Protein target profile

KP13_02396

Sulfite reductase [NADPH] flavoprotein alpha-component

Genome: KpKP13 Gene: AHE42967.1 cysJ 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GWU1

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Length 590

Pocket druggability 0.412

Direct ligand evidence 0 59 total records

Functional annotation 1 EC 8 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Moderate predicted binding pocket FPocket selected-pocket score 0.41. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.61. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 9 structural and 0 bioactivity records.

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 34.568 Lower values reduce human off-target concern.
Human E-value: 1.3699999999999998e-60
Gut microbiome similarity: 2.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 91.57 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.412

Structure A0A0H3GWU1

Pocket Pocket 18

P2Rank 0.614

Structure A0A0H3GWU1

Pocket Pocket 1

ColabFold model

FPocket 0.299 · Pocket 34

P2Rank 0.541 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 128 / 4744 genomes with a hit

Prevalence 2.7%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GWU1

Sequence

Primary amino-acid sequence viewer.

MLPLNPEQLARLQAATTDFTPTQLAWVSGYFWGVLNQQSGAAVAAPAPAAEVPTITLISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIAAEKLLVVVTSTQGEGEPPEEAVALHKFLFSKKAPKLDGTAFAVFGLGDTSYEFFCQSGKDFDNKLAELGAERLLDRVDADVEYQAAAAEWRARVVEALKARAPVAAPAQLATSGAVNDIHTSPYTKEAPLTATLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPQLVKELVELLWLKGDEPVTVEGKTLPLSEALQWHFELTVNTATIVENYATLTRSESLLPLVGDKAQLQQYAAATPIVDMVRFSPAQLDAEALIGLLRPLTPRLYSIASSQAEVESEVHVTVGVVRYEIEGRARAGGASSFLADRVEEDGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGAQGKNWLFFGNPHFTEDFLYQVEWQSYVKEGLLTRIDLAWSRDQQQKIYVQDKLREQGAELWRWITDGAHIYVCGDANRMAKDVENTLLEVIAEYGAMDAEAADEFLSELRVERRYQRDVY

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1.8.1.2

Gene Ontology (GO)

GO:0004783 Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+.
GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0019344 The chemical reactions and pathways resulting in the formation of L-cysteine, 2-amino-3-mercaptopropanoic acid.
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:0000103 The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0070814 The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

58 records

Show feature table

Start	End	DB	Term	Name
1	590	Hamap	MF_01541	Sulfite reductase [NADPH] flavoprotein alpha-component [cysJ].
1	590	InterPro	IPR029758	Sulphite reductase [NADPH] flavoprotein, alpha chain, Proteobacteria
271	375	Gene3D	G3DSA:1.20.990.10	-
271	375	InterPro	IPR023173	NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily
51	585	PANTHER	PTHR19384	NITRIC OXIDE SYNTHASE-RELATED
45	210	FunFam	G3DSA:3.40.50.360:FF:000018	Sulfite reductase [NADPH] flavoprotein alpha-component
221	415	Pfam	PF00667	FAD binding domain
221	415	InterPro	IPR003097	Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding
2	590	NCBIfam	TIGR01931	assimilatory sulfite reductase (NADPH) flavoprotein subunit
2	590	InterPro	IPR010199	Sulphite reductase [NADPH] flavoprotein, alpha chain
231	590	CDD	cd06199	SiR
54	200	SUPERFAMILY	SSF52218	Flavoproteins
54	200	InterPro	IPR029039	Flavoprotein-like superfamily
438	590	FunFam	G3DSA:3.40.50.80:FF:000001	NADPH--cytochrome P450 reductase 1
539	547	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
539	547	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
410	419	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
410	419	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
447	466	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
447	466	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
472	481	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
472	481	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
485	496	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
485	496	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
261	271	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
261	271	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
516	532	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
516	532	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
377	384	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
377	384	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
271	375	FunFam	G3DSA:1.20.990.10:FF:000004	Sulfite reductase [NADPH] flavoprotein alpha-component
58	186	Pfam	PF00258	Flavodoxin
58	186	InterPro	IPR008254	Flavodoxin/nitric oxide synthase
225	439	ProSiteProfiles	PS51384	Ferredoxin reductase-type FAD binding domain profile.
225	439	InterPro	IPR017927	FAD-binding domain, ferredoxin reductase-type
448	554	Pfam	PF00175	Oxidoreductase NAD-binding domain
448	554	InterPro	IPR001433	Oxidoreductase FAD/NAD(P)-binding
435	590	SUPERFAMILY	SSF52343	Ferredoxin reductase-like, C-terminal NADP-linked domain
435	590	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
55	193	ProSiteProfiles	PS50902	Flavodoxin-like domain profile.
55	193	InterPro	IPR008254	Flavodoxin/nitric oxide synthase
44	210	Gene3D	G3DSA:3.40.50.360	-
44	210	InterPro	IPR029039	Flavoprotein-like superfamily
436	590	Gene3D	G3DSA:3.40.50.80	-
436	590	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
1	590	PIRSF	PIRSF000207	SiR-FP_CysJ
1	590	InterPro	IPR010199	Sulphite reductase [NADPH] flavoprotein, alpha chain
218	437	SUPERFAMILY	SSF63380	Riboflavin synthase domain-like
218	437	InterPro	IPR017938	Riboflavin synthase-like beta-barrel
224	430	Gene3D	G3DSA:2.40.30.10	Translation factors
160	179	PRINTS	PR00369	Flavodoxin signature
160	179	InterPro	IPR001094	Flavodoxin-like
56	69	PRINTS	PR00369	Flavodoxin signature
56	69	InterPro	IPR001094	Flavodoxin-like
104	115	PRINTS	PR00369	Flavodoxin signature
104	115	InterPro	IPR001094	Flavodoxin-like
136	146	PRINTS	PR00369	Flavodoxin signature
136	146	InterPro	IPR001094	Flavodoxin-like

