KpKP13 Protein target profile

3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase

Accession: KP13_03868

Gene: AHE45385.1 fabA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GL47

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Length 188

Pocket druggability (P2Rank · AlphaFold DB model) 0.062

Direct ligand evidence 0 63 total records

Functional annotation 2 EC 6 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Risks to review

Microbiome similarity 186 of 4744 screened genomes (3.9%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.29. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.06.

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: 3.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.324 Higher values support similarity to known essential genes.
DEG E-value: 1.74e-130 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 92.6 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) 0.062

Structure A0A0H3GL47

Pocket Pocket 1

Druggability (FPocket) 0.288

Structure A0A0H3GL47

Pocket Pocket 5

ColabFold model

P2Rank 0.095 · Pocket 1

FPocket 0.463 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 186 / 4744 genomes with a hit

Prevalence 3.9%

Sequence

Primary amino-acid sequence viewer.

MLAILRPELKIRLTENMVDKRESYTKEDLLASGRGELFGAKGPQLPAPNMLMMDRVIKMTETGGNYDKGYVEAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVGEVKFTGQVLPTAKKVTYRIHFKRIVNRRLIMGLADGEVLVDDRLIYTANDLKVGLFQDTSAF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
GO:0008693 OBSOLETE. Catalysis of the reaction: (3R)-3-hydroxydecanoyl-[acyl-carrier protein] = 2,3-decenoyl-[acyl-carrier protein] or 3,4-decenoyl-[acyl-carrier protein] + H2O.
GO:0019171 Catalysis of the reaction: a (3R)-hydroxyacyl-[acyl-carrier-protein] = a (2E)-enoyl-[acyl-carrier-protein] + H2O.
GO:0034017 Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
GO:0006636 The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

14 records

Show feature table

Start	End	DB	Term	Name
45	177	PANTHER	PTHR30272	3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE
45	177	InterPro	IPR013114	Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ
45	174	Pfam	PF07977	FabA-like domain
45	174	InterPro	IPR013114	Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ
17	188	FunFam	G3DSA:3.10.129.10:FF:000003	3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
18	188	Hamap	MF_00405	3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase [fabA].
18	188	InterPro	IPR010083	Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA
19	185	SUPERFAMILY	SSF54637	Thioesterase/thiol ester dehydrase-isomerase
19	185	InterPro	IPR029069	HotDog domain superfamily
43	184	CDD	cd01287	FabA
43	184	InterPro	IPR010083	Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA
15	188	Gene3D	G3DSA:3.10.129.10	Hotdog Thioesterase
20	188	NCBIfam	TIGR01749	3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA
20	188	InterPro	IPR010083	Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA

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

0.062

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Surrounding area

Pocket 2 P2Rank #2

0.022

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #5

0.288

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:71-71

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_A0A0H3GL47	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03868	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.

63 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 13 records from similar proteins

Structural ligands 13 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1R3 PDB via homolog 532.6 Da · LogP 3.00 · TPSA 185.6 Open detail RCSB PDB

3MQ PDB via homolog Detail RCSB PDB

4JC PDB via homolog Detail RCSB PDB

54F PDB via homolog Detail RCSB PDB

5VO 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
1R3 RCSB PDB	4KEH	P0A6Q3	532.6 Da LogP 3.00 TPSA 185.6	2 viol.	✓ Clean	`CCCCCCCCCS(CCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=…`
3MQ RCSB PDB	4B0J	O33877	181.2 Da LogP 1.90 TPSA 46.3	✓ Ro5	✓ Clean	`c1cc(sc1)c2cc(no2)CO`
4JC RCSB PDB	7BKA	O33877	185.2 Da LogP 0.90 TPSA 60.2	✓ Ro5	✓ Clean	`CCc1ccc(cc1)S(=O)(=O)N`
54F RCSB PDB	4B0B	O33877	186.2 Da LogP 2.46 TPSA 48.1	✓ Ro5	✓ Clean	`c1ccnc(c1)Oc2cccc(c2)N`
5VO RCSB PDB	5F6R	Q8ZG80	206.2 Da LogP 2.51 TPSA 54.4	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)CCCCC(=O)O`
7SB RCSB PDB	4CL6	O33877	274.7 Da LogP 3.33 TPSA 66.7	✓ Ro5	✓ Clean	`c1cc(oc1)c2[nH]nc(n2)NCc3ccc(cc3)Cl`
C9H RCSB PDB	4B0C	O33877	171.3 Da LogP 2.09 TPSA 41.6	✓ Ro5	✓ Clean	`CCCCCSc1[nH]ncn1`
DAC RCSB PDB	1MKA	P0A6Q3	271.4 Da LogP 3.30 TPSA 46.2	✓ Ro5	✓ Clean	`CCCCCCC\C=C/C(=O)SCCNC(=O)C`
IBK RCSB PDB	4B8U	O33877	294.4 Da LogP 2.69 TPSA 64.4	✓ Ro5	✓ Clean	`CC(C)CNC(=O)COCc1cc(on1)c2cccs2`
KBP RCSB PDB	4B0I	O33877	289.4 Da LogP 2.49 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCC[C@H](CC(=O)SCCNC(=O)C)O`
TQH RCSB PDB	7BHJ	O33877	260.3 Da LogP 3.05 TPSA 66.7	✓ Ro5	✓ Clean	`Cc1ccc(o1)CNc2[nH]c(nn2)c3cccs3`
TZQ RCSB PDB	7BIS	O33877	270.6 Da LogP 3.35 TPSA 59.7	✓ Ro5	✓ Clean	`c1cc(c(cc1OCc2ccc(o2)C(=O)O)Cl)F`
U0W RCSB PDB	7BK9	O33877	258.3 Da LogP 3.05 TPSA 59.7	✓ Ro5	✓ Clean	`c1cc2c(cc1OCc3ccc(o3)C(=O)O)CCC2`

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
ZINC133424 ZINC	1.000	258.3 Da LogP 3.05 TPSA 59.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(COc2ccc3c(c2)CCC3)o1`
ZINC1712905 ZINC	1.000	206.2 Da LogP 2.51 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)c1ccccc1`
ZINC2521382 ZINC	1.000	270.6 Da LogP 3.35 TPSA 59.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(COc2ccc(F)c(Cl)c2)o1`
ZINC1560276 ZINC	0.957	248.3 Da LogP 3.68 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCC(=O)c1ccccc1`
ZINC1594493 ZINC	0.957	220.3 Da LogP 2.90 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)c1ccccc1`
ZINC2168376 ZINC	0.957	234.3 Da LogP 3.29 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)c1ccccc1`
ZINC2168378 ZINC	0.957	262.3 Da LogP 4.07 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)c1ccccc1`
ZINC1587894 ZINC	0.864	266.3 Da LogP 4.31 TPSA 34.1	✓ Ro5	✓ Clean	`O=C(CCCCC(=O)c1ccccc1)c1ccccc1`
ZINC2508114 ZINC	0.826	280.4 Da LogP 4.70 TPSA 34.1	✓ Ro5	✓ Clean	`O=C(CCCCCC(=O)c1ccccc1)c1ccccc1`
ZINC6492881 ZINC	0.815	256.4 Da LogP 1.59 TPSA 83.1	✓ Ro5	✓ Clean	`c1n[nH]c(SCCCCSc2ncn[nH]2)n1`
ZINC87591 ZINC	0.783	252.3 Da LogP 3.92 TPSA 34.1	✓ Ro5	✓ Clean	`O=C(CCCC(=O)c1ccccc1)c1ccccc1`
ZINC2378750 ZINC	0.778	282.3 Da LogP 4.18 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)c1ccc(-c2ccccc2)cc1`
ZINC6876527 ZINC	0.765	280.3 Da LogP 2.44 TPSA 64.4	✓ Ro5	✓ Clean	`CC(C)NC(=O)COCc1cc(-c2cccs2)on1`
ZINC2487633 ZINC	0.756	272.3 Da LogP 3.13 TPSA 48.7	✓ Ro5	✓ Clean	`COC(=O)c1ccc(COc2ccc3c(c2)CCC3)o1`
ZINC373453 ZINC	0.756	284.7 Da LogP 3.44 TPSA 48.7	✓ Ro5	✓ Clean	`COC(=O)c1ccc(COc2ccc(F)c(Cl)c2)o1`
ZINC133437 ZINC	0.750	252.7 Da LogP 3.21 TPSA 59.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(COc2ccc(Cl)cc2)o1`
ZINC2243653 ZINC	0.750	310.4 Da LogP 4.96 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)c1ccc(-c2ccccc2)cc1`
ZINC2345057 ZINC	0.750	242.3 Da LogP 1.20 TPSA 83.1	✓ Ro5	✓ Clean	`c1n[nH]c(SCCCSc2ncn[nH]2)n1`
ZINC2378751 ZINC	0.750	296.4 Da LogP 4.57 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)c1ccc(-c2ccccc2)cc1`
ZINC12868751 ZINC	0.740	264.3 Da LogP 2.72 TPSA 55.1	✓ Ro5	✓ Clean	`CC(C)CNC(=O)Cc1cc(-c2cccs2)on1`
ZINC20479845 ZINC	0.731	334.4 Da LogP 3.30 TPSA 64.4	✓ Ro5	✓ Clean	`O=C(COCc1cc(-c2cccs2)on1)NCc1cccs1`
ZINC6876501 ZINC	0.727	342.4 Da LogP 3.80 TPSA 64.4	✓ Ro5	✓ Clean	`C[C@H](NC(=O)COCc1cc(-c2cccs2)on1)c1ccccc1`
ZINC6876502 ZINC	0.727	342.4 Da LogP 3.80 TPSA 64.4	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)COCc1cc(-c2cccs2)on1)c1ccccc1`
ZINC6876578 ZINC	0.717	348.4 Da LogP 3.34 TPSA 64.4	✓ Ro5	✓ Clean	`O=C(COCc1cc(-c2cccs2)on1)NCCc1cccs1`
ZINC2378749 ZINC	0.714	268.3 Da LogP 3.79 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)c1ccc(-c2ccccc2)cc1`
