Protein profile

KP13_31580

Mercuric reductase

Genome: KpKP13

Gene: merA AHE47230.1 Structure source: AlphaFold + ColabFold UniProt A0A2D1HBC1

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Amino acids 564

Annotations 11

Features 41

PDB binders 18

Druggability 0.997

Overview

Basic information about this protein and its source genome.

Accession: KP13_31580
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: merA AHE47230.1
Status: annotated
Amino acids: 564
Structure source: AlphaFold + ColabFold

1.16.1.1

GO:0045340 Binding to a mercury ion (Hg2+). GO:0050787 Any process that reduce or remove the toxicity of mercuric ion. These include transport of mercury away from sensitive areas and to compartments or complexes whose purpose is sequestration of mercury ion and/or reduction of mercury ion (Hg[II]) to metallic mercury (Hg[0]). 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:0046872 Binding to a metal ion. 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: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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 53.061
Human E-value: 2.46e-08
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 93.16

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 0.997

Structure A0A2D1HBC1

Pocket Pocket 25

P2Rank 0.956

Structure A0A2D1HBC1

Pocket Pocket 1

ColabFold model

FPocket 0.853 · Pocket 26

P2Rank 0.957 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 21 / 4744 genomes with a hit

Normalized 0.004

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1.16.1.1

Gene Ontology (GO)

GO:0045340 Binding to a mercury ion (Hg2+).
GO:0050787 Any process that reduce or remove the toxicity of mercuric ion. These include transport of mercury away from sensitive areas and to compartments or complexes whose purpose is sequestration of mercury ion and/or reduction of mercury ion (Hg[II]) to metallic mercury (Hg[0]).
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:0046872 Binding to a metal ion.
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: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: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.
GO:0016152 Catalysis of the reaction: H+ + Hg + NADP+ = Hg2+ + NADPH.
GO:0003955 Catalysis of the reaction: NAD(P)H + H+ + a quinone = NAD(P)+ + a quinol.
GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

Sequence Features

Domain/signature hits from InterPro and related databases.

41 records

Show feature table

Start	End	DB	Term	Name
3	65	CDD	cd00371	HMA
3	65	InterPro	IPR006121	Heavy metal-associated domain, HMA
1	564	PIRSF	PIRSF000350	Hg-II_reductase_MerA
1	564	InterPro	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I
1	69	Gene3D	G3DSA:3.30.70.100	-
6	35	ProSitePatterns	PS01047	Heavy-metal-associated domain.
6	35	InterPro	IPR017969	Heavy-metal-associated, conserved site
96	558	PANTHER	PTHR43014	MERCURIC REDUCTASE
100	460	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
100	460	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
99	421	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
99	421	InterPro	IPR023753	FAD/NAD(P)-binding domain
439	562	SUPERFAMILY	SSF55424	FAD/NAD-linked reductases, dimerisation (C-terminal) domain
439	562	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
132	142	ProSitePatterns	PS00076	Pyridine nucleotide-disulphide oxidoreductases class-I active site.
132	142	InterPro	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site
2	70	SUPERFAMILY	SSF55008	HMA, heavy metal-associated domain
2	70	InterPro	IPR036163	Heavy metal-associated domain superfamily
439	564	Gene3D	G3DSA:3.30.390.30	-
439	564	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
439	559	FunFam	G3DSA:3.30.390.30:FF:000001	Dihydrolipoyl dehydrogenase
440	548	Pfam	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
440	548	InterPro	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
99	564	NCBIfam	TIGR02053	mercury(II) reductase
99	564	InterPro	IPR021179	Mercury(II) reductase
1	65	ProSiteProfiles	PS50846	Heavy-metal-associated domain profile.
1	65	InterPro	IPR006121	Heavy metal-associated domain, HMA
244	364	Gene3D	G3DSA:3.50.50.60	-
244	364	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
3	62	Pfam	PF00403	Heavy-metal-associated domain
3	62	InterPro	IPR006121	Heavy metal-associated domain, HMA
101	423	Gene3D	G3DSA:3.50.50.60	-
101	423	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
236	253	PRINTS	PR00945	Mercuric reductase class II signature
472	492	PRINTS	PR00945	Mercuric reductase class II signature
271	288	PRINTS	PR00945	Mercuric reductase class II signature
537	556	PRINTS	PR00945	Mercuric reductase class II signature
109	127	PRINTS	PR00945	Mercuric reductase class II signature
13	23	PRINTS	PR00945	Mercuric reductase class II signature
144	163	PRINTS	PR00945	Mercuric reductase class II signature
291	306	PRINTS	PR00945	Mercuric reductase class II signature

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_A0A2D1HBC1	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_31580	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
25				0.997
15				0.399

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	25.89	0.909
2	2.98	0.097
3	2.47	0.068
4	1.92	0.039
5	1.55	0.023

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
26				0.853
7				0.635
10				0.252

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	26.81	0.917
2	3.75	0.144
3	3.51	0.129
4	2.61	0.076
5	1.93	0.039

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.

72 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`
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	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…`
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)…`
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`
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).

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`
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`
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`
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`
ZINC4262829	0.781	263.3 Da LogP 2.74 TPSA 46.2	✓ Ro5	Alert	`O=C1C=C(NCc2ccccc2)C(=O)c2ccccc21`
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)[…`
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…`

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.