KpATCC43816 Protein target profile

DNA topoisomerase IV, B subunit

Accession: VK055_4030

Gene: parE AIK82577.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3H365

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Length 631

Pocket druggability (P2Rank · AlphaFold DB model) 0.816

Direct ligand evidence 0 88 total records

Functional annotation 0 EC 5 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.82, FPocket 0.80). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.80. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.82. 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 (%): 24.696 Lower values reduce human off-target concern.
Human E-value: 4.83e-31
Gut microbiome similarity: 4.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 94.929 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 87.98 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) 0.816

Structure A0A0H3H365

Pocket Pocket 1

Druggability (FPocket) 0.795

Structure A0A0H3H365

Pocket Pocket 3

ColabFold model

P2Rank 0.886 · Pocket 1

FPocket 0.487 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 194 / 4744 genomes with a hit

Prevalence 4.1%

Metabolic context

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

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTQSSYNADAIEVLTGLEPVRRRPGMYTDTTRPNHLGQEVIDNSVDEALAGHAKRVEVILHADQSLEVIDDGRGMPVDIHPEEGVPAVELILCRLHAGGKFSNKNYQFSGGLHGVGISVVNALSKRVEVNVRRDGQVYSIAFENGEKVEDLHVTGTCGKRNTGTSVHFWPDESFFDSPRFSVSRLTHLLKAKAVLCPGVEIVFRDQVNNSEQSWCYADGLNDYLSEAVNGLPLLPEKPFVGAFSGETEAVDWALLWLPEGGELLTESYVNLIPTMQGGTHVNGLRQGLLDAMREFCEYRNILPRGVKLSAEDIWDRCAYVLSVKMQDPQFAGQTKERLSSRQCAAFVSGVVKDAFSLWLNQNVQAAELLAEMAISSAQRRLRAAKKVVRKKLTSGPALPGKLADCTAQDLNRTELFLVEGDSAGGSAKQARDREYQAIMPLKGKILNTWEVSSDEVLASQEVHDISVAIGIDPDSDDLSQLRYGKICILADADSDGLHIATLLCALFVRHFRTLVKEGHVYVALPPLYRIDLGKEVYYALTEEEKTGVLEQLKRKKGKPNVQRFKGLGEMNPMQLRETTLDPNTRRLVQLVISDEDEQQTTAIMDMLLAKKRSEDRRNWLQEKGDMADLEV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0003918 Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0006265 The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number.
GO:0005694 A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

