Protein target profile

KP13_03124

Dihydropteroate synthase type-1

Genome: KpKP13 Gene: sul1 AHE47313.1 3D evidence: AlphaFold DB model + ColabFold model UniProt B3VMX3

Export view

Length 279

Pocket druggability 0.923

Direct ligand evidence 0 123 total records

Functional annotation 0 EC 4 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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

Main supporting evidence

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.92, P2Rank 0.95). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Strong predicted binding pocket FPocket selected-pocket score 0.92. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.95. Review the complete evidence below

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: No hit
Gut microbiome similarity: 0.4% 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: Cytoplasmic

Structure confidence

ColabFold pLDDT: 92.71 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 0.923

Structure B3VMX3

Pocket Pocket 6

P2Rank 0.952

Structure B3VMX3

Pocket Pocket 1

ColabFold model

FPocket 0.534 · Pocket 4

P2Rank 0.86 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 19 / 4744 genomes with a hit

Prevalence 0.4%

Cross-references

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

Sequence

UniProt B3VMX3

Chemistry

ChEMBL CHEMBL158543 ChEMBL CHEMBL159139 ChEMBL CHEMBL159048 ChEMBL CHEMBL422884 ChEMBL 08D ChEMBL CHEMBL1109 ChEMBL CHEMBL1191 ChEMBL CHEMBL1200321 ChEMBL CHEMBL1200351 ChEMBL CHEMBL1200359 ChEMBL CHEMBL1200910 ChEMBL CHEMBL1201161 ChEMBL CHEMBL1382627 ChEMBL CHEMBL1525826 ChEMBL CHEMBL1723241 ChEMBL CHEMBL2107253 ChEMBL CHEMBL268869 ChEMBL CHEMBL438 ChEMBL CHEMBL439 ChEMBL CHEMBL446 ChEMBL CHEMBL453 ChEMBL CHEMBL455 ChEMBL CHEMBL58061 ChEMBL CHEMBL62193 ChEMBL SFY ChEMBL YTZ

Sequence

Primary amino-acid sequence viewer.

MVTVFGILNLTEDSFFDESRRLDPAGAVTAAIEMLRVGSDVVDVGPAASHPDARPVSPADEIRRIAPLLDALSDQMHRVSIDSFQPETQRYALKRGVGYLNDIQGFPDPALYPDIAEADCRLVVMHSAQRDGIATRTGHLRPEDALDEIVRFFEARVSALRRSGVAADRLILDPGMGFFLSPAPETSLHVLSNLQKLKSALGLPLLVSVSRKSFLGATVGLPVKDLGPASLAAELHAIGNGADYVRTHAPGDLRSAITFSETLAKFRSRDARDRGLDHA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

GO:0042558 The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
GO:0004156 Catalysis of the reaction: 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.
GO:0009396 The chemical reactions and pathways resulting in the formation of folic acid and its derivatives.
GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
5	248	Pfam	PF00809	Pterin binding enzyme
5	248	InterPro	IPR000489	Pterin-binding domain
38	51	ProSitePatterns	PS00793	Dihydropteroate synthase signature 2.
38	51	InterPro	IPR000489	Pterin-binding domain
2	261	CDD	cd00739	DHPS
2	261	InterPro	IPR006390	Dihydropteroate synthase domain
3	264	PANTHER	PTHR20941	FOLATE SYNTHESIS PROTEINS
3	264	InterPro	IPR045031	Dihydropteroate synthase
1	276	Gene3D	G3DSA:3.20.20.20	-
1	276	InterPro	IPR011005	Dihydropteroate synthase-like
3	265	SUPERFAMILY	SSF51717	Dihydropteroate synthetase-like
3	265	InterPro	IPR011005	Dihydropteroate synthase-like
4	262	NCBIfam	TIGR01496	dihydropteroate synthase
4	262	InterPro	IPR006390	Dihydropteroate synthase domain
4	19	ProSitePatterns	PS00792	Dihydropteroate synthase signature 1.
4	19	InterPro	IPR000489	Pterin-binding domain
2	258	ProSiteProfiles	PS50972	Pterin-binding domain profile.
2	258	InterPro	IPR000489	Pterin-binding domain

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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 #6

0.923

Likely same site as P2Rank 1 3.9 Å 32 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.952

Likely same site as FPocket 6 3.9 Å 32 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.015

Show in viewer

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_B3VMX3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03124	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.

