Protein target profile

HT085_RS00125

prolyl oligopeptidase family serine peptidase

Genome: NZ_AP023069.1 Gene: TUM19854C_00210 E8M63_03400 N776_09215 3D evidence: AlphaFold DB model UniProt A0AA44ZGT4 UniProt A0AAQ1DU23

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Length 671

Direct ligand evidence 0 65 total records

Functional annotation 0 EC 4 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.

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
Gut microbiome off-target: Hit

Essentiality

Essential (DEG): N

Localization

Localization: Unknown

Binding-site evidence

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket Medium

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MKSYPDPYRHFENLDSAETQNFAAEANAETRARFLENDKARALSDGILNQMQDTRQIPFCQEHRARMYHFHQNAEYPKGVYRMCTAATYRSGYPEWKILFSVADFDELLGDDVYLGGVSHLVEQPNRALLTLNKSGGDTAYTLEVDLEAGELVEGGFHFPAGKNHVSWRDENSVWVCPAWDERQLTESGYPREVWLVERGKSFEESLPAYQIDKGAMMVNAWRYLDPQGSPIDLIEASDGFYTKTYLQVSSEGGAKPLNLPNDCDVVGYLAGHLLLTLRKDWHRANQSYPSGALVAVKLNRGELGAAQLLFAPDETQALESVETTKRFVVASLLENVQGRLKAWRFADSKWQEAELPHLPSGALEMTDQPWGGDVVYLAASDFTTPLTLFALDLNVMELTVMRLQPQQFVSDGIEVRQFWAVSSDGERIPYFHVGKNAAPDTPTLVYAYGGFGIPELPHYLGSVGKYWLEEGNAFVLANIRGGGEFGPRWHQAAQGISKHKSVDDLLAVVRDLSERGMSSPKHIGLQGGSNGGLITAAAFVREPQSIGALVCEVPLTDMIRYPLLSAGSSWTDEYGNPQKYEACKRRLGELSPYHNLSDGIDYPPALITTSLSDDRVHPAHALKFYAKLRETSPQSWLYSPDGGGHTGNGTQRESADKLACVLLFLKEFLG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0070012 Catalysis of the hydrolysis of a peptide bond in an oligopeptide, i.e. a molecule containing a small number (2 to 20) of amino acid residues connected by peptide bonds.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
4	633	Gene3D	G3DSA:3.40.50.1820	alpha/beta hydrolase
4	633	InterPro	IPR029058	Alpha/Beta hydrolase fold
4	409	SUPERFAMILY	SSF50993	Peptidase/esterase 'gauge' domain
5	403	Pfam	PF02897	Prolyl oligopeptidase, N-terminal beta-propeller domain
5	403	InterPro	IPR023302	Peptidase S9A, N-terminal domain
603	625	PRINTS	PR00862	Prolyl oligopeptidase serine protease (S9A) signature
603	625	InterPro	IPR002470	Peptidase S9A, prolyl oligopeptidase
528	548	PRINTS	PR00862	Prolyl oligopeptidase serine protease (S9A) signature
528	548	InterPro	IPR002470	Peptidase S9A, prolyl oligopeptidase
584	599	PRINTS	PR00862	Prolyl oligopeptidase serine protease (S9A) signature
584	599	InterPro	IPR002470	Peptidase S9A, prolyl oligopeptidase
470	494	PRINTS	PR00862	Prolyl oligopeptidase serine protease (S9A) signature
470	494	InterPro	IPR002470	Peptidase S9A, prolyl oligopeptidase
443	461	PRINTS	PR00862	Prolyl oligopeptidase serine protease (S9A) signature
443	461	InterPro	IPR002470	Peptidase S9A, prolyl oligopeptidase
498	517	PRINTS	PR00862	Prolyl oligopeptidase serine protease (S9A) signature
498	517	InterPro	IPR002470	Peptidase S9A, prolyl oligopeptidase
467	670	Pfam	PF00326	Prolyl oligopeptidase family
467	670	InterPro	IPR001375	Peptidase S9, prolyl oligopeptidase, catalytic domain
4	647	PANTHER	PTHR42881	PROLYL ENDOPEPTIDASE
414	670	SUPERFAMILY	SSF53474	alpha/beta-Hydrolases
414	670	InterPro	IPR029058	Alpha/Beta hydrolase fold
55	406	Gene3D	G3DSA:2.130.10.120	-

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 · FPocket

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

Site 1 FPocket #3

0.682

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Surrounding area

Site 2 FPocket #17

0.574

Likely same site as P2Rank 3 1.3 Å 11 shared residues 92% of smaller site

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Surrounding area

Site 3 FPocket #6

0.255

Likely same site as P2Rank 4 7.4 Å 5 shared residues 50% of smaller site

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.6

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Surrounding area

Site 2 P2Rank #2

0.353

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Surrounding area

Site 3 P2Rank #3

0.338

Likely same site as FPocket 17 1.3 Å 11 shared residues 92% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.241

Likely same site as FPocket 6 7.4 Å 5 shared residues 50% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.129

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Surrounding area

All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 1

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 HT085_RS00125	AlphaFold DB	—	—	full sequence	—	Viewing

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.