75 records

Show feature table

Start	End	DB	Term	Name
389	622	SUPERFAMILY	SSF56719	Type II DNA topoisomerase
389	622	InterPro	IPR013760	DNA topoisomerase, type IIA-like domain superfamily
498	515	PRINTS	PR00418	DNA topoisomerase II family signature
110	124	PRINTS	PR00418	DNA topoisomerase II family signature
67	80	PRINTS	PR00418	DNA topoisomerase II family signature
267	280	PRINTS	PR00418	DNA topoisomerase II family signature
480	496	PRINTS	PR00418	DNA topoisomerase II family signature
32	47	PRINTS	PR00418	DNA topoisomerase II family signature
518	530	PRINTS	PR00418	DNA topoisomerase II family signature
561	577	PRINTS	PR00418	DNA topoisomerase II family signature
415	429	PRINTS	PR00418	DNA topoisomerase II family signature
175	192	PRINTS	PR01098	Topoisomerase IV subunit B signature
175	192	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
193	214	PRINTS	PR01098	Topoisomerase IV subunit B signature
193	214	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
312	327	PRINTS	PR01098	Topoisomerase IV subunit B signature
312	327	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
150	165	PRINTS	PR01098	Topoisomerase IV subunit B signature
150	165	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
504	520	PRINTS	PR01098	Topoisomerase IV subunit B signature
504	520	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
470	482	PRINTS	PR01098	Topoisomerase IV subunit B signature
470	482	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
136	150	PRINTS	PR01098	Topoisomerase IV subunit B signature
136	150	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
239	262	PRINTS	PR01098	Topoisomerase IV subunit B signature
239	262	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
449	470	PRINTS	PR01098	Topoisomerase IV subunit B signature
449	470	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
27	40	PRINTS	PR01098	Topoisomerase IV subunit B signature
27	40	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
295	311	PRINTS	PR01098	Topoisomerase IV subunit B signature
295	311	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
538	560	PRINTS	PR01098	Topoisomerase IV subunit B signature
538	560	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
339	362	PRINTS	PR01098	Topoisomerase IV subunit B signature
339	362	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
363	388	PRINTS	PR01098	Topoisomerase IV subunit B signature
363	388	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
29	172	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
29	172	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
3	629	Hamap	MF_00938	DNA topoisomerase 4 subunit B [parE].
3	629	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
2	629	PANTHER	PTHR45866	DNA GYRASE/TOPOISOMERASE SUBUNIT B
557	621	Pfam	PF00986	DNA gyrase B subunit, carboxyl terminus
557	621	InterPro	IPR002288	DNA gyrase B subunit, C-terminal
6	216	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
6	216	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
217	390	Gene3D	G3DSA:3.30.230.10	-
217	390	InterPro	IPR014721	Ribosomal protein S5 domain 2-type fold, subgroup
28	174	SMART	SM00387	HKATPase_4
28	174	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
391	624	FunFam	G3DSA:3.40.50.670:FF:000003	DNA topoisomerase 4 subunit B
413	526	ProSiteProfiles	PS50880	Toprim domain profile.
413	526	InterPro	IPR006171	TOPRIM domain
217	390	FunFam	G3DSA:3.30.230.10:FF:000012	DNA topoisomerase 4 subunit B
414	522	Pfam	PF01751	Toprim domain
414	522	InterPro	IPR006171	TOPRIM domain
33	214	CDD	cd16928	HATPase_GyrB-like
218	383	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
218	383	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold
5	626	NCBIfam	TIGR01055	DNA topoisomerase IV subunit B
5	626	InterPro	IPR005737	DNA topoisomerase IV, subunit B, Gram-negative
417	425	ProSitePatterns	PS00177	DNA topoisomerase II signature.
417	425	InterPro	IPR018522	DNA topoisomerase, type IIA, conserved site
3	216	Gene3D	G3DSA:3.30.565.10	-
3	216	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
391	624	Gene3D	G3DSA:3.40.50.670	-
391	624	InterPro	IPR013759	DNA topoisomerase, type IIA, subunit B, C-terminal
3	217	FunFam	G3DSA:3.30.565.10:FF:000002	DNA gyrase subunit B
35	625	SMART	SM00433	topII5
35	625	InterPro	IPR001241	DNA topoisomerase, type IIA
218	387	CDD	cd00822	TopoII_Trans_DNA_gyrase
219	385	Pfam	PF00204	DNA gyrase B
219	385	InterPro	IPR013506	DNA topoisomerase, type IIA, subunit B, domain 2

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

0.816

Likely same site as FPocket 3 1.2 Å 26 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.247

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Surrounding area

Pocket 3 P2Rank #3

0.071

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Surrounding area

Pocket 4 P2Rank #4

0.058

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Surrounding area

Pocket 5 P2Rank #5

0.018

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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 #3

0.795

Likely same site as P2Rank 1 1.2 Å 26 shared residues 96% of smaller site

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Surrounding area

Pocket 2 FPocket #44

0.317

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Surrounding area

Residue sets

UniProt: Binding site:111-117

UniProt: Binding site:335-335

UniProt: Binding site:43-43

UniProt: Binding site:6-6

UniProt: Binding site:70-70

UniProt: Site:447-447 Interaction with DNA

UniProt: Site:498-498 Interaction with DNA

UniProt: Site:616-616 Interaction with DNA

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.886

Likely same site as FPocket 2 3.4 Å 23 shared residues 92% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.232

Likely same site as FPocket 8 2.4 Å 12 shared residues 80% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.082

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Surrounding area

Pocket 4 P2Rank #4

0.067

Likely same site as FPocket 10 6.1 Å 8 shared residues 73% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.061

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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 #2