123 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 73 records from similar proteins

Structural ligands 47 0 loaded crystals

Measured bioactivity 26 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0HY PDB via homolog 279.3 Da · LogP -0.74 · TPSA 143.8 Open detail RCSB PDB

0J2 PDB via homolog Detail RCSB PDB

0J4 PDB via homolog Detail RCSB PDB

0J5 PDB via homolog Detail RCSB PDB

22D 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
0HY RCSB PDB	4D8A	Q81VW8	279.3 Da LogP -0.74 TPSA 143.8	✓ Ro5	✓ Clean	`C[C@H](CC(=O)OC)C1=NNC2=C(C1=O)C(=O)NC(=N2)N`
0J2 RCSB PDB	4D8Z	Q81VW8	265.2 Da LogP -0.83 TPSA 154.8	✓ Ro5	✓ Clean	`C[C@H](CC(=O)O)C1=NNC2=C(C1=O)C(=O)NC(=N2)N`
0J4 RCSB PDB	4DAF	Q81VW8	251.2 Da LogP -1.22 TPSA 154.8	✓ Ro5	✓ Clean	`C[C@H](C1=NNC2=C(C1=O)C(=O)NC(=N2)N)C(=O)O`
0J5 RCSB PDB	4DAI	Q81VW8	237.2 Da LogP -1.78 TPSA 154.8	✓ Ro5	✓ Clean	`C(C1=NNC2=C(C1=O)C(=O)NC(=N2)N)C(=O)O`
22D RCSB PDB	6OFW	D2UDM3	312.3 Da LogP 0.61 TPSA 146.9	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)NCc2cnc3c(n2)C(=O)NC(=N3)N`
2O6 RCSB PDB	4NHV	Q81VW8	202.1 Da LogP 2.43 TPSA 52.0	✓ Ro5	✓ Clean	`c1cc2c(cc1C(F)(F)F)c(no2)N`
2O8 RCSB PDB	4NIL	Q81VW8	221.2 Da LogP 2.40 TPSA 43.1	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)N)SC(F)(F)F`
2PH RCSB PDB	1AJ2	P0AC13	355.1 Da LogP -0.92 TPSA 209.4	1 viol.	✓ Clean	`C1C(=NC2=C(N1)N=C(NC2=O)N)CO[P@@](=O)(O)OP(=O)(…`
5RU RCSB PDB	5U12	P0AC13	291.3 Da LogP 1.66 TPSA 100.5	✓ Ro5	✓ Clean	`c1ccc(c(c1)CSc2[nH]c3c(n2)C(=O)NC(=N3)N)F`
680 RCSB PDB	1TX2	Q81VW8	185.1 Da LogP -0.70 TPSA 126.9	✓ Ro5	✓ Clean	`CNC1=C(C(=O)NC(=N1)N)[N+](=O)[O-]`
6DH RCSB PDB	4NIR	Q81VW8	244.2 Da LogP 2.51 TPSA 48.9	✓ Ro5	✓ Clean	`c1cc2c(cc1C(F)(F)F)[nH]c(n2)CCCO`
6GU RCSB PDB	6Q62	D2UDM3	169.6 Da LogP 0.59 TPSA 80.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(nc(n2)N)Cl`
