KpATCC43816 Protein target profile

hypothetical protein

Accession: VK055_4279

Gene: AIK82824.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GX39

Export view

Length 719

Pocket druggability (P2Rank · AlphaFold DB model) 0.915

Direct ligand evidence 0 64 total records

Functional annotation 0 EC 8 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 0.92, FPocket 0.95). 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 0.95. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.92. 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 (%): 36.986 Lower values reduce human off-target concern.
Human E-value: 2.21e-08
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 37.975 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 91.67 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) 0.915

Structure A0A0H3GX39

Pocket Pocket 1

Druggability (FPocket) 0.949

Structure A0A0H3GX39

Pocket Pocket 38

ColabFold model

P2Rank 0.956 · Pocket 1

FPocket 0.972 · Pocket 51

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 109 / 4744 genomes with a hit

Prevalence 2.3%

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.

MLLGFFRLLFKGLYRVRLTGDTQALYQQKVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQRWFMRALTPIIDFVPLDPTKPMSIKHLVRLIEQGRPVVIFPEGRISVSGSLMKIYDGAAFVAAKSQATIVPLRIEGAELTPFSRLKGLVKRRLFPRIQLHLLPPTHLPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQDRFGARKPCVEDINFQPDTYRKLLTKTLFVARILEKYSQPGEKIGLMLPNAGISAAVIFGAIARGRIPAMMNYTAGVKGLSSAIAAAELNTIFTSRTFLDKGKLWHLPEQLTQVRWVFLEDLKGDITLADKLWIFAHLLAPRLAQVKQQPEDAAMILFTSGSEGNPKGVVHSHKSLLSNVEQIKTIADFTANDRFMSALPLFHSFGLTVGLLTPLLTGAEVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLANYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKVGTVGRILPGMDARLLAMPGIEQGGRLQLKGPNIMKGYLRVENPGVLEAPAAENQHGEMEAGWYDTGDIVTFDEQGYVRIQGRAKRFAKIAGEMISLEMVEQVALGASPDKMHATAIKQDASKGEALVLFTTDNELTREALLRYARQHGVPELAVPRDIRWLKQLPVLGSGKPDYVTLKNMVDEAETTHE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Subcellular localization

Localization: CytoplasmicMembrane

Gene Ontology (GO)

GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
GO:0008779 Catalysis of the reaction: acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine.
GO:0008654 The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester.
GO:0008922 Catalysis of the reaction: a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons.
GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0031956 Catalysis of the reaction: a medium-chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate. A medium-chain fatty acid has an aliphatic tail containing 6 to 12 carbons.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
7	188	CDD	cd07989	LPLAT_AGPAT-like
203	713	SUPERFAMILY	SSF56801	Acetyl-CoA synthetase-like
16	38	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
370	381	ProSitePatterns	PS00455	Putative AMP-binding domain signature.
370	381	InterPro	IPR020845	AMP-binding, conserved site
1	717	Hamap	MF_01162	Bifunctional protein Aas [aas].
1	717	InterPro	IPR023775	Bifunctional protein Aas
11	15	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	15	Phobius	SIGNAL_PEPTIDE	Signal peptide region
96	701	PANTHER	PTHR43201	ACYL-COA SYNTHETASE
10	170	SUPERFAMILY	SSF69593	Glycerol-3-phosphate (1)-acyltransferase
16	137	Pfam	PF01553	Acyltransferase
16	137	InterPro	IPR002123	Phospholipid/glycerol acyltransferase
615	717	Gene3D	G3DSA:3.30.300.30	-
615	717	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily
59	257	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
258	277	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
30	140	SMART	SM00563	plsc_2
30	140	InterPro	IPR002123	Phospholipid/glycerol acyltransferase
1	1	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
39	58	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
211	612	Gene3D	G3DSA:3.40.50.12780	-
211	612	InterPro	IPR042099	ANL, N-terminal domain
2	10	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
231	619	Pfam	PF00501	AMP-binding enzyme
231	619	InterPro	IPR000873	AMP-dependent synthetase/ligase domain
278	719	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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 · P2Rank

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

Pocket 1 P2Rank #1

0.915

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.895

Likely same site as FPocket 38 0.8 Å 18 shared residues 100% of smaller site

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.786

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.631

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.398

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #38

0.949

Likely same site as P2Rank 2 0.8 Å 18 shared residues 100% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:36-36

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.956

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.915

Likely same site as FPocket 51 2.5 Å 18 shared residues 100% of smaller site

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.785

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.341

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.327

Likely same site as FPocket 50 3.4 Å 14 shared residues 78% of smaller site

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #51

0.972 Unusual size

Likely same site as P2Rank 2 2.5 Å 18 shared residues 100% of smaller site

Show in viewer

Surrounding area

Pocket 2 FPocket #50

0.215 Unusual size

Likely same site as P2Rank 5 3.4 Å 14 shared residues 78% of smaller site

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_A0A0H3GX39	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4279	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.