0.487

Likely same site as P2Rank 1 3.4 Å 23 shared residues 92% of smaller site

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Surrounding area

Pocket 2 FPocket #8

0.449

Likely same site as P2Rank 2 2.4 Å 12 shared residues 80% of smaller site

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Surrounding area

Pocket 3 FPocket #10

0.306

Likely same site as P2Rank 4 6.1 Å 8 shared residues 73% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:111-117

UniProt: Binding site:335-335

UniProt: Binding site:43-43

UniProt: Binding site:6-6

UniProt: Binding site:70-70

UniProt: Site:447-447 Interaction with DNA

UniProt: Site:498-498 Interaction with DNA

UniProt: Site:616-616 Interaction with DNA

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_A0A0H3H365	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4030	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.

88 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 38 records from similar proteins

Structural ligands 20 0 loaded crystals

Measured bioactivity 18 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

19X PDB via homolog 426.9 Da · LogP 3.44 · TPSA 100.3 Open detail RCSB PDB

19Y PDB via homolog Detail RCSB PDB

1AV PDB via homolog Detail RCSB PDB

1EU PDB via homolog Detail RCSB PDB

1UV 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
19X RCSB PDB	4HY1	A0A0J9WZF0	426.9 Da LogP 3.44 TPSA 100.3	✓ Ro5	✓ Clean	`CCc1c(c2c([nH]1)nc(nc2N3CC[C@H](C3)N)Sc4ccc5c(c…`
19Y RCSB PDB	4HXZ	A0A0J9WZF0	314.4 Da LogP 2.89 TPSA 80.8	✓ Ro5	✓ Clean	`CCc1c(c2c([nH]1)nc(nc2OC)Sc3cccnc3)C=O`
1AV RCSB PDB	4HZ0	P20083	295.3 Da LogP 1.92 TPSA 95.4	✓ Ro5	✓ Clean	`c1cc(cnc1)c2nc3c(nc(nc3s2)N)n4ccnc4`
1EU RCSB PDB	3FV5	P20083	323.4 Da LogP 2.97 TPSA 99.8	✓ Ro5	✓ Clean	`CCNC(=O)Nc1[nH]c2cc(cc(c2n1)C(=O)C)c3cccnc3`
1UV RCSB PDB	4KPF	Q59961	373.4 Da LogP 1.61 TPSA 97.8	✓ Ro5	✓ Clean	`c1c2c(c3c(c1F)N4CC[C@H]([C@H]4COC3)N)N(C=C(C2=O…`
1YP RCSB PDB	4LPB	Q8DQB5	477.4 Da LogP 3.77 TPSA 138.7	✓ Ro5	✓ Clean	`CCNC(=O)Nc1cc(c(cn1)c2cc(cnc2)C3=NNC(=O)O3)c4nc…`
2B7 RCSB PDB	4MOT	Q8DQB5	397.5 Da LogP 3.87 TPSA 88.9	✓ Ro5	✓ Clean	`CC(C)CCN1c2c(nc(s2)NC(=O)NCC=C)C=C(C1=O)c3cccnc3`
AF5 RCSB PDB	4KPE	Q59961	369.4 Da LogP 2.50 TPSA 88.6	✓ Ro5	✓ Clean	`c1c2c(c3c(c1F)N4CC[C@H]([C@H]4CC=C3)N)N(C=C(C2=…`
ANP RCSB PDB	1S16	P20083	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BHW RCSB PDB	6ENH	Q5SHZ4	1110.1 Da LogP 5.57 TPSA 354.9	4 viol.	✓ Clean	`Cc1ccc([nH]1)C(=O)O[C@H]2[C@H]([C@@H](OC([C@@H]…`
CJC RCSB PDB	4HYM	A0A0J9WZF0	442.9 Da LogP 2.49 TPSA 129.5	✓ Ro5	✓ Clean	`CCc1c(c2c([nH]1)nc(nc2N3CC[C@H](C3)N)Sc4cc5c(nc…`
DOO RCSB PDB	4KQV	A0A0J9WZF0	434.5 Da LogP 2.98 TPSA 103.9	✓ Ro5	✓ Clean	`Cc1ncc(cn1)Oc2nc3c(c4cc(cc(c4[nH]3)NC)F)c(n2)N5…`
LFX RCSB PDB	3K9F	Q59961	361.4 Da LogP 1.54 TPSA 75.0	✓ Ro5	✓ Clean	`C[C@H]1COc2c3c(cc(c2N4CCN(CC4)C)F)C(=O)C(=CN31)…`
MFX RCSB PDB	3FOF	Q59961	401.4 Da LogP 2.37 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c2c(cc(c1N3C[C@@H]4CCCN[C@@H]4C3)F)C(=O)C(=…`
NFX RCSB PDB	3FOE	Q59961	365.8 Da LogP 2.36 TPSA 88.6	✓ Ro5	✓ Clean	`c1c2c(c(c(c1F)N3CC[C@H](C3)N)Cl)N(C=C(C2=O)C(=O…`
