KpATCC43816 Protein target profile

H(+)/Cl(-) exchange transporter ClcA

Accession: VK055_2395

Gene: AIK80992.1 clcA 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GNH8

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Length 472

Pocket druggability (P2Rank · AlphaFold DB model) 0.818

Direct ligand evidence 0 60 total records

Functional annotation 0 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.58. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.82. Structure available AlphaFold DB model + ColabFold model 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 (%): 32.716 Lower values reduce human off-target concern.
Human E-value: 4.31e-10
Gut microbiome similarity: 2.6% 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.

Structure confidence

ColabFold pLDDT: 91.26 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) 0.818

Structure A0A0H3GNH8

Pocket Pocket 1

Druggability (FPocket) 0.581

Structure A0A0H3GNH8

Pocket Pocket 28

ColabFold model

P2Rank 0.822 · Pocket 1

FPocket 0.714 · Pocket 7

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 123 / 4744 genomes with a hit

Prevalence 2.6%

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.

MKAETPSFEAHQFVRVRRGDAVRRLIQRDKTPLAVLFMAAVVGTLAGLVGVAFEKSVNWVQNQRIGALAQVADHWYLVWPLAFILSALLAMVGYFLVRRFAPEAGGSGIPEIEGALEELRPVRWWRVLPVKFVGGMGTLGAGMVLGREGPMVQLGGNIGRMVLDVFRMRSPEARHTLLATGAASGLSAAFNAPLAGILFIIEEMRPQFRYNLISIKAVFTGVIMSSIVFRIFNGEAAIIEVGKLSNAPVNTLWLYLVLGMLFGCFGPLFNFLVLRTQDLFQRIHGGNIKKWVLIGGLIGGLCGLLGLMQPSAVGGGFNLIPIAAAGNFSVGLLLFIFIARVVTTLICFSSGAPGGIFAPMLALGTLLGTAFGMAAIPLFPAYHLDAGTFAIAGMGALLAASVRAPLTGIVLVLEMTDNYQLILPMIITCLGATLLAQFLGGKPLYSTILQRTLAKQEAEQAAKAQQAPRENT

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Subcellular localization

Localization: CytoplasmicMembrane

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0006821 The directed movement of chloride into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
GO:0005247 Enables the transmembrane transfer of a chloride ion by a voltage-gated channel. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0015108 Enables the transfer of chloride ions from one side of a membrane to the other.
GO:0015297 Enables the active transport of a solute across a membrane by a mechanism whereby two or more species are transported in opposite directions in a tightly coupled process not directly linked to a form of energy other than chemiosmotic energy. The reaction is: solute A(out) + solute B(in) = solute A(in) + solute B(out).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

54 records

Show feature table

Start	End	DB	Term	Name
54	75	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
414	419	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
418	440	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
42	450	CDD	cd01031	EriC
1	32	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
320	342	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
98	127	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
391	413	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
16	461	Gene3D	G3DSA:1.10.3080.10	Clc chloride channel
388	413	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
91	436	Pfam	PF00654	Voltage gated chloride channel
91	436	InterPro	IPR001807	Chloride channel, voltage gated
76	97	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
213	232	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
291	308	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
33	53	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
3	469	Hamap	MF_01128	H(+)/Cl(-) exchange transporter ClcA [clcA].
3	469	InterPro	IPR023861	Chloride channel, ClcA
128	146	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
354	376	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
22	453	SUPERFAMILY	SSF81340	Clc chloride channel
22	453	InterPro	IPR014743	Chloride channel, core
210	232	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
31	53	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
124	146	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
420	439	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
252	271	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
147	176	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
360	382	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
18	453	PANTHER	PTHR45711	CHLORIDE CHANNEL PROTEIN
16	461	FunFam	G3DSA:1.10.3080.10:FF:000005	H(+)/Cl(-) exchange transporter ClcA
349	359	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
102	119	PRINTS	PR00762	Chloride channel signature
102	119	InterPro	IPR001807	Chloride channel, voltage gated
352	372	PRINTS	PR00762	Chloride channel signature
352	372	InterPro	IPR001807	Chloride channel, voltage gated
183	202	PRINTS	PR00762	Chloride channel signature
183	202	InterPro	IPR001807	Chloride channel, voltage gated
387	403	PRINTS	PR00762	Chloride channel signature
387	403	InterPro	IPR001807	Chloride channel, voltage gated
405	424	PRINTS	PR00762	Chloride channel signature
405	424	InterPro	IPR001807	Chloride channel, voltage gated
202	212	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
233	251	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
291	310	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
252	274	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
309	327	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
272	290	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
383	387	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
440	472	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
328	348	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
177	201	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
179	201	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
75	97	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.

