KpATCC43816 Protein target profile

arylsulfatase

Accession: VK055_2016

Gene: atsA AIK80622.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GKX6

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Length 577

Pocket druggability (P2Rank · AlphaFold DB model) 0.951

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 57 total records

Functional annotation 0 EC 3 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.95, FPocket 0.78). Use the 3D pocket comparison to verify whether they identify the same site. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.78. This is a computational pocket signal, not binding validation. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 41.379 Lower values reduce human off-target concern.
Human E-value: 1.56e-10
Gut microbiome similarity: 0.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 26.799 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 90.9 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.951

Structure A0A0H3GKX6

Pocket Pocket 1

Druggability (FPocket) 0.784

Structure A0A0H3GKX6

Pocket Pocket 1

ColabFold model

P2Rank 0.954 · Pocket 1

FPocket 0.395 · Pocket 30

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 10 / 4744 genomes with a hit

Prevalence 0.2%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MNKKAMAAAVSMILAGGAHAAQQERPNVIVIIADDMGYSDISPFGGEIPTPNLQAMAEQGMRMSQYYTSPMSAPARSMLLTGNSNQQAGMGGMWWYDSTIGKEGYELRLTDRVTTMAERFKDAGYNTLMAGKWHLGFVPGATPKDRGFNHAFAFMGGGTSHFNDAIPLGTVEAFHTYYTRDGERVSLPDDFYSSEAYARQMNSWIKATPKEQPVFAWLAFTAPHDPLQAPDEWIKRFKGQYEQGYAEVYRQRIARLKALGIIHDDTPLPHLELDKEWEALTPEQQKYTAKVMQVYAAMIANMDAQIGTLMETLKQTGRDKNTLLVFLTDNGANPAQGFYYESTPEFWKQFDNSYDNVGRKGSFVSYGPHWANVSNAPYANYHKTTSAQGGINTDFMISGPGITRHGKIDASTMAVYDVAPTLYEFAGIDPNKSLAKKPVLPMIGVSFKRYLTGEVQEPPRGNYGVELHHQAAWVDGEWKLRRLVPRGLTAGDAPWQLFNLHDDPLETHDVAAEHPDRVKAMSEAYEAFAKRTMVTKAQGKMIDYVGIDSKTGRYLAVDPATMKPVPAPQAIPVSEIH

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Subcellular localization

Localization: Unknown

Gene Ontology (GO)

GO:0008484 Catalysis of the reaction: RSO-R' + H2O = RSOOH + R'H. This reaction is the hydrolysis of a sulfuric ester bond, an ester formed from sulfuric acid, O=SO(OH)2.
GO:0004065 Catalysis of the reaction: a phenol sulfate + H2O = a phenol + sulfate.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
24	510	CDD	cd16025	PAS_like
1	20	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	20	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
7	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
70	82	ProSitePatterns	PS00523	Sulfatases signature 1.
70	82	InterPro	IPR024607	Sulfatase, conserved site
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
21	577	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
11	536	PANTHER	PTHR42693	ARYLSULFATASE FAMILY MEMBER
26	428	Pfam	PF00884	Sulfatase
26	428	InterPro	IPR000917	Sulfatase, N-terminal
124	134	ProSitePatterns	PS00149	Sulfatases signature 2.
124	134	InterPro	IPR024607	Sulfatase, conserved site
24	532	SUPERFAMILY	SSF53649	Alkaline phosphatase-like
24	532	InterPro	IPR017850	Alkaline-phosphatase-like, core domain superfamily
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
459	542	Gene3D	G3DSA:3.30.1120.10	-
23	456	Gene3D	G3DSA:3.40.720.10	Alkaline Phosphatase, subunit A
23	456	InterPro	IPR017850	Alkaline-phosphatase-like, core domain superfamily

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.951

Likely same site as FPocket 1 0.7 Å 25 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.314

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Surrounding area

Pocket 3 P2Rank #3

0.075

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Surrounding area

Pocket 4 P2Rank #4

0.069

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Surrounding area

Pocket 5 P2Rank #5

0.067

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1

0.784

Likely same site as P2Rank 1 0.7 Å 25 shared residues 96% of smaller site

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Surrounding area

Pocket 2 FPocket #2

0.298

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.954

Likely same site as FPocket 30 7.0 Å 19 shared residues 68% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.306

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Surrounding area

Pocket 3 P2Rank #3

0.109

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Surrounding area

Pocket 4 P2Rank #4

0.099

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Surrounding area

Pocket 5 P2Rank #5

0.062

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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_A0A0H3GKX6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2016	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.