NOV RCSB PDB	1S14	P20083	612.6 Da LogP 3.63 TPSA 200.0	2 viol.	✓ Clean	`Cc1c(ccc2c1OC(=O)C(=C2O)NC(=O)c3ccc(c(c3)CC=C(C…`
PDQ RCSB PDB	3LTN	Q59961	361.4 Da LogP 0.83 TPSA 99.3	✓ Ro5	✓ Clean	`Cc1c2c(cc(c1N3CC[C@H](C3)[C@H](C)N)F)C(=O)N(C(=…`
TR6 RCSB PDB	4KOE	Q59961	416.4 Da LogP 1.89 TPSA 101.5	✓ Ro5	✓ Clean	`c1cc(c(cc1F)F)N2C=C(C(=O)c3c2nc(c(c3)F)N4C[C@@H…`
TSJ RCSB PDB	5BOC	Q8DQB5	403.4 Da LogP 4.66 TPSA 95.1	✓ Ro5	✓ Clean	`Cc1cc(cc(c1)C(F)(F)F)c2cc([nH]n2)NC(=O)c3ccc(cc…`
TTJ RCSB PDB	5BOD	Q8DQB5	301.3 Da LogP 2.05 TPSA 76.2	✓ Ro5	✓ Clean	`Cc1cc(cc(c1)c2cc([nH]n2)NC(=O)[C@H]3COCCO3)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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL4283208 ChEMBL	P20083	8.52 ~3.0 nM	573.7 Da LogP 3.91 TPSA 145.2	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C3CC3)cs2)c(-c2cc(-c3n[nH]c…`
CHEMBL4289998 ChEMBL	P20083	8.40 ~4.0 nM	585.6 Da LogP 3.89 TPSA 140.7	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc(-c3nnn…`
CHEMBL4294467 ChEMBL	P20083	8.40 ~4.0 nM	601.6 Da LogP 4.05 TPSA 145.2	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc(-c3n[n…`
CHEMBL4281775 ChEMBL	P20083	8.10 ~7.9 nM	561.6 Da LogP 4.41 TPSA 123.6	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc(C(=O)O…`
CHEMBL4279313 ChEMBL	P20083	8.05 ~8.9 nM	638.7 Da LogP 3.40 TPSA 149.5	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc(C(=O)N…`
CHEMBL4289650 ChEMBL	P20083	8.00 ~10.0 nM	560.6 Da LogP 5.01 TPSA 110.7	2 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc(C(=O)O…`
CHEMBL4291061 ChEMBL	P20083	7.92 ~12.0 nM	601.6 Da LogP 4.23 TPSA 167.9	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc(-c3n[n…`
CHEMBL4279382 ChEMBL	P20083	7.85 ~14.1 nM	568.6 Da LogP 5.26 TPSA 99.2	2 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc3ncccc3…`
CHEMBL4278317 ChEMBL	P20083	7.68 ~20.9 nM	554.6 Da LogP 4.92 TPSA 108.0	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc3ncccc3…`
CHEMBL4286573 ChEMBL	P20083	7.64 ~22.9 nM	575.6 Da LogP 3.70 TPSA 167.9	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc(-c3n[n…`
CHEMBL4295081 ChEMBL	P20083	7.62 ~24.0 nM	568.6 Da LogP 5.43 TPSA 121.9	2 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc3ncccc3…`
CHEMBL4286232 ChEMBL	P20083	7.60 ~25.1 nM	568.6 Da LogP 5.31 TPSA 108.0	2 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc3ncccc3…`
CHEMBL4293447 ChEMBL	P20083	7.31 ~49.0 nM	542.6 Da LogP 4.90 TPSA 121.9	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc3ncccc3…`
CHEMBL4290062 ChEMBL	P20083	6.70 ~199.5 nM	554.6 Da LogP 4.87 TPSA 99.2	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc3ncccc3…`
CHEMBL4294536 ChEMBL	P20083	6.40 ~398.1 nM	542.6 Da LogP 4.73 TPSA 99.2	1 viol.	✓ Clean	`CCNC(=O)Nc1cc(-c2nc(C(F)(F)F)cs2)c(-c2cc3ncccc3…`
1YM ChEMBL	P20083	6.16 ~691.8 nM	437.4 Da LogP 4.13 TPSA 117.1	✓ Ro5	✓ Clean	`CCNC(=O)Nc1cc(c(cn1)c2cc(cnc2)C(=O)O)c3nc(cs3)C…`
CHEMBL3329318 ChEMBL	P20083	6.11 ~776.2 nM	392.4 Da LogP 3.32 TPSA 128.3	✓ Ro5	✓ Clean	`CCNC(=O)Nc1cc(Nc2cccc(O)c2)c(C(=O)Nc2cccnc2)cn1`
CHEMBL3329317 ChEMBL	P20083	6.03 ~933.3 nM	392.4 Da LogP 3.32 TPSA 128.3	✓ Ro5	✓ Clean	`CCNC(=O)Nc1cc(Nc2ccc(O)cc2)c(C(=O)Nc2cccnc2)cn1`