65 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 15 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 13 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

15P PDB via homolog 1529.8 Da · LogP 0.17 · TPSA 334.1 Open detail RCSB PDB

BKO PDB via homolog Detail RCSB PDB

CHEMBL189620 ChEMBL via homolog · pchembl 9.52 (~0.3 nM) Detail ChEMBL

ZPR ChEMBL via homolog · pchembl 9.46 (~0.3 nM) Detail ChEMBL

CHEMBL1086705 ChEMBL via homolog · pchembl 8.62 (~2.4 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
15P RCSB PDB	3IUR	Q9X6R4	1529.8 Da LogP 0.17 TPSA 334.1	2 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO…`
BKO RCSB PDB	6JCI	A0A1X9T5X9	466.6 Da LogP 3.51 TPSA 70.1	✓ Ro5	✓ Clean	`c1ccc(cc1)/C=C/c2ccccc2OCCCC(=O)N3CC(CC3C(=O)N4…`

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
CHEMBL189620 ChEMBL	Q9QUR6	9.52 ~0.3 nM	339.4 Da LogP 2.51 TPSA 64.4	✓ Ro5	✓ Clean	`N#C[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CCCc1ccccc1`
ZPR ChEMBL	Q9QUR6	9.46 ~0.3 nM	330.4 Da LogP 1.98 TPSA 66.9	✓ Ro5	✓ Clean	`c1ccc(cc1)COC(=O)N2CCC[C@H]2C(=O)N3CCC[C@H]3C=O`
CHEMBL1086705 ChEMBL	Q9QUR6	8.62 ~2.4 nM	378.4 Da LogP 2.94 TPSA 66.9	✓ Ro5	✓ Clean	`O=C[C@@H]1CCCN1C(=O)[C@H]1Cc2ccccc2N1C(=O)OCc1c…`
CHEMBL345903 ChEMBL	Q9QUR6	8.62 ~2.4 nM	378.4 Da LogP 2.94 TPSA 66.9	✓ Ro5	✓ Clean	`O=C[C@@H]1CCCN1C(=O)C1Cc2ccccc2N1C(=O)OCc1ccccc1`
CHEMBL154968 ChEMBL	Q9QUR6	8.52 ~3.0 nM	343.4 Da LogP 2.73 TPSA 63.7	✓ Ro5	✓ Clean	`O=C[C@@H]1CCCN1C(=O)[C@H]1CCCC[C@H]1C(=O)OCc1cc…`
CHEMBL155614 ChEMBL	Q9QUR6	8.52 ~3.0 nM	343.4 Da LogP 2.73 TPSA 63.7	✓ Ro5	✓ Clean	`O=C[C@@H]1CCCN1C(=O)[C@H]1CCCC[C@@H]1C(=O)OCc1c…`
CHEMBL3236271 ChEMBL	Q9QUR6	8.51 ~3.1 nM	342.5 Da LogP 2.66 TPSA 52.7	✓ Ro5	✓ Clean	`[11CH3]Nc1ccc(CCCC(=O)N2CCC[C@H]2C(=O)N2CCCC2)c…`
CHEMBL4549821 ChEMBL	Q9QUR6	8.48 ~3.3 nM	313.4 Da LogP 2.03 TPSA 73.2	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CCCc1ccccc1)C(=O)N1CCC[C@H]1C#N`
CHEMBL289651 ChEMBL	Q9QUR6	8.33 ~4.7 nM	314.4 Da LogP 2.62 TPSA 40.6	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCN1C(=O)CCCc1ccccc1)N1CCCC1`
CHEMBL4528594 ChEMBL	Q9QUR6	7.04 ~91.2 nM	356.4 Da LogP 1.39 TPSA 103.9	✓ Ro5	✓ Clean	`C[C@H](NC(=O)CCCc1ccccc1)C(=O)N1CCC[C@H]1c1nnn[…`
CHEMBL4465322 ChEMBL	Q9QUR6	6.58 ~263.0 nM	299.4 Da LogP 1.64 TPSA 73.2	✓ Ro5	✓ Clean	`N#C[C@@H]1CCCN1C(=O)CNC(=O)CCCc1ccccc1`
CHEMBL4556841 ChEMBL	Q9QUR6	6.53 ~295.1 nM	302.4 Da LogP 2.48 TPSA 40.6	✓ Ro5	✓ Clean	`C[C@@H](C(=O)N1CCCC1)N(C)C(=O)CCCc1ccccc1`
CHEMBL4536787 ChEMBL	Q9QUR6	—	313.4 Da LogP 1.98 TPSA 64.4	✓ Ro5	✓ Clean	`CN(CC(=O)N1CCC[C@H]1C#N)C(=O)CCCc1ccccc1`