ZINC20550797 ZINC	0.709	310.4 Da LogP 2.07 TPSA 73.6	✓ Ro5	✓ Clean	`COC[C@@H](C)NC(=O)COCc1cc(-c2cccs2)on1`
ZINC20550799 ZINC	0.709	310.4 Da LogP 2.07 TPSA 73.6	✓ Ro5	✓ Clean	`COC[C@H](C)NC(=O)COCc1cc(-c2cccs2)on1`
ZINC34484858 ZINC	0.704	204.3 Da LogP 3.02 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)CCCCC(=O)c1ccccc1`
ZINC6876482 ZINC	0.704	328.4 Da LogP 3.24 TPSA 64.4	✓ Ro5	✓ Clean	`O=C(COCc1cc(-c2cccs2)on1)NCc1ccccc1`
ZINC6876493 ZINC	0.704	278.3 Da LogP 2.22 TPSA 64.4	✓ Ro5	✓ Clean	`C=CCNC(=O)COCc1cc(-c2cccs2)on1`
ZINC28229734 ZINC	0.700	347.4 Da LogP 4.28 TPSA 51.5	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)c1ccc(COc2ccc3c(c2)CCC3)o1`
ZINC360330 ZINC	0.700	290.4 Da LogP 2.51 TPSA 72.2	✓ Ro5	✓ Clean	`CCc1ccc(CNc2ccc(S(N)(=O)=O)cc2)cc1`
ZINC6876552 ZINC	0.696	342.4 Da LogP 3.54 TPSA 64.4	✓ Ro5	✓ Clean	`Cc1ccc(CNC(=O)COCc2cc(-c3cccs3)on2)cc1`
ZINC161099 ZINC	0.696	238.3 Da LogP 3.53 TPSA 34.1	✓ Ro5	✓ Clean	`O=C(CCC(=O)c1ccccc1)c1ccccc1`
ZINC2764004 ZINC	0.694	297.4 Da LogP 3.24 TPSA 51.5	✓ Ro5	✓ Clean	`O=C(NC1CC1)c1ccc(COc2ccc3c(c2)CCC3)o1`
ZINC6876525 ZINC	0.691	342.4 Da LogP 3.28 TPSA 64.4	✓ Ro5	✓ Clean	`O=C(COCc1cc(-c2cccs2)on1)NCCc1ccccc1`
ZINC15679212 ZINC	0.690	370.5 Da LogP 4.06 TPSA 64.4	✓ Ro5	✓ Clean	`C[C@@H](CCc1ccccc1)NC(=O)COCc1cc(-c2cccs2)on1`
ZINC15679213 ZINC	0.690	370.5 Da LogP 4.06 TPSA 64.4	✓ Ro5	✓ Clean	`C[C@H](CCc1ccccc1)NC(=O)COCc1cc(-c2cccs2)on1`
ZINC133376 ZINC	0.689	266.7 Da LogP 3.52 TPSA 59.7	✓ Ro5	✓ Clean	`Cc1cc(OCc2ccc(C(=O)O)o2)ccc1Cl`
ZINC2791325 ZINC	0.686	363.4 Da LogP 4.21 TPSA 60.7	✓ Ro5	✓ Clean	`O=C(NOCc1ccccc1)c1ccc(COc2ccc3c(c2)CCC3)o1`
ZINC28229297 ZINC	0.686	313.4 Da LogP 3.88 TPSA 51.5	✓ Ro5	✓ Clean	`CC[C@@H](C)NC(=O)c1ccc(COc2ccc3c(c2)CCC3)o1`
ZINC28229299 ZINC	0.686	313.4 Da LogP 3.88 TPSA 51.5	✓ Ro5	✓ Clean	`CC[C@H](C)NC(=O)c1ccc(COc2ccc3c(c2)CCC3)o1`
ZINC6876569 ZINC	0.684	356.4 Da LogP 4.68 TPSA 64.4	✓ Ro5	✓ Clean	`CC(C)c1ccc(NC(=O)COCc2cc(-c3cccs3)on2)cc1`
ZINC133381 ZINC	0.682	252.7 Da LogP 3.21 TPSA 59.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(COc2cccc(Cl)c2)o1`
ZINC2759866 ZINC	0.680	339.4 Da LogP 4.41 TPSA 51.5	✓ Ro5	✓ Clean	`O=C(NC1CCCCC1)c1ccc(COc2ccc3c(c2)CCC3)o1`
ZINC1049561 ZINC	0.679	402.5 Da LogP 4.31 TPSA 45.9	✓ Ro5	✓ Clean	`O=C(c1ccc(COc2ccc3c(c2)CCC3)o1)N1CCN(c2ccccc2)C…`
ZINC1695218 ZINC	0.679	238.3 Da LogP 4.28 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(CCCCc1ccccc1)c1ccccc1`
ZINC2242949 ZINC	0.679	224.2 Da LogP 2.65 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)c1ccc(F)cc1`
ZINC2243769 ZINC	0.679	228.3 Da LogP 0.81 TPSA 83.1	✓ Ro5	✓ Clean	`c1n[nH]c(SCCSc2ncn[nH]2)n1`
ZINC6876534 ZINC	0.679	329.4 Da LogP 2.63 TPSA 77.2	✓ Ro5	✓ Clean	`O=C(COCc1cc(-c2cccs2)on1)NCc1ccccn1`

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 A0A0H3GL47