KpKP13 Protein target profile

Beta-ketoadipyl-CoA thiolase

Accession: KP13_04976

Gene: paaJ AHE44851.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GSN7

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Length 401

Pocket druggability (P2Rank · AlphaFold DB model) 0.781

Direct ligand evidence 0 61 total records

Functional annotation 1 EC 4 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 0.78, FPocket 0.80). 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 0.80. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.78. 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: Hit
Human identity (%): 47.083 Lower values reduce human off-target concern.
Human E-value: 2.950000000000001e-59
Gut microbiome similarity: 2.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 47.525 Higher values support similarity to known essential genes.
DEG E-value: 3.66e-107 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 98.01 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) 0.781

Structure A0A0H3GSN7

Pocket Pocket 1

Druggability (FPocket) 0.801

Structure A0A0H3GSN7

Pocket Pocket 1

ColabFold model

P2Rank 0.841 · Pocket 1

FPocket 0.699 · Pocket 6

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 118 / 4744 genomes with a hit

Prevalence 2.5%

Sequence

Primary amino-acid sequence viewer.

MRDAFICDGIRTPIGRYGGALASVRADDLAAIPLRELLSRNPGLDPAAIDDVIFGCANQAGEDNRNVAHMATLLAGYPYTVPGTTINRLCGSGLDAIGFAARAIKAGDAELLIAGGVESMSRAPFVMGKASAPYQRQAELFDTTIGWRFVNPLMAQHFGTDSMPETAENVAELLNISRADQDAFAWRSQQRTAQAQRDGILAQEIVPVQIVGRKGAVSDVREDEHPRPETTLEQLAKLKAPFRQGGVITAGNASGVNDGAAALIIASEQQAAIQGLTPRARIVAMATAGVEPRLMGLGPVPAVRKVLERAGLNINDMDLIELNEAFAAQALGVLRQLGVPDDAAHVNPNGGAIALGHPLGMSGARLALSASLELQRRGGRYALCTMCIGVGQGIAMILERV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.3.1.174

Gene Ontology (GO)

GO:0019619 The chemical reactions and pathways resulting in the breakdown of 3,4-dihydroxybenzoate.
GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
GO:0033812 Catalysis of the reaction: succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
1	401	Gene3D	G3DSA:3.40.47.10	-
1	401	InterPro	IPR016039	Thiolase-like
2	401	PANTHER	PTHR18919	ACETYL-COA C-ACYLTRANSFERASE
2	401	NCBIfam	TIGR02430	3-oxoadipyl-CoA thiolase
2	401	InterPro	IPR012793	Beta-ketoadipyl CoA thiolase
1	401	PIRSF	PIRSF000429	Ac-CoA_Ac_transf
1	401	InterPro	IPR002155	Thiolase
382	395	ProSitePatterns	PS00099	Thiolases active site.
382	395	InterPro	IPR020610	Thiolase, active site
3	272	SUPERFAMILY	SSF53901	Thiolase-like
3	272	InterPro	IPR016039	Thiolase-like
347	363	ProSitePatterns	PS00737	Thiolases signature 2.
347	363	InterPro	IPR020613	Thiolase, conserved site
5	269	Pfam	PF00108	Thiolase, N-terminal domain
5	269	InterPro	IPR020616	Thiolase, N-terminal
86	104	ProSitePatterns	PS00098	Thiolases acyl-enzyme intermediate signature.
86	104	InterPro	IPR020615	Thiolase, acyl-enzyme intermediate active site
5	400	CDD	cd00751	thiolase
5	400	InterPro	IPR002155	Thiolase
277	400	Pfam	PF02803	Thiolase, C-terminal domain
277	400	InterPro	IPR020617	Thiolase, C-terminal
6	399	NCBIfam	TIGR01930	acetyl-CoA C-acyltransferase
6	399	InterPro	IPR002155	Thiolase
1	400	FunFam	G3DSA:3.40.47.10:FF:000010	Acetyl-CoA acetyltransferase (Thiolase)
277	400	SUPERFAMILY	SSF53901	Thiolase-like
277	400	InterPro	IPR016039	Thiolase-like

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

0.781

Likely same site as FPocket 1 4.8 Å 14 shared residues 78% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

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 #1

0.801

Likely same site as P2Rank 1 4.8 Å 14 shared residues 78% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:357-357 Proton acceptor

UniProt: Active site:387-387 Proton acceptor

UniProt: Active site:90-90 Acyl-thioester intermediate

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.841

Likely same site as FPocket 6 3.4 Å 16 shared residues 80% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.029

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Surrounding area

Pocket 3 P2Rank #3

0.015

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Surrounding area

Pocket 4 P2Rank #4

0.01

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Surrounding area

Pocket 5 P2Rank #5

0.005

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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 #6

0.699 Unusual size

Likely same site as P2Rank 1 3.4 Å 16 shared residues 80% of smaller site

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Surrounding area

Pocket 2 FPocket #8

0.302

Likely same site as P2Rank 1 4.0 Å 10 shared residues 91% of smaller site

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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_A0A0H3GSN7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04976	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.