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
ZINC100030989 ZINC	1.000	416.4 Da LogP 1.89 TPSA 101.4	✓ Ro5	✓ Clean	`N[C@H]1[C@@H]2CN(c3nc4c(cc3F)c(=O)c(C(=O)O)cn4-…`
ZINC100232307 ZINC	1.000	416.4 Da LogP 1.89 TPSA 101.4	✓ Ro5	✓ Clean	`NC1[C@@H]2CN(c3nc4c(cc3F)c(=O)c(C(=O)O)cn4-c3cc…`
ZINC100232310 ZINC	1.000	416.4 Da LogP 1.89 TPSA 101.4	✓ Ro5	✓ Clean	`NC1[C@H]2CN(c3nc4c(cc3F)c(=O)c(C(=O)O)cn4-c3ccc…`
ZINC12503149 ZINC	1.000	416.4 Da LogP 1.89 TPSA 101.4	✓ Ro5	✓ Clean	`NC1[C@@H]2CN(c3nc4c(cc3F)c(=O)c(C(=O)O)cn4-c3cc…`
ZINC1278767 ZINC	1.000	365.8 Da LogP 2.36 TPSA 88.6	✓ Ro5	✓ Clean	`N[C@@H]1CCN(c2c(F)cc3c(=O)c(C(=O)O)cn(C4CC4)c3c…`
ZINC147175374 ZINC	1.000	416.4 Da LogP 1.89 TPSA 101.4	✓ Ro5	✓ Clean	`N[C@@H]1[C@@H]2CN(c3nc4c(cc3F)c(=O)c(C(=O)O)cn4…`
ZINC14768406 ZINC	1.000	401.4 Da LogP 2.37 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c(N2C[C@@H]3CCCN[C@H]3C2)c(F)cc2c(=O)c(C(=O…`
ZINC27213606 ZINC	1.000	401.4 Da LogP 2.37 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c(N2C[C@H]3CCCN[C@H]3C2)c(F)cc2c(=O)c(C(=O)…`
ZINC3826253 ZINC	1.000	401.4 Da LogP 2.37 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c(N2C[C@@H]3CCCN[C@@H]3C2)c(F)cc2c(=O)c(C(=…`
ZINC3873790 ZINC	1.000	401.4 Da LogP 2.37 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c(N2C[C@H]3NCCC[C@@H]3C2)c(F)cc2c(=O)c(C(=O…`
ZINC3882444 ZINC	1.000	365.8 Da LogP 2.36 TPSA 88.6	✓ Ro5	✓ Clean	`N[C@H]1CCN(c2c(F)cc3c(=O)c(C(=O)O)cn(C4CC4)c3c2…`
ZINC537891 ZINC	1.000	361.4 Da LogP 1.54 TPSA 75.0	✓ Ro5	✓ Clean	`C[C@@H]1COc2c(N3CCN(C)CC3)c(F)cc3c(=O)c(C(=O)O)…`
ZINC538273 ZINC	1.000	361.4 Da LogP 1.54 TPSA 75.0	✓ Ro5	✓ Clean	`C[C@H]1COc2c(N3CCN(C)CC3)c(F)cc3c(=O)c(C(=O)O)c…`
ZINC69416057 ZINC	1.000	301.3 Da LogP 2.05 TPSA 76.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-c2cc(NC(=O)[C@@H]3COCCO3)[nH]n2)c1`