78H RCSB PDB	3TYA	Q81VW8	314.3 Da LogP 0.66 TPSA 145.5	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)NCC2=NC3=C(NC2)N=C(NC3=O)N`
7PJ RCSB PDB	5U0Y	P0AC13	241.2 Da LogP -0.59 TPSA 137.7	✓ Ro5	✓ Clean	`C(C(=O)O)Sc1[nH]c2c(n1)C(=O)NC(=N2)N`
7PM RCSB PDB	5U0Z	P0AC13	317.3 Da LogP 1.15 TPSA 137.7	✓ Ro5	✓ Clean	`c1ccc(cc1)[C@H](C(=O)O)Sc2[nH]c3c(n2)C(=O)NC(=N…`
7PS RCSB PDB	5U11	P0AC13	254.3 Da LogP -0.93 TPSA 129.5	✓ Ro5	✓ Clean	`CNC(=O)CSc1[nH]c2c(n1)C(=O)NC(=N2)N`
7PV RCSB PDB	5U14	P0AC13	366.4 Da LogP 0.21 TPSA 160.6	✓ Ro5	✓ Clean	`c1cc(ccc1CCSc2[nH]c3c(n2)C(=O)NC(=N3)N)S(=O)(=O…`
7VJ RCSB PDB	5U0V	P0AC13	169.1 Da LogP -0.21 TPSA 113.2	✓ Ro5	✓ Clean	`CNC1=C(C(=O)NC(=N1)N)N=O`
8Y4 RCSB PDB	5V79	P0AC13	330.4 Da LogP 0.97 TPSA 118.7	✓ Ro5	✓ Clean	`Cn1c2c(nc1SCC(=O)Nc3ccccc3)C(=O)NC(=N2)N`
8Y7 RCSB PDB	5V7A	P0AC13	255.3 Da LogP -0.58 TPSA 126.9	✓ Ro5	✓ Clean	`Cn1c2c(nc1SCC(=O)O)C(=O)NC(=N2)N`
9MG RCSB PDB	5U0W	P0AC13	165.2 Da LogP -0.35 TPSA 89.8	✓ Ro5	✓ Clean	`Cn1cnc2c1nc(nc2O)N`
B52 RCSB PDB	3H21	Q81VW8	265.2 Da LogP -1.21 TPSA 144.0	✓ Ro5	✓ Clean	`C[C@H](C1=NN(C2=C(C1=O)C(=O)NC(=N2)N)C)C(=O)O`
B53 RCSB PDB	3H22	Q81VW8	155.1 Da LogP -0.67 TPSA 127.2	✓ Ro5	✓ Clean	`C1(=C(N=C(NC1=O)N)N)N=O`
B54 RCSB PDB	3H23	Q81VW8	333.3 Da LogP 1.33 TPSA 159.8	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)OCCCNC2=C(C(=O)NC(=N2)N)N=O`
B55 RCSB PDB	3H24	Q81VW8	183.2 Da LogP -0.48 TPSA 100.5	✓ Ro5	✓ Clean	`c12c([nH]c(n1)S)N=C(NC2=O)N`
B56 RCSB PDB	3H26	Q81VW8	223.2 Da LogP -1.04 TPSA 124.7	✓ Ro5	✓ Clean	`CN1CC(=NC2=C1N=C(NC2=O)N)C(=O)O`
B57 RCSB PDB	3H2A	Q81VW8	171.1 Da LogP -1.16 TPSA 140.9	✓ Ro5	✓ Clean	`C1(=C(N=C(NC1=O)N)N)[N+](=O)[O-]`
B58 RCSB PDB	3H2C	Q81VW8	150.1 Da LogP -0.48 TPSA 106.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(nnc2N)N`
B59 RCSB PDB	3H2E	Q81VW8	236.2 Da LogP -1.87 TPSA 106.8	✓ Ro5	✓ Clean	`CN1C2=C(C(=O)N(C1=O)C)N=C(C(=O)N2)C=O`
B60 RCSB PDB	3H2F	Q81VW8	179.2 Da LogP -0.50 TPSA 87.4	✓ Ro5	✓ Clean	`CN1CC=NC2=C1N=C(NC2=O)N`