57 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

62Y PDB via homolog 313.1 Da · LogP 3.34 · TPSA 46.5 Open detail RCSB PDB

CHT PDB via homolog Detail RCSB PDB

DDZ PDB via homolog Detail RCSB PDB

NH4 PDB via homolog Detail RCSB PDB

SV7 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
62Y RCSB PDB	4CXU	P51691	313.1 Da LogP 3.34 TPSA 46.5	✓ Ro5	✓ Clean	`c1ccc(cc1)P(=O)(O)Oc2cccc(c2)Br`
CHT RCSB PDB	6G60	O69787	104.2 Da LogP -0.32 TPSA 20.2	✓ Ro5	✓ Clean	`C[N+](C)(C)CCO`
DDZ RCSB PDB	6G60	O69787	121.1 Da LogP -2.29 TPSA 103.8	✓ Ro5	✓ Clean	`[C@H](C(O)O)(C(=O)O)N`
NH4 RCSB PDB	4CYS	P51691	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
SV7 RCSB PDB	4CXS	P51691	158.1 Da LogP 0.49 TPSA 57.5	✓ Ro5	✓ Clean	`c1ccc(cc1)P(=O)(O)O`

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
CHEMBL283560 ChEMBL	P51691	6.89 ~128.8 nM	218.2 Da LogP 0.18 TPSA 112.5	✓ Ro5	✓ Clean	`NS(=O)(=O)Oc1cccc([N+](=O)[O-])c1`
DME ChEMBL	P15289	—	258.5 Da LogP 3.52 TPSA 0.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCCCCCCCCC[N+](C)(C)C`

