186	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
282	304	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
131	149	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
7	26	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
253	269	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature

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 PA2025	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
4				0.268

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.

94 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`
ACM	1GRF	P00390	59.1 Da LogP -0.51 TPSA 43.1	✓ Ro5	✓ Clean	`CC(=O)N`
AUP	2AAQ	P00390	368.4 Da LogP 6.67 TPSA 25.8	1 viol.	✓ Clean	`c1ccc(cc1)p2c(c3c(c2c4ccccn4)CCCC3)c5ccccn5`
BTB	6N7F	Q9A0E2	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
ELI	2GH5	P00390	286.3 Da LogP 3.42 TPSA 71.4	✓ Ro5	Alert	`CC1=C(C(=O)c2ccccc2C1=O)CCCCCC(=O)O`
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…`
GSH	1DNC	P00390	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`C(CC(=O)N[C@@H](CS)C(=O)NCC(=O)O)[C@@H](C(=O)O)N`
HXP	1XAN	P00390	286.3 Da LogP 3.20 TPSA 87.0	✓ Ro5	✓ Clean	`c1cc2c(cc1O)Oc3cc(ccc3C2CCC(=O)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…`
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…`
RGS	4GR1	P00390	612.6 Da LogP -3.88 TPSA 317.6	3 viol.	✓ Clean	`C(CNC(=O)[C@@H](CSSC[C@H](C(=O)NCC[C@@H](C(=O)O…`
TS2	3GRT	P00390	721.9 Da LogP -4.04 TPSA 313.3	3 viol.	✓ Clean	`C1CCNC(=O)CNC(=O)[C@H](CSSC[C@@H](C(=O)NCC(=O)N…`
TS4	5GRT	P00390	867.1 Da LogP -4.38 TPSA 377.3	3 viol.	✓ Clean	`C(CCNCCCNC(=O)CNC(=O)[C@H](CSSC[C@@H](C(=O)NCC(…`
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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL1836603	P39051	6.72	355.9 Da LogP 5.06 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(C)cc2)N1CCCN(C)C`
CHEMBL1836570	P39051	6.57	454.0 Da LogP 3.50 TPSA 42.4	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C(=O)CN(C…`
CHEMBL1836378	P39051	6.50	382.9 Da LogP 4.04 TPSA 22.1	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C)CC1`
CHEMBL1836574	P39051	6.46	459.4 Da LogP 5.23 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(I)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836567	P39051	6.38	463.0 Da LogP 4.85 TPSA 52.3	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C(=O)c2cc…`
CHEMBL1836559	P39051	6.36	393.9 Da LogP 4.82 TPSA 57.8	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCNC(=O)c1ccco1`
CHEMBL1836615	P39051	6.23	382.0 Da LogP 5.59 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(C)cc2)N1CCN1CCCCC1`
CHEMBL1836612	P39051	6.14	402.4 Da LogP 5.93 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(Cl)cc2)N1CCN1CCCCC1`
CHEMBL135536	P00390	6.12	302.3 Da LogP 3.12 TPSA 91.7	✓ Ro5	Alert	`CC1=C(CCCCCC(=O)O)C(=O)c2c(O)cccc2C1=O`
CHEMBL1836571	P39051	6.11	333.5 Da LogP 4.63 TPSA 18.8	✓ Ro5	✓ Clean	`CC1=Nc2ccccc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836572	P39051	6.10	412.4 Da LogP 5.39 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Br)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836577	P39051	6.10	415.6 Da LogP 6.36 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(-c3ccsc3)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836371	P39051	6.09	389.9 Da LogP 6.06 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1cccc(N(C)C)c1`
CHEMBL1836562	P39051	6.09	384.9 Da LogP 3.47 TPSA 47.9	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCNC(=O)CN(C)C`
CHEMBL1836606	P39051	6.05	385.9 Da LogP 5.42 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2cccc(F)c2)N1CCN1CCCCC1`
CHEMBL1836365	P39051	6.03	346.9 Da LogP 6.00 TPSA 15.6	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1ccccc1`
CHEMBL1836368	P39051	6.03	364.9 Da LogP 6.13 TPSA 15.6	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1ccccc1F`
CHEMBL135504	P00390	6.00	288.3 Da LogP 2.73 TPSA 91.7	✓ Ro5	Alert	`CC1=C(CCCCC(=O)O)C(=O)c2c(O)cccc2C1=O`
CHEMBL1836380	P39051	6.00	341.9 Da LogP 4.75 TPSA 18.8	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCCN(C)C`
CHEMBL4859269	P39051	6.00	1157.2 Da LogP 7.07 TPSA 297.0	4 viol.	✓ Clean	`NCCCCc1cn(-c2ccc(-c3nc(-c4cccc(-c5csc(-c6ccc(-n…`
GDS	P00390	—	612.6 Da LogP -3.88 TPSA 317.6	3 viol.	✓ Clean	`C(CC(=O)N[C@@H](CSSC[C@@H](C(=O)NCC(=O)O)NC(=O)…`

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`
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)…`
ZINC3830891	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)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`
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)[…`
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)[…`
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…`

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.