B61 RCSB PDB	3H2M	Q81VW8	251.3 Da LogP 0.04 TPSA 107.6	✓ Ro5	✓ Clean	`CC(C)(CC1=NC2=C(N=C(NC2=O)N)N(C1)C)O`
B62 RCSB PDB	3H2N	Q81VW8	181.2 Da LogP -0.42 TPSA 95.8	✓ Ro5	✓ Clean	`C[C@@H]1CNC2=C(N1)C(=O)NC(=N2)N`
B63 RCSB PDB	3H2O	Q81VW8	328.3 Da LogP 1.05 TPSA 145.5	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)NCCC2=NC3=C(NC2)N=C(NC3=O)N`
HH2 RCSB PDB	2DZB	Q5SLV2	353.1 Da LogP -0.98 TPSA 210.8	✓ Ro5	✓ Clean	`c1c(nc2c(n1)N=C(NC2=O)N)CO[P@](=O)(O)OP(=O)(O)O`
ICB RCSB PDB	6Q62	D2UDM3	161.2 Da LogP 1.87 TPSA 53.1	✓ Ro5	✓ Clean	`c1ccc2c(c1)cc([nH]2)C(=O)O`
PAB RCSB PDB	2DZA	Q5SLV2	137.1 Da LogP 0.97 TPSA 63.3	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)N`
PH2 RCSB PDB	1AJ0	P0AC13	195.2 Da LogP -1.16 TPSA 116.4	✓ Ro5	✓ Clean	`C1C(=NC2=C(N1)N=C(NC2=O)N)CO`
PHB RCSB PDB	3TYB	Q81VW8	138.1 Da LogP 1.09 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)O`
PMM RCSB PDB	1EYE	P9WND1	273.1 Da LogP -1.10 TPSA 164.3	✓ Ro5	✓ Clean	`c1c(nc2c(n1)N=C(NC2=O)N)COP(=O)(O)O`
POP RCSB PDB	3TYD	Q81VW8	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
SAN RCSB PDB	1AJ0	P0AC13	172.2 Da LogP -0.08 TPSA 86.2	✓ Ro5	✓ Clean	`c1cc(ccc1N)S(=O)(=O)N`
XHP RCSB PDB	3TYB	Q81VW8	177.2 Da LogP -1.88 TPSA 96.5	✓ Ro5	✓ Clean	`C=C1CN=C2C(=N1)C(=O)NC(=N2)N`
XTZ RCSB PDB	3TYE	Q81VW8	432.5 Da LogP 1.22 TPSA 167.2	✓ Ro5	✓ Clean	`c1cc(ccc1NCC2=NC3=C(NC2)N=C(NC3=O)N)S(=O)(=O)Nc…`
YH5 RCSB PDB	5U13	P0AC13	331.4 Da LogP 1.21 TPSA 126.8	✓ Ro5	✓ Clean	`COc1ccc(cc1)C(=O)CSc2[nH]c3c(n2)C(=O)NC(=N3)N`
Z13 RCSB PDB	4NL1	Q81VW8	331.3 Da LogP 5.34 TPSA 12.4	1 viol.	✓ Clean	`c1cc(ccc1CN=Cc2ccc(cc2)C(F)(F)F)C(F)(F)F`
Z17 RCSB PDB	4D9P	Q81VW8	279.3 Da LogP -0.82 TPSA 144.0	✓ Ro5	✓ Clean	`C[C@H](CC(=O)O)C1=NN(C2=C(C1=O)C(=O)NC(=N2)N)C`
Z25 RCSB PDB	4DB7	Q81VW8	251.2 Da LogP -1.39 TPSA 154.8	✓ Ro5	✓ Clean	`C(CC(=O)O)C1=NNC2=C(C1=O)C(=O)NC(=N2)N`

