KpATCC43816 Protein target profile

exonuclease I, 3' -- 5' specific deoxyribophosphodiesterase

Accession: VK055_5051

Gene: AIK83577.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GSG0

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Length 474

Pocket druggability (P2Rank · AlphaFold DB model) 0.678

Direct ligand evidence 0 52 total records

Functional annotation 1 EC 7 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

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: No hit
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 83.898 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.87 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) 0.678

Structure A0A0H3GSG0

Pocket Pocket 1

Druggability (FPocket) 0.468

Structure A0A0H3GSG0

Pocket Pocket 15

ColabFold model

P2Rank 0.678 · Pocket 1

FPocket 0.78 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 143 / 4744 genomes with a hit

Prevalence 3.0%

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.

MQDSVNQPGFLFHDYETFGTSPSLDRPAQFAAIRTDAELNVLGEPEVFYCKPADDYLPQPQAVMITGITPQEALAKGDNEATFARRIHDLFTVPQTCIVGYNNVRFDDEVTRNIFYRNFYDPYAWSWQHDNSRWDLLDVMRACYALRPEGIAWPENDEGLPSFRLEHLTVANGIEHQNAHDAMADVYATIAMAKLVKTRQPRLFDYLYSHRNKRKLATLIDVPQMKPLVHVSGMFGAARGNTSLVAPLAWHPENRNAVIMVDLAGDMAPLLELDADALRERLYTPRAELGDLPAASIKLVHLNKCPVLAQANTLRPQDADRLGISIQRCLENAQLLRANPQVREKVVAVYAEAEPFVPSENVDAQLYNGFFSDADRAAMKIVLETEPRNLPALDITFADQRIERLLFNYRARNFPGTLDEHEQQRWLEHRRQVFTPAFLQAYADELQMLYQQYADDKEKLAQLKALWQYAQDIV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.1.11.1

Gene Ontology (GO)

GO:0003676 Binding to a nucleic acid.
GO:0004529 Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a DNA molecule.
GO:0000175 Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of an RNA molecule.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0008310 Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a single-stranded DNA molecule.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
12	189	Pfam	PF00929	Exonuclease
12	189	InterPro	IPR013520	Exonuclease, RNase T/DNA polymerase III
358	474	ProSiteProfiles	PS51785	Exonuclease I (ExoI) C-terminal domain profile.
358	474	InterPro	IPR034748	Exonuclease I, C-terminal alpha-helical domain
439	466	Coils	Coil	Coil
213	352	Gene3D	G3DSA:3.30.1520.20	Exonuclease ExoI, domain 2
213	352	InterPro	IPR038649	Exonuclease I, SH3-like domain superfamily
13	431	PANTHER	PTHR11046	OLIGORIBONUCLEASE, MITOCHONDRIAL
13	431	InterPro	IPR022894	Oligoribonuclease
358	419	Gene3D	G3DSA:1.20.1280.70	Exonuclease ExoI, domain 3
421	474	Gene3D	G3DSA:1.10.287.1240	-
201	354	ProSiteProfiles	PS51784	Exonuclease I (ExoI) SH3-like domain profile.
201	354	InterPro	IPR034747	Exonuclease I, SH3-like domain
9	473	SUPERFAMILY	SSF53098	Ribonuclease H-like
9	473	InterPro	IPR012337	Ribonuclease H-like superfamily
9	200	Gene3D	G3DSA:3.30.420.10	-
9	200	InterPro	IPR036397	Ribonuclease H superfamily
9	202	SMART	SM00479	exoiiiendus
9	202	InterPro	IPR013520	Exonuclease, RNase T/DNA polymerase III
2	474	PIRSF	PIRSF000977	Exodeoxyribonuclease_I
2	474	InterPro	IPR023607	Exodeoxyribonuclease I
213	351	FunFam	G3DSA:3.30.1520.20:FF:000001	Exodeoxyribonuclease I
11	194	CDD	cd06138	ExoI_N
8	200	FunFam	G3DSA:3.30.420.10:FF:000033	Exodeoxyribonuclease I
359	419	FunFam	G3DSA:1.20.1280.70:FF:000001	Exodeoxyribonuclease I
211	471	Pfam	PF08411	Exonuclease C-terminal
211	471	InterPro	IPR013620	Exodeoxyribonuclease I, C-terminal