ZINC69416059 ZINC	1.000	301.3 Da LogP 2.05 TPSA 76.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-c2cc(NC(=O)[C@H]3COCCO3)[nH]n2)c1`
ZINC3787097 ZINC	0.873	393.8 Da LogP 3.14 TPSA 88.6	✓ Ro5	✓ Clean	`N[C@@H]1CCCCN(c2c(F)cc3c(=O)c(C(=O)O)cn(C4CC4)c…`
ZINC606260 ZINC	0.873	393.8 Da LogP 3.14 TPSA 88.6	✓ Ro5	✓ Clean	`N[C@H]1CCCCN(c2c(F)cc3c(=O)c(C(=O)O)cn(C4CC4)c3…`
ZINC168542421 ZINC	0.870	359.4 Da LogP 2.05 TPSA 54.8	✓ Ro5	✓ Clean	`CC(=O)c1cn2c3c(c(N4CCN(C)CC4)c(F)cc3c1=O)OC[C@@…`
ZINC168641115 ZINC	0.870	359.4 Da LogP 2.05 TPSA 54.8	✓ Ro5	✓ Clean	`CC(=O)c1cn2c3c(c(N4CCN(C)CC4)c(F)cc3c1=O)OC[C@H…`
ZINC77311493 ZINC	0.859	415.5 Da LogP 2.46 TPSA 72.8	✓ Ro5	✓ Clean	`COC(=O)c1cn(C2CC2)c2c(OC)c(N3C[C@@H]4CCCN[C@@H]…`
ZINC1857526844 ZINC	0.855	397.5 Da LogP 2.54 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c(N2C[C@H]3NCCC[C@@H]3C2)c(C)cc2c(=O)c(C(=O…`
ZINC1857526845 ZINC	0.855	397.5 Da LogP 2.54 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c(N2C[C@H]3CCCN[C@H]3C2)c(C)cc2c(=O)c(C(=O)…`
ZINC1857526846 ZINC	0.855	397.5 Da LogP 2.54 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c(N2C[C@@H]3CCCN[C@H]3C2)c(C)cc2c(=O)c(C(=O…`
ZINC1857526847 ZINC	0.855	397.5 Da LogP 2.54 TPSA 83.8	✓ Ro5	✓ Clean	`COc1c(N2C[C@@H]3CCCN[C@@H]3C2)c(C)cc2c(=O)c(C(=…`
ZINC215766222 ZINC	0.841	413.5 Da LogP 2.24 TPSA 93.0	✓ Ro5	✓ Clean	`COc1cc2c(=O)c(C(=O)O)cn(C3CC3)c2c(OC)c1N1C[C@H]…`
ZINC256001979 ZINC	0.841	413.5 Da LogP 2.24 TPSA 93.0	✓ Ro5	✓ Clean	`COc1cc2c(=O)c(C(=O)O)cn(C3CC3)c2c(OC)c1N1C[C@@H…`
ZINC256001980 ZINC	0.841	413.5 Da LogP 2.24 TPSA 93.0	✓ Ro5	✓ Clean	`COc1cc2c(=O)c(C(=O)O)cn(C3CC3)c2c(OC)c1N1C[C@H]…`
ZINC65740505 ZINC	0.841	413.5 Da LogP 2.24 TPSA 93.0	✓ Ro5	✓ Clean	`COc1cc2c(=O)c(C(=O)O)cn(C3CC3)c2c(OC)c1N1C[C@@H…`
ZINC1148154205 ZINC	0.839	443.5 Da LogP 1.23 TPSA 61.3	✓ Ro5	✓ Clean	`C[C@H]1COc2c(N3CCN(C)CC3)c(F)cc3c(=O)c(C(=O)N4C…`
ZINC5932777 ZINC	0.839	389.4 Da LogP 2.50 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2c(F)c(N3C[C@@H]4CCCN[C@@H]4C…`