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
CHEMBL158543 ChEMBL	P0AC13	6.22 ~602.6 nM	458.5 Da LogP 3.15 TPSA 168.9	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)Nc2ccc(OCCCNc3nc(N)nc(O)c3N=O)c…`
CHEMBL159139 ChEMBL	P0AC13	6.16 ~691.8 nM	349.3 Da LogP 2.06 TPSA 141.2	✓ Ro5	✓ Clean	`COc1cc(OC)cc(OCCCNc2nc(N)nc(O)c2N=O)c1`
CHEMBL159048 ChEMBL	P0AC13	6.00 ~1.0 µM	334.3 Da LogP 1.95 TPSA 165.9	✓ Ro5	✓ Clean	`Nc1nc(O)c(N=O)c(NCCCOc2ccc([N+](=O)[O-])cc2)n1`
CHEMBL422884 ChEMBL	P0AC13	6.00 ~1.0 µM	323.7 Da LogP 2.70 TPSA 122.7	✓ Ro5	✓ Clean	`Nc1nc(O)c(N=O)c(NCCCOc2ccc(Cl)cc2)n1`
08D ChEMBL	P0AC13	—	253.3 Da LogP 1.37 TPSA 98.2	✓ Ro5	✓ Clean	`Cc1cc(no1)NS(=O)(=O)c2ccc(cc2)N`
CHEMBL1109 ChEMBL	P0AC13	—	314.4 Da LogP 2.26 TPSA 90.0	✓ Ro5	✓ Clean	`Nc1ccc(S(=O)(=O)Nc2ccnn2-c2ccccc2)cc1`
CHEMBL1191 ChEMBL	P0AC13	—	270.3 Da LogP 1.23 TPSA 98.0	✓ Ro5	✓ Clean	`Cc1nnc(NS(=O)(=O)c2ccc(N)cc2)s1`
CHEMBL1200321 ChEMBL	P0AC13	—	372.4 Da LogP 0.24 TPSA 150.7	✓ Ro5	✓ Clean	`Cc1noc(NS(=O)(=O)c2ccc(N)cc2)c1C.OCCNCCO`
CHEMBL1200351 ChEMBL	P0AC13	—	272.3 Da LogP -1.54 TPSA 100.0	✓ Ro5	✓ Clean	`Nc1ccc(S(=O)(=O)[N-]c2ncccn2)cc1.[Na+]`
CHEMBL1200359 ChEMBL	P0AC13	—	280.3 Da LogP 0.87 TPSA 107.2	✓ Ro5	✓ Clean	`COc1cnc(NS(=O)(=O)c2ccc(N)cc2)nc1`
CHEMBL1200910 ChEMBL	P0AC13	—	309.3 Da LogP 1.62 TPSA 106.5	✓ Ro5	✓ Clean	`CC(=O)N(c1onc(C)c1C)S(=O)(=O)c1ccc(N)cc1`
CHEMBL1201161 ChEMBL	P0AC13	—	246.3 Da LogP -0.12 TPSA 123.5	✓ Ro5	✓ Clean	`CC(=O)O.NCc1ccc(S(N)(=O)=O)cc1`
CHEMBL1382627 ChEMBL	P0AC13	—	357.1 Da LogP 1.45 TPSA 100.0	✓ Ro5	✓ Clean	`Nc1ccc(S(=O)(=O)[N-]c2ncccn2)cc1.[Ag+]`
CHEMBL1525826 ChEMBL	P0AC13	—	280.3 Da LogP 0.87 TPSA 107.2	✓ Ro5	✓ Clean	`COc1nccnc1NS(=O)(=O)c1ccc(N)cc1`
CHEMBL1723241 ChEMBL	P0AC13	—	254.2 Da LogP -2.94 TPSA 122.8	✓ Ro5	✓ Clean	`CC(=O)[N-]S(=O)(=O)c1ccc(N)cc1.O.[Na+]`
CHEMBL2107253 ChEMBL	P0AC13	—	332.3 Da LogP -1.53 TPSA 118.5	✓ Ro5	✓ Clean	`COc1cc([N-]S(=O)(=O)c2ccc(N)cc2)nc(OC)n1.[Na+]`
CHEMBL268869 ChEMBL	P0AC13	—	280.3 Da LogP 0.87 TPSA 107.2	✓ Ro5	✓ Clean	`COc1ccc(NS(=O)(=O)c2ccc(N)cc2)nn1`
CHEMBL438 ChEMBL	P0AC13	—	264.3 Da LogP 1.17 TPSA 98.0	✓ Ro5	✓ Clean	`Cc1ccnc(NS(=O)(=O)c2ccc(N)cc2)n1`
CHEMBL439 ChEMBL	P0AC13	—	250.3 Da LogP 0.86 TPSA 98.0	✓ Ro5	✓ Clean	`Nc1ccc(S(=O)(=O)Nc2ncccn2)cc1`
CHEMBL446 ChEMBL	P0AC13	—	278.3 Da LogP 1.48 TPSA 98.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NS(=O)(=O)c2ccc(N)cc2)n1`
CHEMBL453 ChEMBL	P0AC13	—	267.3 Da LogP 1.67 TPSA 98.2	✓ Ro5	✓ Clean	`Cc1noc(NS(=O)(=O)c2ccc(N)cc2)c1C`
CHEMBL455 ChEMBL	P0AC13	—	214.2 Da LogP 0.09 TPSA 89.3	✓ Ro5	✓ Clean	`CC(=O)NS(=O)(=O)c1ccc(N)cc1`
CHEMBL58061 ChEMBL	P0AC13	—	543.6 Da LogP 2.62 TPSA 203.7	2 viol.	✓ Clean	`COc1cc(Cc2cnc(N)nc2N)cc(OC)c1OC.Cc1cc(NS(=O)(=O…`
CHEMBL62193 ChEMBL	P0AC13	—	310.3 Da LogP 0.88 TPSA 116.4	✓ Ro5	✓ Clean	`COc1cc(NS(=O)(=O)c2ccc(N)cc2)nc(OC)n1`
SFY ChEMBL	P0AC13	—	249.3 Da LogP 1.46 TPSA 85.1	✓ Ro5	✓ Clean	`c1ccnc(c1)NS(=O)(=O)c2ccc(cc2)N`
YTZ ChEMBL	P0AC13	—	255.3 Da LogP 1.53 TPSA 85.1	✓ Ro5	✓ Clean	`c1cc(ccc1N)S(=O)(=O)Nc2nccs2`