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

0.678

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Surrounding area

Pocket 2 P2Rank #2

0.278

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Surrounding area

Pocket 3 P2Rank #3

0.22

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Surrounding area

Pocket 4 P2Rank #4

0.154

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Surrounding area

Pocket 5 P2Rank #5

0.044

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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 #15

0.468

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Surrounding area

Pocket 2 FPocket #36

0.218

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Surrounding area

Residue sets

UniProt: Binding site:14-14

UniProt: Binding site:16-16

UniProt: Binding site:164-164

UniProt: Binding site:185-185

UniProt: Site:147-147 Important for interaction with ssb

UniProt: Site:180-180 Important for activity

UniProt: Site:206-206 Important for interaction with ssb

UniProt: Site:310-310 Important for interaction with ssb

UniProt: Site:337-337 Important for interaction with ssb

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.678

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Surrounding area

Pocket 2 P2Rank #2

0.285

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Surrounding area

Pocket 3 P2Rank #3

0.284

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Surrounding area

Pocket 4 P2Rank #4

0.242

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Surrounding area

Pocket 5 P2Rank #5

0.042

Likely same site as FPocket 2 6.1 Å 6 shared residues 55% of smaller site

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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

0.78

Likely same site as P2Rank 5 6.1 Å 6 shared residues 55% of smaller site

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Surrounding area

Pocket 2 FPocket #5

0.476

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Surrounding area

Pocket 3 FPocket #14

0.251

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Surrounding area

Residue sets

UniProt: Binding site:14-14

UniProt: Binding site:16-16

UniProt: Binding site:164-164

UniProt: Binding site:185-185

UniProt: Site:147-147 Important for interaction with ssb

UniProt: Site:180-180 Important for activity

UniProt: Site:206-206 Important for interaction with ssb

UniProt: Site:310-310 Important for interaction with ssb

UniProt: Site:337-337 Important for interaction with ssb

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_A0A0H3GSG0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_5051	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

BBP PDB via homolog 307.8 Da · LogP 4.09 · TPSA 45.6 Open detail RCSB PDB

CF1 PDB via homolog Detail RCSB PDB

ZINC5283936 ZINC proposed compound · Tanimoto 0.702 Detail ZINC

ZINC1579743 ZINC proposed compound · Tanimoto 0.660 Detail ZINC

ZINC4099443 ZINC proposed compound · Tanimoto 0.660 Detail ZINC

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
BBP RCSB PDB	3HL8	P04995	307.8 Da LogP 4.09 TPSA 45.6	✓ Ro5	✓ Clean	`CC(C)(C)C1=NN(C(=O)C1)c2nc3ccc(cc3s2)Cl`
CF1 RCSB PDB	3HP9	P04995	345.7 Da LogP 4.81 TPSA 58.6	✓ Ro5	Alert	`COc1ccc(c(c1)C(=O)O)Nc2cc(ccc2Cl)C(F)(F)F`