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #18

0.412

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.614

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Surrounding area

Site 2 P2Rank #2

0.442

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Surrounding area

Site 3 P2Rank #3

0.165

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Surrounding area

Site 4 P2Rank #4

0.136

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Surrounding area

Site 5 P2Rank #5

0.106

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Surrounding area

Residue sets

UniProt: Binding site:108-111

UniProt: Binding site:144-153

UniProt: Binding site:313-313

UniProt: Binding site:347-347

UniProt: Binding site:377-380

UniProt: Binding site:395-397

UniProt: Binding site:401-401

UniProt: Binding site:410-413

UniProt: Binding site:510-511

UniProt: Binding site:516-520

UniProt: Binding site:552-552

UniProt: Binding site:590-590

UniProt: Binding site:61-66

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.541

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Surrounding area

Site 2 P2Rank #2

0.361

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Surrounding area

Site 3 P2Rank #3

0.165

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Surrounding area

Site 4 P2Rank #4

0.112

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Surrounding area

Site 5 P2Rank #5

0.074

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GWU1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02396	ColabFold	—	—	full sequence	—	Loaded

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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2AM PDB via homolog 347.2 Da · LogP -1.86 · TPSA 186.1 Open detail RCSB PDB

A2P PDB via homolog Detail RCSB PDB

CXS PDB via homolog Detail RCSB PDB

EN6 PDB via homolog Detail RCSB PDB

FDA PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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
2AM RCSB PDB	4YAF	P00388	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
A2P RCSB PDB	1FNC	P00455	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CXS RCSB PDB	6EFV	W8SX42	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCCS(=O)(=O)O`
EN6 RCSB PDB	6LI0	P00323	489.5 Da LogP 4.22 TPSA 87.4	✓ Ro5	✓ Clean	`Cc1c(c(n(n1)c2cccc3c2sc(c3)Cc4cccc(c4)C(F)(F)F)…`
FDA RCSB PDB	5VW2	B4G043	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
FLC RCSB PDB	6LI0	P00323	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
NCA RCSB PDB	5VW4	B4G043	122.1 Da LogP 0.18 TPSA 56.0	✓ Ro5	✓ Clean	`c1cc(cnc1)C(=O)N`
OLC RCSB PDB	6LI0	P00323	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](CO)O`
RBF RCSB PDB	1BU5	P00323	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).

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 ZINC	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)…`
ZINC13424932 ZINC	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1…`
ZINC13424933 ZINC	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O…`
ZINC1501016272 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC1501016273 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC1501016315 ZINC	1.000	314.5 Da LogP 3.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC1501016316 ZINC	1.000	314.5 Da LogP 3.75 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC1532585 ZINC	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…`
ZINC1769096 ZINC	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)[…`
ZINC2004372 ZINC	1.000	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC2036187 ZINC	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1OP…`
ZINC2036848 ZINC	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)[…`
ZINC2038077522 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2038077523 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC221534416 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@@H](O)CO`
ZINC32840893 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840894 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840895 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840896 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840901 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840902 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840903 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC32840904 ZINC	1.000	356.5 Da LogP 4.92 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC3650334 ZINC	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 ZINC	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 ZINC	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 ZINC	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…`
ZINC3861741 ZINC	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O…`
ZINC44960119 ZINC	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O…`
ZINC4513863 ZINC	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1…`
ZINC4513866 ZINC	1.000	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC725433050 ZINC	1.000	342.5 Da LogP 4.53 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCC(=O)OC[C@@H](O)CO`
ZINC725433052 ZINC	1.000	342.5 Da LogP 4.53 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCCC(=O)OC[C@H](O)CO`
ZINC98208566 ZINC	1.000	328.5 Da LogP 4.14 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCCCC(=O)OC[C@H](O)CO`
ZINC4353342 ZINC	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 ZINC	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 ZINC	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 ZINC	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…`
ZINC32840885 ZINC	0.943	300.4 Da LogP 3.36 TPSA 66.8	✓ Ro5	✓ Clean	`CCCC/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC38364153 ZINC	0.926	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC2053467566 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC=CCC=CCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC2053467567 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCC=CCC=CCCCCCCCC(=O)OC[C@H](O)CO`
ZINC29045599 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4557100 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@H](O)CO`
ZINC4557101 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC5819989 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC5819990 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C/C/C=C/CCCCCCCC(=O)OC[C@@H](O)CO`
ZINC85425978 ZINC	0.919	354.5 Da LogP 4.70 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C/CCCCCCCC(=O)OC[C@H](O)CO`
ZINC29045446 ZINC	0.892	352.5 Da LogP 4.47 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCC/C=C\C/C=C\C/C=C\CCCCC(=O)OC[C@@H](O)CO`
ZINC79090744 ZINC	0.882	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](OP(=O)(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.