64 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 14 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3UK PDB via homolog 466.3 Da · LogP -0.42 · TPSA 218.2 Open detail RCSB PDB

9SN PDB via homolog Detail RCSB PDB

JSA PDB via homolog Detail RCSB PDB

MCA PDB via homolog Detail RCSB PDB

MLC 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
3UK RCSB PDB	5OE3	Q9I4X3	466.3 Da LogP -0.42 TPSA 218.2	1 viol.	✓ Clean	`c1ccc(c(c1)C(=O)OP(=O)(O)OC[C@@H]2[C@H]([C@H]([…`
9SN RCSB PDB	5OE6	Q9I4X3	484.3 Da LogP -0.28 TPSA 218.2	1 viol.	✓ Clean	`c1cc(c(c(c1)F)C(=O)OP(=O)(O)OC[C@@H]2[C@H]([C@H…`
JSA RCSB PDB	5ZRN	P9WQ37	530.6 Da LogP 1.12 TPSA 194.9	2 viol.	✓ Clean	`CCCCCCCCCCC[C@H](NS(=O)(=O)OC[C@@H]1[C@H]([C@H]…`
MCA RCSB PDB	3NYQ	Q9L0A2	867.6 Da LogP -1.61 TPSA 400.9	3 viol.	✓ Clean	`C[C@H](C(=O)O)C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)…`
MLC RCSB PDB	3NYR	Q9L0A2	853.6 Da LogP -1.86 TPSA 400.9	3 viol.	✓ Clean	`CC(C)(CO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]…`
MLI RCSB PDB	3R44	P9WQ37	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
OXD RCSB PDB	5IE3	Q9SMT7	90.0 Da LogP -0.84 TPSA 74.6	✓ Ro5	✓ Clean	`C(=O)(C(=O)O)O`
SRT RCSB PDB	5IE0	Q9SMT7	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@H](C(=O)O)O)(C(=O)O)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL371502 ChEMBL	Q9I4X3	7.06 ~87.1 nM	466.4 Da LogP -1.58 TPSA 212.0	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(=O)(=O)NC(=O)c2…`
CHEMBL377483 ChEMBL	Q9I4X3	6.96 ~109.6 nM	465.4 Da LogP -2.00 TPSA 214.8	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CNS(=O)(=O)NC(=O)c2…`
CHEMBL1315633 ChEMBL	Q94696	—	365.2 Da LogP -2.69 TPSA 217.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
CHEMBL1326967 ChEMBL	Q94696	—	226.3 Da LogP 3.55 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccccc3)sc2c1`
CHEMBL1375740 ChEMBL	Q94696	—	255.3 Da LogP 2.95 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1F`
CHEMBL3392220 ChEMBL	Q94696	—	448.4 Da LogP -0.51 TPSA 189.3	1 viol.	✓ Clean	`CCN(CC)CC.Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(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
ZINC361067 ZINC	1.000	226.3 Da LogP 3.55 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccccc3)sc2c1`
ZINC225954 ZINC	0.806	241.3 Da LogP 3.13 TPSA 64.9	✓ Ro5	✓ Clean	`Nc1ccc(-c2nc3ccc(N)cc3s2)cc1`
ZINC235533 ZINC	0.788	241.3 Da LogP 3.13 TPSA 64.9	✓ Ro5	✓ Clean	`Nc1cccc(-c2nc3ccc(N)cc3s2)c1`
ZINC8345430 ZINC	0.750	312.3 Da LogP 2.07 TPSA 86.9	✓ Ro5	✓ Clean	`O=C(CNC(=O)c1ccccc1F)Nc1nc2ccccc2[nH]1`
ZINC381794 ZINC	0.744	253.3 Da LogP 2.52 TPSA 78.0	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1O`
ZINC405324 ZINC	0.744	271.7 Da LogP 3.47 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1Cl`
ZINC4538149 ZINC	0.735	227.3 Da LogP 2.94 TPSA 51.8	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccncc3)sc2c1`
ZINC6653557 ZINC	0.721	309.2 Da LogP 3.37 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(F)c(F)c(F)c1F`
ZINC235507 ZINC	0.714	242.3 Da LogP 3.25 TPSA 59.1	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccc(O)cc3)sc2c1`
ZINC5589186 ZINC	0.714	260.7 Da LogP 4.20 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccc(Cl)cc3)sc2c1`
ZINC13218513 ZINC	0.707	316.2 Da LogP 3.58 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1Br`
ZINC441673 ZINC	0.707	251.3 Da LogP 3.12 TPSA 57.8	✓ Ro5	✓ Clean	`Cc1ccccc1C(=O)Nc1nc2ccccc2[nH]1`