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

0.818

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Surrounding area

Pocket 2 P2Rank #2

0.676

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Surrounding area

Pocket 3 P2Rank #3

0.048

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Surrounding area

Pocket 4 P2Rank #4

0.039

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Surrounding area

Pocket 5 P2Rank #5

0.01

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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 #28

0.581

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Surrounding area

Pocket 2 FPocket #8

0.568

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Surrounding area

Pocket 3 FPocket #9

0.247

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Surrounding area

Residue sets

UniProt: Binding site:138-138

UniProt: Binding site:387-387

UniProt: Binding site:388-388

UniProt: Binding site:476-476

UniProt: Site:179-179 Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport

UniProt: Site:234-234 Mediates proton transfer from the protein to the inner aqueous phase

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.822

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Surrounding area

Pocket 2 P2Rank #2

0.717

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Surrounding area

Pocket 3 P2Rank #3

0.068

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Surrounding area

Pocket 4 P2Rank #4

0.013

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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 #7

0.714

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Surrounding area

Pocket 2 FPocket #3

0.391

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Surrounding area

Pocket 3 FPocket #9

0.329

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Surrounding area

Residue sets

UniProt: Binding site:138-138

UniProt: Binding site:387-387

UniProt: Binding site:388-388

UniProt: Binding site:476-476

UniProt: Site:179-179 Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport

UniProt: Site:234-234 Mediates proton transfer from the protein to the inner aqueous phase

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_A0A0H3GNH8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2395	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.

60 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

BXA PDB via homolog 138.9 Da · LogP 0.47 · TPSA 37.3 Open detail RCSB PDB

MYS PDB via homolog Detail RCSB PDB

SEK PDB via homolog Detail RCSB PDB

Y01 PDB via homolog Detail RCSB PDB

CHEMBL6028327 ChEMBL via homolog · pchembl 8.70 (~2.0 nM) Detail ChEMBL

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
BXA RCSB PDB	6ADC	P37019	138.9 Da LogP 0.47 TPSA 37.3	✓ Ro5	✓ Clean	`C(C(=O)O)Br`
MYS RCSB PDB	1KPL	Q8ZRP8	212.4 Da LogP 6.10 TPSA 0.0	1 viol.	✓ Clean	`CCCCCCCCCCCCCCC`
SEK RCSB PDB	2H2P	P37019	105.0 Da LogP -0.36 TPSA 23.8	✓ Ro5	✓ Clean	`C(#N)[Se-]`
Y01 RCSB PDB	5TR1	E1B792	486.7 Da LogP 7.80 TPSA 63.6	1 viol.	✓ Clean	`CC(C)CCC[C@@H](C)[C@H]1CC[C@@H]2[C@@]1(CC[C@H]3…`

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
CHEMBL6028327 ChEMBL	P51788	8.70 ~2.0 nM	388.3 Da LogP 6.01 TPSA 58.6	1 viol.	✓ Clean	`O=C(O)c1ccccc1Nc1c(Cl)ccc(OCc2ccccc2)c1Cl`
CHEMBL5788508 ChEMBL	P51788	6.70 ~199.5 nM	277.7 Da LogP 4.12 TPSA 53.1	✓ Ro5	✓ Clean	`Cc1ccc(Cl)c2[nH]c3c(C(=O)O)ccc(F)c3c12`
CHEMBL541236 ChEMBL	P51788	6.52 ~302.0 nM	310.2 Da LogP 4.67 TPSA 49.3	✓ Ro5	✓ Clean	`Cc1ccc(Cl)c(Nc2ccccc2CC(=O)O)c1Cl`
CHEMBL5889110 ChEMBL	P51788	6.16 ~691.8 nM	297.1 Da LogP 4.14 TPSA 62.2	✓ Ro5	✓ Clean	`Cc1ccc(Cl)c(Nc2ncccc2C(=O)O)c1Cl`
CHEMBL1201134 ChEMBL	P51788	—	390.5 Da LogP 4.31 TPSA 83.8	✓ Ro5	✓ Clean	`CCCCC(F)(F)[C@@]1(O)CC[C@H]2[C@@H](CC(=O)[C@@H]…`
CHEMBL2103799 ChEMBL	P51788	—	404.5 Da LogP 4.56 TPSA 83.8	✓ Ro5	✓ Clean	`CC[C@H](C)CC(F)(F)[C@@]1(O)CC[C@H]2[C@@H](CC(=O…`

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
ZINC43773422 ZINC	1.000	390.5 Da LogP 4.31 TPSA 83.8	✓ Ro5	✓ Clean	`CCCCC(F)(F)[C@]1(O)CC[C@@H]2[C@H](CC(=O)[C@@H]2…`
ZINC6095281 ZINC	0.725	312.2 Da LogP 4.07 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)ccc(O)c1Cl`
ZINC1281 ZINC	0.684	296.2 Da LogP 4.36 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC1655 ZINC	0.683	296.2 Da LogP 4.74 TPSA 49.3	✓ Ro5	✓ Clean	`Cc1ccc(Cl)c(Nc2ccccc2C(=O)O)c1Cl`
ZINC4217348 ZINC	0.676	416.6 Da LogP 4.93 TPSA 80.7	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H](OC(=O)C…`
ZINC1329556 ZINC	0.667	262.7 Da LogP 3.49 TPSA 62.2	✓ Ro5	✓ Clean	`Cc1ccc(Nc2ncccc2C(=O)O)cc1Cl`
ZINC118930840 ZINC	0.657	432.6 Da LogP 4.52 TPSA 89.9	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H](OC(=O)…`
ZINC2382312535 ZINC	0.657	432.6 Da LogP 4.52 TPSA 89.9	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H](OC(=O…`
ZINC2382312536 ZINC	0.657	432.6 Da LogP 4.52 TPSA 89.9	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CC[C@@H]2[C@@H]3CC=C4C[C@@H](OC(=O…`
ZINC2382312537 ZINC	0.657	432.6 Da LogP 4.52 TPSA 89.9	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@@H]2[C@@H]3CC=C4C[C@@H](OC(=…`
ZINC247818219 ZINC	0.657	432.6 Da LogP 4.52 TPSA 89.9	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@@H]2[C@H]3CC=C4C[C@H](OC(=O)…`
ZINC247818226 ZINC	0.657	432.6 Da LogP 4.52 TPSA 89.9	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@@H]2[C@H]3CC=C4C[C@@H](OC(=O…`
ZINC253614182 ZINC	0.657	432.6 Da LogP 4.52 TPSA 89.9	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@@H]2[C@H]3CC=C4C[C@H](OC(=O)…`
ZINC253614183 ZINC	0.657	432.6 Da LogP 4.52 TPSA 89.9	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CC[C@@H]2[C@H]3CC=C4C[C@@H](OC(=O…`
ZINC159568333 ZINC	0.630	266.7 Da LogP 3.32 TPSA 62.2	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1Nc1c(F)cccc1Cl`
ZINC1545440 ZINC	0.615	213.4 Da LogP 4.65 TPSA 26.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCN`
ZINC1644076 ZINC	0.615	214.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCO`
ZINC1680803 ZINC	0.615	200.4 Da LogP 4.29 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCO`
ZINC195766643 ZINC	0.615	231.9 Da LogP 2.93 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCC[Sn+3]`
ZINC59144932 ZINC	0.615	202.4 Da LogP 4.84 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCS`
ZINC206312151 ZINC	0.614	262.7 Da LogP 3.62 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(O)c1cccc(OCc2ccccc2)c1Cl`
ZINC5781224 ZINC	0.614	310.2 Da LogP 4.83 TPSA 38.3	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1Nc1c(Cl)ccc(C)c1Cl`
ZINC1560409987 ZINC	0.613	389.5 Da LogP 4.81 TPSA 86.7	✓ Ro5	✓ Clean	`CCCCC(F)(F)[C@@]1(O)CC[C@@H]2C(CCCCCCC(=O)O)=C(…`
ZINC2506700 ZINC	0.605	340.6 Da LogP 4.47 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cccc1Br`
ZINC26395789 ZINC	0.605	279.7 Da LogP 3.85 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(F)cccc1Cl`
ZINC21509888 ZINC	0.600	283.1 Da LogP 3.83 TPSA 62.2	✓ Ro5	✓ Clean	`O=C(O)c1cccnc1Nc1ccc(Cl)c(Cl)c1`
ZINC34493982 ZINC	0.600	297.1 Da LogP 4.27 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(O)c1c(Cl)ccc(OCc2ccccc2)c1Cl`
ZINC1195 ZINC	0.596	262.7 Da LogP 3.49 TPSA 62.2	✓ Ro5	✓ Clean	`Cc1c(Cl)cccc1Nc1ncccc1C(=O)O`
ZINC2383046 ZINC	0.595	312.2 Da LogP 4.07 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cc(O)cc1Cl`
ZINC257356886 ZINC	0.594	360.5 Da LogP 4.88 TPSA 46.5	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CC[C@]2(C)C(=CC[C@@H]3[C@@H]2CC[C@…`
ZINC257356887 ZINC	0.594	360.5 Da LogP 4.88 TPSA 46.5	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CC[C@]2(C)C(=CC[C@@H]3[C@@H]2CC[C@…`
ZINC257356888 ZINC	0.594	360.5 Da LogP 4.88 TPSA 46.5	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CC[C@]2(C)C(=CC[C@@H]3[C@@H]2CC[C@…`
ZINC257356889 ZINC	0.594	360.5 Da LogP 4.88 TPSA 46.5	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CC[C@]2(C)C(=CC[C@@H]3[C@@H]2CC[C@…`
ZINC930771 ZINC	0.587	242.3 Da LogP 3.14 TPSA 62.2	✓ Ro5	✓ Clean	`Cc1ccc(Nc2ncccc2C(=O)O)cc1C`
ZINC82041028 ZINC	0.586	359.6 Da LogP 4.84 TPSA 52.3	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CC[C@@]2(C)C(=CC[C@H]3[C@@H]4CC[C@…`
ZINC82041029 ZINC	0.586	359.6 Da LogP 4.84 TPSA 52.3	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CC[C@@]2(C)C(=CC[C@H]3[C@@H]4CC[C@…`
ZINC82041030 ZINC	0.586	359.6 Da LogP 4.84 TPSA 52.3	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1CC[C@@]2(C)C(=CC[C@H]3[C@@H]4CC[C…`
ZINC82041031 ZINC	0.586	359.6 Da LogP 4.84 TPSA 52.3	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1CC[C@@]2(C)C(=CC[C@H]3[C@@H]4CC[C…`
ZINC2569322 ZINC	0.581	282.1 Da LogP 4.44 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1c(Cl)cccc1Cl`
ZINC1329558 ZINC	0.578	228.3 Da LogP 2.83 TPSA 62.2	✓ Ro5	✓ Clean	`Cc1ccccc1Nc1ncccc1C(=O)O`
ZINC3201071 ZINC	0.574	276.7 Da LogP 3.93 TPSA 46.5	✓ Ro5	✓ Clean	`Cc1c(C(=O)O)ccc(OCc2ccccc2)c1Cl`
ZINC930772 ZINC	0.574	242.3 Da LogP 3.14 TPSA 62.2	✓ Ro5	✓ Clean	`Cc1ccc(C)c(Nc2ncccc2C(=O)O)c1`
ZINC100027350 ZINC	0.571	227.4 Da LogP 4.91 TPSA 12.0	✓ Ro5	✓ Clean	`CCCCCCCCNCCCCCCC`
ZINC1627284 ZINC	0.571	214.4 Da LogP 4.94 TPSA 9.2	✓ Ro5	✓ Clean	`CCCCCCCOCCCCCCC`
ZINC1699899 ZINC	0.571	202.4 Da LogP 4.88 TPSA 0.0	✓ Ro5	✓ Clean	`CCCCCCSCCCCCC`
ZINC1724011 ZINC	0.571	213.4 Da LogP 4.52 TPSA 12.0	✓ Ro5	✓ Clean	`CCCCCCCNCCCCCCC`
ZINC2564179 ZINC	0.571	214.4 Da LogP 4.94 TPSA 9.2	✓ Ro5	✓ Clean	`CCCCCCCCOCCCCCC`
ZINC118924147 ZINC	0.569	387.6 Da LogP 4.62 TPSA 69.4	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1CC[C@@]2(C)C(=CC[C@H]3[C@@H]4CC[C@…`
ZINC118924150 ZINC	0.569	387.6 Da LogP 4.62 TPSA 69.4	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1CC[C@@]2(C)C(=CC[C@H]3[C@@H]4CC[C…`
ZINC118924152 ZINC	0.569	387.6 Da LogP 4.62 TPSA 69.4	✓ Ro5	✓ Clean	`CC(=O)O[C@@H]1CC[C@@]2(C)C(=CC[C@H]3[C@@H]4CC[C…`

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 A0A0H3GNH8

Chemistry

ChEMBL CHEMBL6028327 ChEMBL CHEMBL5788508 ChEMBL CHEMBL541236 ChEMBL CHEMBL5889110 ChEMBL CHEMBL1201134 ChEMBL CHEMBL2103799