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
ZINC121458 ZINC	1.000	255.3 Da LogP 1.53 TPSA 85.1	✓ Ro5	✓ Clean	`Nc1ccc(S(=O)(=O)Nc2nccs2)cc1`
ZINC2114 ZINC	1.000	309.3 Da LogP 1.62 TPSA 106.5	✓ Ro5	✓ Clean	`CC(=O)N(c1onc(C)c1C)S(=O)(=O)c1ccc(N)cc1`
ZINC3306788 ZINC	1.000	221.2 Da LogP 2.40 TPSA 43.1	✓ Ro5	✓ Clean	`NC(=O)c1ccc(SC(F)(F)F)cc1`
ZINC39470954 ZINC	1.000	202.1 Da LogP 2.43 TPSA 52.0	✓ Ro5	✓ Clean	`Nc1noc2ccc(C(F)(F)F)cc12`
ZINC5502659 ZINC	1.000	223.2 Da LogP -1.04 TPSA 124.7	✓ Ro5	✓ Clean	`CN1CC(C(=O)O)=Nc2c1nc(N)[nH]c2=O`
ZINC6628789 ZINC	1.000	312.3 Da LogP 0.61 TPSA 146.9	✓ Ro5	✓ Clean	`Nc1nc2ncc(CNc3ccc(C(=O)O)cc3)nc2c(=O)[nH]1`
ZINC1245666585 ZINC	0.850	289.3 Da LogP 4.30 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(-c2ccc(-c3ccc(C(=O)O)cc3)cc2)cc1`
ZINC1746121 ZINC	0.850	213.2 Da LogP 2.63 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(-c2ccc(C(=O)O)cc2)cc1`
ZINC22018837 ZINC	0.850	241.2 Da LogP 2.20 TPSA 80.4	✓ Ro5	✓ Clean	`Nc1ccc(C(=O)c2ccc(C(=O)O)cc2)cc1`
ZINC4823107 ZINC	0.824	328.3 Da LogP 1.05 TPSA 145.5	✓ Ro5	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N=C(CCNc1ccc(C(=O)O)cc1)CN2`
ZINC4243182 ZINC	0.795	244.2 Da LogP 2.51 TPSA 48.9	✓ Ro5	✓ Clean	`OCCCc1nc2cc(C(F)(F)F)ccc2[nH]1`
ZINC90951 ZINC	0.771	252.3 Da LogP 2.09 TPSA 72.2	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)Nc2cc(C)on2)cc1`
ZINC12970896 ZINC	0.765	236.3 Da LogP -1.02 TPSA 120.3	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(S(N)(=O)=O)cc1`
ZINC39075364 ZINC	0.750	202.1 Da LogP 2.43 TPSA 52.0	✓ Ro5	✓ Clean	`Nc1noc2cc(C(F)(F)F)ccc12`
ZINC74936874 ZINC	0.750	316.4 Da LogP 1.19 TPSA 106.3	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2ccc(S(C)(=O)=O)cc2)no1`
ZINC100412109 ZINC	0.739	241.3 Da LogP 3.38 TPSA 88.0	✓ Ro5	Alert	`Nc1ccc(/N=N\c2ccc(C(=O)O)cc2)cc1`
ZINC113407075 ZINC	0.739	237.3 Da LogP 2.37 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(C#Cc2ccc(C(=O)O)cc2)cc1`
ZINC127654 ZINC	0.739	229.2 Da LogP 2.76 TPSA 72.5	✓ Ro5	Alert	`Nc1ccc(Oc2ccc(C(=O)O)cc2)cc1`
ZINC1628139 ZINC	0.739	239.3 Da LogP 3.14 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(/C=C/c2ccc(C(=O)O)cc2)cc1`
ZINC17285708 ZINC	0.739	239.3 Da LogP 3.14 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(/C=C\c2ccc(C(=O)O)cc2)cc1`
ZINC17322332 ZINC	0.739	241.3 Da LogP 3.38 TPSA 88.0	✓ Ro5	Alert	`Nc1ccc(N=Nc2ccc(C(=O)O)cc2)cc1`
ZINC1750451 ZINC	0.739	227.3 Da LogP 2.56 TPSA 63.3	✓ Ro5	Alert	`Nc1ccc(Cc2ccc(C(=O)O)cc2)cc1`
ZINC4707411 ZINC	0.739	241.3 Da LogP 3.38 TPSA 88.0	✓ Ro5	Alert	`Nc1ccc(/N=N/c2ccc(C(=O)O)cc2)cc1`
ZINC116196 ZINC	0.730	256.3 Da LogP 1.92 TPSA 72.2	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2ccc(F)cc2)no1`
ZINC31021 ZINC	0.730	317.2 Da LogP 2.55 TPSA 72.2	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2ccc(Br)cc2)no1`