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
ZINC1530808 ZINC	1.000	202.4 Da LogP 1.96 TPSA 0.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCCCCC[N+](C)(C)C`
ZINC1532339 ZINC	1.000	258.5 Da LogP 3.52 TPSA 0.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCCCCCCCCC[N+](C)(C)C`
ZINC1730254 ZINC	1.000	216.4 Da LogP 2.35 TPSA 0.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCCCCCC[N+](C)(C)C`
ZINC1730255 ZINC	1.000	230.4 Da LogP 2.74 TPSA 0.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCCCCCCC[N+](C)(C)C`
ZINC1730256 ZINC	1.000	244.5 Da LogP 3.13 TPSA 0.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCCCCCCCC[N+](C)(C)C`
ZINC1673414 ZINC	0.733	228.4 Da LogP 4.61 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)C`
ZINC1700269 ZINC	0.733	200.4 Da LogP 3.83 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)C`
ZINC2566335 ZINC	0.706	238.1 Da LogP -0.71 TPSA 115.1	✓ Ro5	✓ Clean	`O=P(O)(O)c1ccc(P(=O)(O)O)cc1`
ZINC40880076 ZINC	0.688	246.5 Da LogP 4.13 TPSA 0.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCCCCCCCCCCS`
ZINC1621972 ZINC	0.677	234.2 Da LogP 2.58 TPSA 46.5	✓ Ro5	✓ Clean	`O=[P@](O)(Oc1ccccc1)c1ccccc1`
ZINC20095926 ZINC	0.677	260.2 Da LogP 3.30 TPSA 95.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(Oc2cccc([N+](=O)[O-])c2)c1`
ZINC145086558 ZINC	0.650	238.1 Da LogP -0.71 TPSA 115.1	✓ Ro5	✓ Clean	`O=P(O)(O)c1cccc(P(=O)(O)O)c1`
ZINC1599347 ZINC	0.649	279.3 Da LogP 2.36 TPSA 86.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(OS(=O)(=O)c2ccccc2)c1`
ZINC13440981 ZINC	0.636	218.2 Da LogP 0.18 TPSA 112.5	✓ Ro5	✓ Clean	`NS(=O)(=O)Oc1ccc([N+](=O)[O-])cc1`
ZINC1725599 ZINC	0.625	250.2 Da LogP 2.28 TPSA 66.8	✓ Ro5	✓ Clean	`O=P(O)(O)c1ccc(Oc2ccccc2)cc1`
ZINC1667490 ZINC	0.618	215.2 Da LogP 3.39 TPSA 52.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(Oc2ccccc2)c1`
ZINC1867065 ZINC	0.615	293.3 Da LogP 2.67 TPSA 86.5	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)Oc2cccc([N+](=O)[O-])c2)cc1`
ZINC195784618 ZINC	0.611	216.5 Da LogP 3.59 TPSA 0.0	✓ Ro5	✓ Clean	`C[N+](C)(C)CCCCCC[Si](C)(C)C`
ZINC15415840 ZINC	0.600	286.3 Da LogP 1.70 TPSA 89.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(OS(=O)(=O)N2CCCCC2)c1`
ZINC1677207 ZINC	0.600	260.2 Da LogP 3.30 TPSA 95.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Oc2cccc([N+](=O)[O-])c2)cc1`
ZINC1870275 ZINC	0.600	314.2 Da LogP 0.96 TPSA 115.1	✓ Ro5	✓ Clean	`O=P(O)(O)c1ccc(-c2ccc(P(=O)(O)O)cc2)cc1`
ZINC1569727 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC1569728 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@@H](C)C(=O)O`
ZINC1569729 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC1569730 ZINC	0.593	202.3 Da LogP -0.05 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](C)C(=O)O`
ZINC1600154 ZINC	0.591	310.2 Da LogP 2.18 TPSA 74.6	✓ Ro5	✓ Clean	`O=[P@](O)(CC[P@](=O)(O)c1ccccc1)c1ccccc1`
ZINC295906 ZINC	0.591	296.2 Da LogP 2.14 TPSA 74.6	✓ Ro5	✓ Clean	`O=[P@](O)(C[P@](=O)(O)c1ccccc1)c1ccccc1`
ZINC8034715 ZINC	0.591	298.2 Da LogP 2.02 TPSA 83.8	✓ Ro5	✓ Clean	`O=[P@](O)(O[P@](=O)(O)c1ccccc1)c1ccccc1`
ZINC2522597 ZINC	0.586	246.3 Da LogP -0.60 TPSA 129.7	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC16091748 ZINC	0.585	338.3 Da LogP 2.58 TPSA 129.7	✓ Ro5	✓ Clean	`Cc1ccc([N+](=O)[O-])cc1S(=O)(=O)Oc1cccc([N+](=O…`
ZINC25398729 ZINC	0.585	338.3 Da LogP 1.70 TPSA 121.8	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(OCCOc2cccc([N+](=O)[O-])c2)cc1`
ZINC60377679 ZINC	0.585	273.3 Da LogP 2.35 TPSA 86.5	✓ Ro5	✓ Clean	`CC(C)CCS(=O)(=O)Oc1cccc([N+](=O)[O-])c1`
ZINC112977758 ZINC	0.579	244.5 Da LogP 3.13 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCC[N+](C)(C)CCC[N+](C)(C)C`
ZINC1532219 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)O`
ZINC1532220 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](NC(=O)[C@H](N)CC(C)C)C(=O)O`
ZINC1532221 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC1532222 ZINC	0.571	244.3 Da LogP 0.98 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](CC(C)C)C(=O)O`
ZINC1704133 ZINC	0.571	304.3 Da LogP 2.96 TPSA 104.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(OCCOc2cccc([N+](=O)[O-])c2)c1`
ZINC4262218 ZINC	0.571	202.2 Da LogP 0.24 TPSA 103.3	✓ Ro5	✓ Clean	`NS(=O)(=O)c1cccc([N+](=O)[O-])c1`
ZINC7616193 ZINC	0.571	288.3 Da LogP 0.55 TPSA 99.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(OS(=O)(=O)N2CCOCC2)c1`
ZINC100172862 ZINC	0.568	305.2 Da LogP 3.20 TPSA 138.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(Oc2c([N+](=O)[O-])cccc2[N+](…`
ZINC141670423 ZINC	0.568	229.2 Da LogP 3.70 TPSA 52.4	✓ Ro5	✓ Clean	`Cc1cccc(Oc2cccc([N+](=O)[O-])c2)c1`
ZINC2065201 ZINC	0.568	480.4 Da LogP 3.04 TPSA 173.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(S(=O)(=O)Oc2cccc(OS(=O)(=O)c3…`
ZINC261493776 ZINC	0.568	233.2 Da LogP 3.53 TPSA 52.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(Oc2cccc(F)c2)c1`
ZINC1591869 ZINC	0.565	202.1 Da LogP 0.19 TPSA 94.8	✓ Ro5	✓ Clean	`O=C(O)c1ccc(P(=O)(O)O)cc1`
ZINC16091754 ZINC	0.558	315.3 Da LogP 2.64 TPSA 86.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(OS(=O)(=O)c2ccc(F)cc2F)c1`
ZINC69871241 ZINC	0.558	323.3 Da LogP 2.51 TPSA 95.7	✓ Ro5	✓ Clean	`COc1cccc(CS(=O)(=O)Oc2cccc([N+](=O)[O-])c2)c1`
ZINC1704134 ZINC	0.556	318.3 Da LogP 3.35 TPSA 104.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(OCCCOc2cccc([N+](=O)[O-])c2)…`
ZINC1870276 ZINC	0.556	250.2 Da LogP 2.28 TPSA 66.8	✓ Ro5	✓ Clean	`O=P(O)(O)c1cccc(Oc2ccccc2)c1`
ZINC137500004 ZINC	0.553	249.7 Da LogP 4.04 TPSA 52.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(Oc2ccc(Cl)cc2)c1`

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.

Cross-references

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

arylsulfatase

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways