KpKP13 Protein target profile

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Accession: KP13_01121

Gene: AHE42485.1 murA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GYZ6

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Length 419

Pocket druggability (P2Rank · AlphaFold DB model) 0.952

Direct ligand evidence 0 74 total records

Functional annotation 1 EC 9 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

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.95. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 12.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.124 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 96.35 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) 0.952

Structure A0A0H3GYZ6

Pocket Pocket 1

Druggability (FPocket) 0.245

Structure A0A0H3GYZ6

Pocket Pocket 22

ColabFold model

P2Rank 0.947 · Pocket 1

FPocket 0.161 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 609 / 4744 genomes with a hit

Prevalence 12.8%

Sequence

Primary amino-acid sequence viewer.

MDKFRVQGPTRLQGEVTISGAKNAALPILFSALLAEEPVEIQNVPKLKDIDTTMKLLSQLGAKVERNGSVWIDAGPVDVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHISGLEQLGAEIKLEEGYVKASVSGRLKGAHIVMDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLNALGAKITGQGSDRITIEGVQRLGGGVYRVLPDRIETGTFLVAAAISGGKILCRNAQPDTLDAVLAKLRDAGADIETGEDWISLDMHGNRPKAVNVRTAPHPGFPTDMQAQFTLLNLVAEGTGVITETIFENRFMHIPELIRMGAHAEIESNTAICHGVKQLSGAQVMATDLRASASLVLAGCIAEGTTIVDRIYHIDRGYERIEDKLQALGANIQRVKGE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.5.1.7

Gene Ontology (GO)

GO:0008760 Catalysis of the reaction: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine.
GO:0019277 The chemical reactions and pathways resulting in the formation of UDP-N-acetylgalactosamine, a substance composed of N-acetylgalactosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
GO:0008360 Any process that modulates the surface configuration of a cell.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
2	417	PANTHER	PTHR43783	UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE
1	418	SUPERFAMILY	SSF55205	EPT/RTPC-like
1	418	InterPro	IPR013792	RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta
5	414	Gene3D	G3DSA:3.65.10.10	Enolpyruvate transferase domain
5	414	InterPro	IPR036968	Enolpyruvate transferase domain superfamily
6	406	Pfam	PF00275	EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
6	406	InterPro	IPR001986	Enolpyruvate transferase domain
1	416	Hamap	MF_00111	UDP-N-acetylglucosamine 1-carboxyvinyltransferase [murA].
1	416	InterPro	IPR005750	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
399	419	Coils	Coil	Coil
214	414	FunFam	G3DSA:3.65.10.10:FF:000002	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
12	409	CDD	cd01555	UdpNAET
12	409	InterPro	IPR005750	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
1	415	NCBIfam	TIGR01072	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
1	415	InterPro	IPR005750	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
21	228	Gene3D	G3DSA:3.65.10.10	Enolpyruvate transferase domain
21	228	InterPro	IPR036968	Enolpyruvate transferase domain superfamily

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

0.952

Likely same site as FPocket 22 2.2 Å 34 shared residues 97% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.027

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Surrounding area

Pocket 3 P2Rank #3

0.009

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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 #22

0.245 Unusual size

Likely same site as P2Rank 1 2.2 Å 34 shared residues 97% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:115-115 Proton donor

UniProt: Binding site:120-124

UniProt: Binding site:160-163

UniProt: Binding site:22-23

UniProt: Binding site:305-305

UniProt: Binding site:327-327

UniProt: Binding site:91-91

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_A0A0H3GYZ6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01121	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.

74 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 24 records from similar proteins

Structural ligands 18 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0V5 PDB via homolog 170.1 Da · LogP -0.43 · TPSA 104.1 Open detail RCSB PDB

2AN PDB via homolog Detail RCSB PDB

EPU PDB via homolog Detail RCSB PDB

EPZ PDB via homolog Detail RCSB PDB

FFQ 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
0V5 RCSB PDB	6CN1	Q88P88	170.1 Da LogP -0.43 TPSA 104.1	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)OP(=O)(O)O`
2AN RCSB PDB	1EYN	P33038	299.4 Da LogP 3.83 TPSA 66.4	✓ Ro5	✓ Clean	`c1ccc(cc1)Nc2cccc3c2c(ccc3)S(=O)(=O)O`
EPU RCSB PDB	1RYW	P33038	677.4 Da LogP -4.03 TPSA 332.2	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
EPZ RCSB PDB	3SU9	P33038	679.4 Da LogP -4.15 TPSA 332.2	3 viol.	✓ Clean	`C[C@H](C(=O)O)O[C@@H]1[C@H]([C@H](O[C@@H]([C@H]…`
FFQ RCSB PDB	3LTH	P33038	140.1 Da LogP -0.11 TPSA 77.8	✓ Ro5	✓ Clean	`CC[C@H](O)P(=O)(O)O`
GG6 RCSB PDB	2RL2	P45025	156.1 Da LogP -1.14 TPSA 98.0	✓ Ro5	✓ Clean	`C[C@@H]([C@@H](O)P(=O)(O)O)O`
HAI RCSB PDB	1DLG	P33038	100.2 Da LogP 0.56 TPSA 27.6	✓ Ro5	✓ Clean	`C1CCC(CC1)[NH3+]`
MOE RCSB PDB	3SWI	P33038	75.1 Da LogP -1.01 TPSA 32.3	✓ Ro5	✓ Clean	`COCC[O-]`
PG0 RCSB PDB	3SWI	P33038	120.1 Da LogP -0.36 TPSA 38.7	✓ Ro5	✓ Clean	`COCCOCCO`
PO3 RCSB PDB	3ISS	P0A749	79.0 Da LogP -1.64 TPSA 63.2	✓ Ro5	✓ Clean	`[O-][P-](=O)[O-]`
TAV RCSB PDB	1YBG	P33038	662.7 Da LogP 4.56 TPSA 184.4	1 viol.	✓ Clean	`CN([C@@H](CC(=O)O)C(=O)O)C(=O)c1cc(ccc1NS(=O)(=…`
TET RCSB PDB	1A2N	P0A749	793.4 Da LogP -4.77 TPSA 398.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
TR9 RCSB PDB	3KQA	P33038	156.1 Da LogP -0.28 TPSA 74.6	✓ Ro5	✓ Clean	`CC1=C(C(=O)C[C@@H](C1=O)O)O`
UD1 RCSB PDB	3LTH	P33038	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
UD2 RCSB PDB	3SWI	P33038	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@H]([C@H](O[C@@H]1O[P@@](…`
UDA RCSB PDB	1Q3G	P33038	775.4 Da LogP -4.72 TPSA 398.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
UPG RCSB PDB	4E7B	P33038	566.3 Da LogP -4.79 TPSA 297.0	3 viol.	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
UPN RCSB PDB	3SWI	P33038	677.4 Da LogP -4.03 TPSA 332.2	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@H]([C@H](O[C@@H]1O[P@](=…`