ZINC35354342 ZINC	0.730	270.3 Da LogP 1.23 TPSA 97.1	✓ Ro5	✓ Clean	`NNc1ccc(S(=O)(=O)Nc2nccs2)cc1`
ZINC90945 ZINC	0.730	272.7 Da LogP 2.44 TPSA 72.2	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2ccc(Cl)cc2)no1`
ZINC11615790 ZINC	0.727	388.4 Da LogP 0.67 TPSA 136.6	✓ Ro5	✓ Clean	`COc1cc(NS(=O)(=O)c2ccc(NS(C)(=O)=O)cc2)nc(OC)n1`
ZINC7948924 ZINC	0.727	340.3 Da LogP 3.65 TPSA 72.2	✓ Ro5	✓ Clean	`NC(=O)c1ccc(NC(=O)c2ccc(SC(F)(F)F)cc2)cc1`
ZINC1641309 ZINC	0.722	256.3 Da LogP 1.65 TPSA 79.3	✓ Ro5	✓ Clean	`O=S(=O)(Nc1nccs1)c1ccc(O)cc1`
ZINC1662550 ZINC	0.722	254.3 Da LogP 2.25 TPSA 59.1	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)Nc2nccs2)cc1`
ZINC1739302 ZINC	0.722	274.8 Da LogP 2.60 TPSA 59.1	✓ Ro5	✓ Clean	`O=S(=O)(Nc1nccs1)c1ccc(Cl)cc1`
ZINC191309 ZINC	0.722	238.3 Da LogP 1.78 TPSA 72.2	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2ccccc2)no1`
ZINC29871 ZINC	0.722	319.2 Da LogP 2.71 TPSA 59.1	✓ Ro5	✓ Clean	`O=S(=O)(Nc1nccs1)c1ccc(Br)cc1`
ZINC39783 ZINC	0.722	258.3 Da LogP 2.08 TPSA 59.1	✓ Ro5	✓ Clean	`O=S(=O)(Nc1nccs1)c1ccc(F)cc1`
ZINC65554816 ZINC	0.722	318.4 Da LogP 1.35 TPSA 93.2	✓ Ro5	✓ Clean	`CS(=O)(=O)c1ccc(S(=O)(=O)Nc2nccs2)cc1`
ZINC682328 ZINC	0.722	366.2 Da LogP 2.55 TPSA 59.1	✓ Ro5	✓ Clean	`O=S(=O)(Nc1nccs1)c1ccc(I)cc1`
ZINC4228265 ZINC	0.721	443.4 Da LogP 0.01 TPSA 211.9	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N=C(CNc1ccc(C(=O)N[C@@H](CCC…`
ZINC4517559 ZINC	0.721	443.4 Da LogP 0.01 TPSA 211.9	1 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N=C(CNc1ccc(C(=O)N[C@H](CCC(…`
ZINC22223556 ZINC	0.718	253.3 Da LogP 1.37 TPSA 98.2	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2cccc(N)c2)no1`
ZINC116166 ZINC	0.714	297.8 Da LogP 2.55 TPSA 72.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NS(=O)(=O)c2ccc(Cl)cc2)n1`
ZINC116233 ZINC	0.714	342.2 Da LogP 2.66 TPSA 72.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NS(=O)(=O)c2ccc(Br)cc2)n1`
ZINC12477663 ZINC	0.714	240.3 Da LogP 1.94 TPSA 59.1	✓ Ro5	✓ Clean	`O=S(=O)(Nc1nccs1)c1ccccc1`
ZINC30986 ZINC	0.714	281.3 Da LogP 2.03 TPSA 72.0	✓ Ro5	✓ Clean	`Cc1cc(C)nc(NS(=O)(=O)c2ccc(F)cc2)n1`
ZINC1655608 ZINC	0.711	337.4 Da LogP 1.50 TPSA 107.5	✓ Ro5	✓ Clean	`COc1cc(NS(=O)(=O)c2ccc(C(C)=O)cc2)nc(OC)n1`
ZINC2182515 ZINC	0.711	450.5 Da LogP 2.10 TPSA 136.6	✓ Ro5	✓ Clean	`COc1cc(NS(=O)(=O)c2ccc(NS(=O)(=O)c3ccccc3)cc2)n…`
ZINC2500430 ZINC	0.711	464.5 Da LogP 2.40 TPSA 136.6	✓ Ro5	✓ Clean	`COc1cc(NS(=O)(=O)c2ccc(NS(=O)(=O)c3ccc(C)cc3)cc…`
ZINC4775653 ZINC	0.711	267.3 Da LogP 2.43 TPSA 87.2	✓ Ro5	✓ Clean	`N#[N+]c1ccc(S(=O)(=O)Nc2nccs2)cc1`
ZINC68374 ZINC	0.711	268.3 Da LogP 1.79 TPSA 81.4	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)Nc2cc(C)on2)cc1`
ZINC91187 ZINC	0.711	294.4 Da LogP 3.08 TPSA 72.2	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2ccc(C(C)(C)C)cc2)no1`

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.