Protein profile

VK055_3604

glutathione-disulfide reductase

Genome: KpATCC43816

Gene: AIK82159.1 gor Structure source: AlphaFold + ColabFold UniProt A0A0H3H498

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Amino acids 450

Annotations 7

Features 38

PDB binders 24

Druggability 0.488

Overview

Basic information about this protein and its source genome.

Accession: VK055_3604
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: AIK82159.1 gor
Status: annotated
Amino acids: 450
Structure source: AlphaFold + ColabFold

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:0006749 The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle. GO:0004362 Catalysis of the reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH + 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:0045454 Any process that maintains the redox environment of a cell or compartment within a cell. 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 (%): 54.329
Human E-value: 2.44e-160
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 92.444
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 98.29

Selected Druggability evidence

AlphaFold / UniProt model

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 0.488

Structure A0A0H3H498

Pocket Pocket 24

P2Rank 0.96

Structure A0A0H3H498

Pocket Pocket 1

ColabFold model

FPocket 0.718 · Pocket 36

P2Rank 0.93 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 229 / 4744 genomes with a hit

Normalized 0.048

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

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:0006749 The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle.
GO:0004362 Catalysis of the reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH + 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:0045454 Any process that maintains the redox environment of a cell or compartment within a cell.
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.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
144	261	Gene3D	G3DSA:3.50.50.60	-
144	261	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
4	450	PANTHER	PTHR42737	GLUTATHIONE REDUCTASE
4	450	InterPro	IPR046952	Glutathione reductase/thioredoxin reductase-like
5	159	FunFam	G3DSA:3.50.50.60:FF:000030	Glutathione reductase
336	450	SUPERFAMILY	SSF55424	FAD/NAD-linked reductases, dimerisation (C-terminal) domain
336	450	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
3	450	NCBIfam	TIGR01421	glutathione-disulfide reductase
3	450	InterPro	IPR006322	Glutathione reductase, eukaryote/bacterial
1	447	PIRSF	PIRSF000350	Hg-II_reductase_MerA
1	447	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
339	449	Pfam	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
339	449	InterPro	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
338	450	Gene3D	G3DSA:3.30.390.30	-
338	450	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
338	450	FunFam	G3DSA:3.30.390.30:FF:000003	Glutathione reductase
255	269	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
298	305	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
335	356	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
135	144	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
424	444	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
169	194	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
402	417	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
6	318	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
6	318	InterPro	IPR023753	FAD/NAD(P)-binding domain
5	320	Gene3D	G3DSA:3.50.50.60	-
5	320	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
7	26	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
169	187	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
254	270	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
283	305	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
132	150	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
1	366	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
1	366	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily

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...

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Structural evidence

0 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3H498	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_3604	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
24				0.488
3				0.436

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	17.36	0.801
2	10.56	0.568
3	1.59	0.025
4	1.47	0.02
5	1.41	0.018

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
36				0.718

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	19.87	0.846
2	10.92	0.586
3	2.66	0.078
4	1.74	0.031
5	1.11	0.008

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.

76 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…`
GDS	2GRT	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)…`
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
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`
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`

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`
ZINC3830892	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`
ZINC3830893	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`
ZINC3830894	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…`
ZINC1532230	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556979	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556980	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556981	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC5828410	0.821	306.3 Da LogP -2.81 TPSA 164.6	1 viol.	✓ Clean	`NC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(=O)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`
ZINC13549503	0.780	321.4 Da LogP -2.12 TPSA 147.8	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O`
ZINC4096455	0.775	321.4 Da LogP -1.82 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCCC(=O)O)C(=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`
ZINC31350707	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC…`
ZINC31350710	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(…`
ZINC31350713	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(…`
ZINC3872734	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC4544082	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544083	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544085	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=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.