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
FCN ChEMBL	P0A749	7.00 ~100.0 nM	138.1 Da LogP -0.09 TPSA 70.1	✓ Ro5	✓ Clean	`C[C@H]1[C@H](O1)P(=O)(O)O`
CHEMBL1200331 ChEMBL	P0A749	—	259.2 Da LogP -2.43 TPSA 156.8	1 viol.	✓ Clean	`C[C@@H]1O[C@@H]1P(=O)(O)O.NC(CO)(CO)CO`
CHEMBL2335230 ChEMBL	P0A749	—	296.9 Da LogP 3.01 TPSA 56.3	✓ Ro5	✓ Clean	`O=[N+]([O-])/C(Br)=C/c1ccc(Br)o1`
CHEMBL5219390 ChEMBL	P0A749	—	509.0 Da LogP 6.45 TPSA 92.9	2 viol.	✓ Clean	`CC(C)(C)OC(=O)C1=C(O)C(=O)N(c2nc3ccccc3s2)C1c1c…`
CHEMBL5417308 ChEMBL	P0A749	—	229.8 Da LogP 2.70 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(CCl)NC1CCCC2CCCCC21`
FOM ChEMBL	P0A749	—	183.1 Da LogP -0.60 TPSA 98.1	✓ Ro5	✓ Clean	`C(CN(C=O)O)CP(=O)(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
ZINC1532216 ZINC	1.000	299.4 Da LogP 3.83 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)c1cccc2cccc(Nc3ccccc3)c12`
ZINC1580161 ZINC	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059 ZINC	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860 ZINC	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC7571 ZINC	1.000	296.9 Da LogP 3.01 TPSA 56.3	✓ Ro5	✓ Clean	`O=[N+]([O-])/C(Br)=C/c1ccc(Br)o1`
ZINC1712810 ZINC	0.757	313.4 Da LogP 4.14 TPSA 66.4	✓ Ro5	✓ Clean	`Cc1ccc(Nc2cccc3cccc(S(=O)(=O)O)c23)cc1`
ZINC575419714 ZINC	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC115163232 ZINC	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC258837490 ZINC	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC5162495 ZINC	0.697	249.3 Da LogP 2.68 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)c1ccccc1Nc1ccccc1`
ZINC12501520 ZINC	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1692489 ZINC	0.688	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC3874716 ZINC	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC4530388 ZINC	0.688	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5178829 ZINC	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5701172 ZINC	0.688	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	0.688	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC2053549711 ZINC	0.676	232.0 Da LogP 2.68 TPSA 56.3	✓ Ro5	✓ Clean	`CC(=Cc1ccc(Br)o1)[N+](=O)[O-]`
ZINC34984414 ZINC	0.676	232.0 Da LogP 2.68 TPSA 56.3	✓ Ro5	✓ Clean	`C/C(=C\c1ccc(Br)o1)[N+](=O)[O-]`
ZINC575432150 ZINC	0.667	344.4 Da LogP -0.89 TPSA 100.5	✓ Ro5	✓ Clean	`COCCOCCOCCS(=O)(=O)CCOCCOCCO`
ZINC1857524240 ZINC	0.652	207.3 Da LogP -0.75 TPSA 60.0	✓ Ro5	✓ Clean	`COCCNCCOCCOCCO`
ZINC71772395 ZINC	0.605	265.3 Da LogP 2.04 TPSA 83.5	✓ Ro5	✓ Clean	`CC(=O)Nc1cccc2cccc(S(=O)(=O)O)c12`
ZINC5650743 ZINC	0.600	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.600	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC116981890 ZINC	0.594	288.3 Da LogP 1.33 TPSA 108.7	✓ Ro5	✓ Clean	`O=S(=O)(O)c1cccc2cccc(S(=O)(=O)O)c12`
ZINC116078641 ZINC	0.583	222.2 Da LogP -0.80 TPSA 74.2	✓ Ro5	✓ Clean	`COC(=O)COCCOCCOCCO`
ZINC1857790631 ZINC	0.583	280.3 Da LogP -0.39 TPSA 83.5	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCOCCO`
ZINC196151418 ZINC	0.583	266.3 Da LogP -0.78 TPSA 83.5	✓ Ro5	✓ Clean	`COC(=O)COCCOCCOCCOCCO`
ZINC202958272 ZINC	0.583	236.3 Da LogP -0.41 TPSA 74.2	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCO`
ZINC34111591 ZINC	0.583	207.3 Da LogP -1.06 TPSA 62.2	✓ Ro5	✓ Clean	`COCCOCCN(CCO)CCO`
ZINC642881862 ZINC	0.583	324.4 Da LogP -0.38 TPSA 92.7	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCOCCOCCO`
ZINC2169453 ZINC	0.575	266.3 Da LogP 1.46 TPSA 92.4	✓ Ro5	✓ Clean	`NCCNc1cccc2cccc(S(=O)(=O)O)c12`
ZINC5575424 ZINC	0.565	200.0 Da LogP -1.37 TPSA 141.4	✓ Ro5	✓ Clean	`O=C(O)C(OP(=O)(O)O)C(=O)O`
ZINC22590709 ZINC	0.561	312.4 Da LogP 3.54 TPSA 72.2	✓ Ro5	✓ Clean	`Cc1ccc(Nc2cccc3cccc(S(N)(=O)=O)c23)cc1`
ZINC1586638 ZINC	0.559	223.4 Da LogP 3.26 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H]1CCCC[C@H]1C1CCCCC1`
ZINC1586639 ZINC	0.559	223.4 Da LogP 3.26 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1CCCC[C@H]1C1CCCCC1`
ZINC1586640 ZINC	0.559	223.4 Da LogP 3.26 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H]1CCCC[C@@H]1C1CCCCC1`
ZINC1586641 ZINC	0.559	223.4 Da LogP 3.26 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1CCCC[C@@H]1C1CCCCC1`
ZINC139635624 ZINC	0.556	207.3 Da LogP 2.65 TPSA 29.1	✓ Ro5	✓ Clean	`C=CC(=O)N[C@@H]1CCC[C@H]2CCCC[C@@H]21`
ZINC139635897 ZINC	0.556	207.3 Da LogP 2.65 TPSA 29.1	✓ Ro5	✓ Clean	`C=CC(=O)N[C@@H]1CCC[C@@H]2CCCC[C@@H]21`
ZINC141055552 ZINC	0.556	207.3 Da LogP 2.65 TPSA 29.1	✓ Ro5	✓ Clean	`C=CC(=O)N[C@@H]1CCC[C@@H]2CCCC[C@H]21`
ZINC141055927 ZINC	0.556	207.3 Da LogP 2.65 TPSA 29.1	✓ Ro5	✓ Clean	`C=CC(=O)N[C@@H]1CCC[C@H]2CCCC[C@H]21`
ZINC12959005 ZINC	0.551	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)…`

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 A0A0H3GYZ6

Chemistry

ChEMBL FCN ChEMBL CHEMBL1200331 ChEMBL CHEMBL2335230 ChEMBL CHEMBL5219390 ChEMBL CHEMBL5417308 ChEMBL FOM