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
ZINC5283936 ZINC	0.702	273.4 Da LogP 3.44 TPSA 45.6	✓ Ro5	✓ Clean	`CC(C)(C)C1=NN(c2nc3ccccc3s2)C(=O)C1`
ZINC1579743 ZINC	0.660	315.7 Da LogP 4.80 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1cc(C(F)(F)F)ccc1Cl`
ZINC4099443 ZINC	0.660	277.7 Da LogP 3.79 TPSA 58.6	✓ Ro5	Alert	`COc1ccc(Nc2ccccc2Cl)c(C(=O)O)c1`
ZINC101566 ZINC	0.600	329.7 Da LogP 4.62 TPSA 38.3	✓ Ro5	✓ Clean	`COc1ccc(C(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1`
ZINC1729836 ZINC	0.587	273.3 Da LogP 3.15 TPSA 67.8	✓ Ro5	Alert	`COc1ccc(Nc2ccc(OC)cc2C(=O)O)cc1`
ZINC272451 ZINC	0.566	343.7 Da LogP 4.55 TPSA 38.3	✓ Ro5	✓ Clean	`COc1ccc(CC(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1`
ZINC58157306 ZINC	0.561	423.8 Da LogP 3.95 TPSA 81.7	✓ Ro5	✓ Clean	`COC(=O)c1cc(OC)ccc1NS(=O)(=O)c1cc(C(F)(F)F)ccc1…`
ZINC437703 ZINC	0.556	329.7 Da LogP 4.62 TPSA 38.3	✓ Ro5	✓ Clean	`COc1cccc(C(=O)Nc2cc(C(F)(F)F)ccc2Cl)c1`
ZINC6936383 ZINC	0.556	369.3 Da LogP 3.67 TPSA 84.9	✓ Ro5	✓ Clean	`COc1ccc(C(=O)Nc2cc(C(F)(F)F)ccc2C(=O)O)c(OC)c1`
ZINC2848323 ZINC	0.545	373.8 Da LogP 4.77 TPSA 47.6	✓ Ro5	✓ Clean	`COc1ccc(O[C@@H](C)C(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1`
ZINC2848324 ZINC	0.545	373.8 Da LogP 4.77 TPSA 47.6	✓ Ro5	✓ Clean	`COc1ccc(O[C@H](C)C(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1`
ZINC2172100 ZINC	0.542	253.6 Da LogP 3.54 TPSA 38.3	✓ Ro5	✓ Clean	`COC(=O)Nc1cc(C(F)(F)F)ccc1Cl`
ZINC94596758 ZINC	0.542	281.2 Da LogP 4.15 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(F)(F)F)ccc1Nc1ccccc1`
ZINC22151790 ZINC	0.537	316.7 Da LogP 4.20 TPSA 62.2	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1Nc1cc(C(F)(F)F)ccc1Cl`
ZINC481307 ZINC	0.537	310.3 Da LogP 3.56 TPSA 64.3	✓ Ro5	✓ Clean	`COc1ccc(Nc2cccc(C(F)(F)F)c2)c(C(N)=O)c1`
ZINC1140239 ZINC	0.536	357.8 Da LogP 4.94 TPSA 38.3	✓ Ro5	✓ Clean	`COc1ccc(CCC(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1`
ZINC13320435 ZINC	0.536	358.7 Da LogP 4.69 TPSA 50.4	✓ Ro5	✓ Clean	`COc1ccc(CNC(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1`
ZINC753310 ZINC	0.528	365.8 Da LogP 4.17 TPSA 55.4	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1`
ZINC4922336 ZINC	0.526	358.7 Da LogP 4.91 TPSA 53.8	✓ Ro5	Alert	`COc1ccc(/C(C)=N/Nc2cc(C(F)(F)F)ccc2Cl)c(O)c1`
ZINC13320494 ZINC	0.525	413.8 Da LogP 4.72 TPSA 44.8	✓ Ro5	Alert	`COc1ccc(N2CCN(C(=O)Nc3cc(C(F)(F)F)ccc3Cl)CC2)cc1`
ZINC56838 ZINC	0.523	224.6 Da LogP 3.06 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(F)(F)F)ccc1Cl`
ZINC164757 ZINC	0.520	250.2 Da LogP 2.33 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(OCC(F)(F)F)c(C(=O)O)c1`
ZINC2814773 ZINC	0.519	343.7 Da LogP 4.31 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1C(=O)Nc1cc(C(F)(F)F)ccc1Cl`
ZINC683171 ZINC	0.519	389.8 Da LogP 4.64 TPSA 56.8	✓ Ro5	✓ Clean	`COc1cc(OC)c(C(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1OC`
ZINC13320421 ZINC	0.517	372.8 Da LogP 4.73 TPSA 50.4	✓ Ro5	✓ Clean	`COc1ccc(CCNC(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1`
ZINC20739021 ZINC	0.517	382.8 Da LogP 4.96 TPSA 43.3	✓ Ro5	✓ Clean	`COc1ccc2c(ccn2CC(=O)Nc2cc(C(F)(F)F)ccc2Cl)c1`
ZINC13320508 ZINC	0.516	457.9 Da LogP 4.73 TPSA 54.0	✓ Ro5	✓ Clean	`COc1ccc(OC)c(CN2CCN(C(=O)Nc3cc(C(F)(F)F)ccc3Cl)…`
ZINC12956694 ZINC	0.511	220.1 Da LogP 2.41 TPSA 46.5	✓ Ro5	✓ Clean	`COc1ccc(C(F)(F)F)cc1C(=O)O`
ZINC134025 ZINC	0.511	209.2 Da LogP 1.35 TPSA 75.6	✓ Ro5	✓ Clean	`COc1ccc(NC(C)=O)c(C(=O)O)c1`
ZINC20220689 ZINC	0.511	238.6 Da LogP 3.15 TPSA 26.3	✓ Ro5	✓ Clean	`COC(=O)c1cc(C(F)(F)F)ccc1Cl`
ZINC308840216 ZINC	0.511	299.5 Da LogP 3.52 TPSA 26.3	✓ Ro5	✓ Clean	`COc1ccc(Cl)c(C(=O)C(F)(F)Br)c1`
ZINC351305 ZINC	0.511	237.6 Da LogP 3.32 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)Nc1cc(C(F)(F)F)ccc1Cl`
ZINC389373086 ZINC	0.511	238.6 Da LogP 3.09 TPSA 26.3	✓ Ro5	✓ Clean	`COc1ccc(Cl)c(C(=O)C(F)(F)F)c1`
ZINC54527155 ZINC	0.511	219.2 Da LogP 2.45 TPSA 49.3	✓ Ro5	✓ Clean	`CNc1ccc(C(F)(F)F)cc1C(=O)O`
ZINC72338570 ZINC	0.511	220.1 Da LogP 2.41 TPSA 46.5	✓ Ro5	✓ Clean	`COc1ccc(C(F)(F)F)c(C(=O)O)c1`
ZINC18044165 ZINC	0.510	319.6 Da LogP 4.79 TPSA 32.7	✓ Ro5	✓ Clean	`CC(C)(C)C1=NN(c2c(Cl)cc(Cl)cc2Cl)C(=O)C1`
ZINC102646525 ZINC	0.509	327.8 Da LogP 4.09 TPSA 45.6	✓ Ro5	✓ Clean	`O=C1CC(c2ccc(Cl)cc2)=NN1c1nc2ccccc2s1`
ZINC438360 ZINC	0.509	329.7 Da LogP 4.62 TPSA 38.3	✓ Ro5	✓ Clean	`COc1ccccc1C(=O)Nc1cc(C(F)(F)F)ccc1Cl`
ZINC712722 ZINC	0.509	359.7 Da LogP 4.63 TPSA 47.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)Nc2cc(C(F)(F)F)ccc2Cl)cc1OC`
ZINC7791601 ZINC	0.509	343.7 Da LogP 4.55 TPSA 38.3	✓ Ro5	✓ Clean	`COc1ccc(CC(=O)Nc2ccc(C(F)(F)F)cc2Cl)cc1`
ZINC1182672 ZINC	0.509	418.8 Da LogP 4.50 TPSA 59.6	✓ Ro5	✓ Clean	`COc1cc(OC)cc(C(=O)NC(=S)Nc2cc(C(F)(F)F)ccc2Cl)c1`
ZINC4922856 ZINC	0.509	358.7 Da LogP 4.82 TPSA 42.9	✓ Ro5	✓ Clean	`COc1ccc(OC)c(/C=N/Nc2cc(C(F)(F)F)ccc2Cl)c1`
ZINC12697899 ZINC	0.508	429.8 Da LogP 3.88 TPSA 70.7	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CN(C)CC(=O)Nc2cc(C(F)(F)F)ccc2Cl)…`
ZINC1148669 ZINC	0.508	436.8 Da LogP 3.63 TPSA 75.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N(C)CC(=O)Nc2cc(C(F)(F)F)ccc2C…`
ZINC3052213 ZINC	0.500	422.8 Da LogP 3.80 TPSA 75.7	✓ Ro5	✓ Clean	`CN(C)S(=O)(=O)Oc1ccc(C(=O)Nc2cc(C(F)(F)F)ccc2Cl…`
ZINC308807291 ZINC	0.500	255.0 Da LogP 3.36 TPSA 26.3	✓ Ro5	✓ Clean	`COc1ccc(Cl)c(C(=O)C(F)(F)Cl)c1`
ZINC346997 ZINC	0.500	279.8 Da LogP 4.31 TPSA 28.5	✓ Ro5	✓ Clean	`CC1=NN(c2nc3ccc(Cl)cc3s2)C(C)(C)C1`
ZINC4842878 ZINC	0.500	359.7 Da LogP 4.63 TPSA 47.6	✓ Ro5	✓ Clean	`COc1cc(OC)cc(C(=O)Nc2ccc(C(F)(F)F)cc2Cl)c1`
ZINC6145620 ZINC	0.500	344.7 Da LogP 4.52 TPSA 53.9	✓ Ro5	Alert	`COc1ccc(O)c(/C=N/Nc2cc(C(F)(F)F)ccc2Cl)c1`
ZINC753351 ZINC	0.500	359.7 Da LogP 4.63 TPSA 47.6	✓ Ro5	✓ Clean	`COc1cccc(OC)c1C(=O)Nc1cc(C(F)(F)F)ccc1Cl`

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 A0A0H3GSG0