ZINC43204969 ZINC	0.836	362.4 Da LogP 0.79 TPSA 101.0	✓ Ro5	✓ Clean	`C[C@H]1COc2c(N3CCN(N)CC3)c(F)cc3c(=O)c(C(=O)O)c…`
ZINC65740892 ZINC	0.833	415.5 Da LogP 2.76 TPSA 83.8	✓ Ro5	✓ Clean	`CCOc1c(N2C[C@@H]3CCCN[C@@H]3C2)c(F)cc2c(=O)c(C(…`
ZINC26666727 ZINC	0.825	375.4 Da LogP 1.63 TPSA 64.0	✓ Ro5	✓ Clean	`COC(=O)c1cn2c3c(c(N4CCN(C)CC4)c(F)cc3c1=O)OC[C@…`
ZINC69504953 ZINC	0.825	375.4 Da LogP 1.63 TPSA 64.0	✓ Ro5	✓ Clean	`COC(=O)c1cn2c3c(c(N4CCN(C)CC4)c(F)cc3c1=O)OC[C@…`
ZINC117702629 ZINC	0.818	437.4 Da LogP 2.96 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2c(OC(F)F)c(N3C[C@H]4CCCN[C@H…`
ZINC207801987 ZINC	0.818	437.4 Da LogP 2.96 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2c(OC(F)F)c(N3C[C@H]4NCCC[C@@…`
ZINC2382315469 ZINC	0.818	437.4 Da LogP 2.96 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2c(OC(F)F)c(N3C[C@@H]4CCCN[C@…`
ZINC9132747 ZINC	0.818	437.4 Da LogP 2.96 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)c1cn(C2CC2)c2c(OC(F)F)c(N3C[C@@H]4CCCN[C@…`
ZINC15202 ZINC	0.815	349.3 Da LogP 1.85 TPSA 88.6	✓ Ro5	✓ Clean	`N[C@@H]1CCN(c2c(F)cc3c(=O)c(C(=O)O)cn(C4CC4)c3c…`
ZINC3933 ZINC	0.815	349.3 Da LogP 1.85 TPSA 88.6	✓ Ro5	✓ Clean	`N[C@H]1CCN(c2c(F)cc3c(=O)c(C(=O)O)cn(C4CC4)c3c2…`
ZINC12360002 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC31977053 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`

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.

Sequence

UniProt A0A0H3H365

Chemistry

ChEMBL CHEMBL4283208 ChEMBL CHEMBL4289998 ChEMBL CHEMBL4294467 ChEMBL CHEMBL4281775 ChEMBL CHEMBL4279313 ChEMBL CHEMBL4289650 ChEMBL CHEMBL4291061 ChEMBL CHEMBL4279382 ChEMBL CHEMBL4278317 ChEMBL CHEMBL4286573 ChEMBL CHEMBL4295081 ChEMBL CHEMBL4286232 ChEMBL CHEMBL4293447 ChEMBL CHEMBL4290062 ChEMBL CHEMBL4294536 ChEMBL 1YM ChEMBL CHEMBL3329318 ChEMBL CHEMBL3329317