ZINC6506834 ZINC	0.707	363.2 Da LogP 3.42 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1I`
ZINC12589519 ZINC	0.705	307.7 Da LogP 3.75 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(F)c(F)cc1Cl`
ZINC4245368 ZINC	0.703	227.3 Da LogP 2.94 TPSA 51.8	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3cccnc3)sc2c1`
ZINC4245370 ZINC	0.703	242.3 Da LogP 3.25 TPSA 59.1	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3cccc(O)c3)sc2c1`
ZINC62538947 ZINC	0.703	260.7 Da LogP 4.20 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3cccc(Cl)c3)sc2c1`
ZINC12546511 ZINC	0.698	305.3 Da LogP 3.83 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1C(F)(F)F`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC12588992 ZINC	0.690	306.2 Da LogP 4.12 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cccc(Cl)c1Cl`
ZINC13218630 ZINC	0.690	287.3 Da LogP 3.97 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cccc2ccccc12`
ZINC17304201 ZINC	0.689	324.1 Da LogP 4.26 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(F)c(Cl)cc1Cl`
ZINC9115469 ZINC	0.681	285.3 Da LogP 2.96 TPSA 67.0	✓ Ro5	✓ Clean	`COc1ccc(C(=O)Nc2nc3ccccc3[nH]2)c(F)c1`
ZINC6589933 ZINC	0.674	341.4 Da LogP 4.05 TPSA 74.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1C(=O)c1ccccc1`
ZINC12544692 ZINC	0.667	330.4 Da LogP 2.19 TPSA 103.9	✓ Ro5	✓ Clean	`CS(=O)(=O)Nc1ccccc1C(=O)Nc1nc2ccccc2[nH]1`
ZINC12538671 ZINC	0.659	306.2 Da LogP 4.12 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(Cl)ccc1Cl`
ZINC13228399 ZINC	0.659	265.3 Da LogP 3.43 TPSA 57.8	✓ Ro5	✓ Clean	`Cc1cccc(C(=O)Nc2nc3ccccc3[nH]2)c1C`
ZINC14048562 ZINC	0.659	270.3 Da LogP 2.50 TPSA 70.7	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cccnc1S`
ZINC406618 ZINC	0.659	267.3 Da LogP 2.82 TPSA 67.0	✓ Ro5	✓ Clean	`COc1ccccc1C(=O)Nc1nc2ccccc2[nH]1`
ZINC9910431 ZINC	0.659	273.2 Da LogP 3.09 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccc(F)c(F)c1`
ZINC1595024 ZINC	0.657	245.7 Da LogP 4.62 TPSA 12.9	✓ Ro5	✓ Clean	`Clc1ccc2nc(-c3ccccc3)sc2c1`
ZINC1682939 ZINC	0.657	229.3 Da LogP 4.10 TPSA 12.9	✓ Ro5	✓ Clean	`Fc1ccc2nc(-c3ccccc3)sc2c1`
ZINC29413288 ZINC	0.657	227.3 Da LogP 3.67 TPSA 33.1	✓ Ro5	✓ Clean	`Oc1ccc2nc(-c3ccccc3)sc2c1`
ZINC402244 ZINC	0.657	225.3 Da LogP 4.27 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1ccc2nc(-c3ccccc3)sc2c1`
ZINC73638544 ZINC	0.657	290.2 Da LogP 4.73 TPSA 12.9	✓ Ro5	✓ Clean	`Brc1ccc2nc(-c3ccccc3)sc2c1`
ZINC12603357 ZINC	0.652	289.7 Da LogP 3.61 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccc(F)cc1Cl`
ZINC17304200 ZINC	0.652	334.1 Da LogP 3.72 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccc(F)cc1Br`
ZINC6567101 ZINC	0.652	303.3 Da LogP 3.42 TPSA 67.0	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1OC(F)F`
ZINC72704 ZINC	0.652	331.4 Da LogP 4.62 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(-c2nc3ccccc3[nH]2)cc1)c1ccccc1F`
ZINC6566971 ZINC	0.651	273.2 Da LogP 3.09 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(F)cc(F)c1`
ZINC936069043 ZINC	0.649	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C…`
ZINC6299 ZINC	0.647	226.3 Da LogP 3.55 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc(-c2nc3ccccc3s2)cc1`

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 A0A0H3GX39

Chemistry

ChEMBL CHEMBL371502 ChEMBL CHEMBL377483 ChEMBL CHEMBL1315633 ChEMBL CHEMBL1326967 ChEMBL CHEMBL1375740 ChEMBL CHEMBL3392220