61 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

168 PDB via homolog 388.5 Da · LogP 0.15 · TPSA 131.0 Open detail RCSB PDB

3G6 PDB via homolog Detail RCSB PDB

5UG PDB via homolog Detail RCSB PDB

CAA PDB via homolog Detail RCSB PDB

COZ 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
168 RCSB PDB	1OU6	P07097	388.5 Da LogP 0.15 TPSA 131.0	✓ Ro5	✓ Clean	`CC(=O)OCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COC(=O)C(C…`
3G6 RCSB PDB	4UBT	I6XHI4	344.5 Da LogP 4.86 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@@H]([C@H]1CC[C@@H]2[C@@]1(CC[C@H]3[C@H]2CCC…`
5UG RCSB PDB	5F38	P76461	438.3 Da LogP -0.85 TPSA 191.7	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)OP(=O)(O)O)[C@@H](C(=O)NCCC(=O)…`
CAA RCSB PDB	1M1O	P07097	851.6 Da LogP -1.36 TPSA 380.7	3 viol.	✓ Clean	`CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
COZ RCSB PDB	5F38	P76461	767.5 Da LogP -1.67 TPSA 346.6	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…`
DNO RCSB PDB	2WKU	P07097	180.2 Da LogP -3.38 TPSA 118.2	✓ Ro5	✓ Clean	`C([C@H]([C@H]([C@@H]([C@@H](C=O)O)O)O)O)O`
DTT RCSB PDB	4C2K	P42765	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
O8Y RCSB PDB	6PCC	Q88N39	100.2 Da LogP 1.77 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC=O`
OPI RCSB PDB	2VU1	P07097	346.4 Da LogP -0.42 TPSA 125.0	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCC(C)(C)[C@H](C(=O)NCCC(=O)NCCO)O`
OYA RCSB PDB	6PCD	Q88N39	128.2 Da LogP 2.55 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCCCC=O`
PN5 RCSB PDB	2VU2	P07097	362.5 Da LogP 0.52 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCC(C)(C)[C@H](C(=O)NCCC(=O)NCCS)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).

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
ZINC4403984 ZINC	1.000	344.5 Da LogP 4.86 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)…`
ZINC5763280 ZINC	1.000	344.5 Da LogP 4.86 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)C…`
ZINC100056793 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC100056796 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC12953159 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC12953162 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC12953168 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC13522675 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC13522684 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC4353166 ZINC	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353167 ZINC	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353168 ZINC	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353169 ZINC	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353180 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353181 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353182 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)…`
ZINC95884213 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC9915770 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC9915771 ZINC	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC1693894 ZINC	0.938	212.4 Da LogP 4.89 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC=O`
ZINC13542964 ZINC	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@…`
ZINC253497962 ZINC	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C…`
ZINC253497963 ZINC	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@…`
ZINC2539736 ZINC	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C…`
ZINC36323232 ZINC	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C…`
ZINC3875971 ZINC	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@]…`
ZINC4096295 ZINC	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@…`
ZINC968170 ZINC	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@…`
ZINC43061660 ZINC	0.789	210.4 Da LogP 4.66 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC=O`
ZINC43061664 ZINC	0.789	210.4 Da LogP 4.66 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCC=O`
ZINC13540558 ZINC	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@…`
ZINC1848438168 ZINC	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[C…`
ZINC1848438169 ZINC	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](CO)[C@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC256518048 ZINC	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C…`
ZINC257359313 ZINC	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC257359314 ZINC	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC257359315 ZINC	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C…`
ZINC13759936 ZINC	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@H](C=O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC1700147 ZINC	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@H](C=O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC2042904 ZINC	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@H](C=O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC…`
ZINC255004289 ZINC	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@H](C=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[…`
ZINC255004290 ZINC	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@H](C=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC…`
ZINC255004291 ZINC	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@H](C=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[…`
ZINC36323209 ZINC	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@H](C=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC…`
ZINC4416476 ZINC	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@H](C=O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C…`
ZINC245224552 ZINC	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC253618174 ZINC	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@@]12CCC(=O)C=C1CC[C@H]1[C@H]2CC[C@]2(C)[C@H…`
ZINC253648944 ZINC	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC32911458 ZINC	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC3927796 ZINC	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[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 A0A0H3GSN7