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
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`
ZINC3803443 ZINC	1.000	330.4 Da LogP 1.98 TPSA 66.9	✓ Ro5	✓ Clean	`O=C[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)OCc1ccccc1`
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`
ZINC16124510 ZINC	0.814	233.3 Da LogP 1.99 TPSA 46.6	✓ Ro5	✓ Clean	`O=C[C@H]1CCCN1C(=O)OCc1ccccc1`
ZINC2527696 ZINC	0.814	233.3 Da LogP 1.99 TPSA 46.6	✓ Ro5	✓ Clean	`O=C[C@@H]1CCCN1C(=O)OCc1ccccc1`
ZINC14808384 ZINC	0.773	247.3 Da LogP 2.38 TPSA 46.6	✓ Ro5	✓ Clean	`O=C[C@@H]1CCCCN1C(=O)OCc1ccccc1`
ZINC2577451 ZINC	0.773	247.3 Da LogP 2.38 TPSA 46.6	✓ Ro5	✓ Clean	`O=C[C@H]1CCCCN1C(=O)OCc1ccccc1`
ZINC1576171 ZINC	0.761	346.4 Da LogP 1.86 TPSA 87.2	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)OCc1ccc…`
ZINC1576172 ZINC	0.761	346.4 Da LogP 1.86 TPSA 87.2	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)[C@H]1CCCN1C(=O)OCc1cccc…`
ZINC1576173 ZINC	0.761	346.4 Da LogP 1.86 TPSA 87.2	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)OCc1cccc…`
ZINC1576174 ZINC	0.761	346.4 Da LogP 1.86 TPSA 87.2	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)[C@H]1CCCN1C(=O)OCc1ccccc1`
ZINC575419714 ZINC	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC11622 ZINC	0.723	302.4 Da LogP 2.41 TPSA 49.9	✓ Ro5	✓ Clean	`O=C([C@H]1CCCN1C(=O)OCc1ccccc1)N1CCCC1`
ZINC57064 ZINC	0.723	302.4 Da LogP 2.41 TPSA 49.9	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCN1C(=O)OCc1ccccc1)N1CCCC1`
ZINC43763716 ZINC	0.714	360.4 Da LogP 1.95 TPSA 76.2	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)OCc1cc…`
ZINC72149813 ZINC	0.714	329.4 Da LogP 1.43 TPSA 52.7	✓ Ro5	✓ Clean	`O=C([C@H]1CNCCN1C(=O)CCCc1ccccc1)N1CCCC1`
ZINC72149814 ZINC	0.714	329.4 Da LogP 1.43 TPSA 52.7	✓ Ro5	✓ Clean	`O=C([C@@H]1CNCCN1C(=O)CCCc1ccccc1)N1CCCC1`
ZINC105333 ZINC	0.711	249.3 Da LogP 1.87 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1C(=O)OCc1ccccc1`
ZINC130672 ZINC	0.711	249.3 Da LogP 1.87 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCN1C(=O)OCc1ccccc1`
ZINC11620 ZINC	0.708	316.4 Da LogP 2.80 TPSA 49.9	✓ Ro5	✓ Clean	`O=C([C@H]1CCCN1C(=O)OCc1ccccc1)N1CCCCC1`
ZINC3803447 ZINC	0.708	316.4 Da LogP 2.80 TPSA 49.9	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCN1C(=O)OCc1ccccc1)N1CCCCC1`
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`
ZINC399373 ZINC	0.696	248.3 Da LogP 1.27 TPSA 72.6	✓ Ro5	✓ Clean	`NC(=O)[C@@H]1CCCN1C(=O)OCc1ccccc1`
ZINC399374 ZINC	0.696	248.3 Da LogP 1.27 TPSA 72.6	✓ Ro5	✓ Clean	`NC(=O)[C@H]1CCCN1C(=O)OCc1ccccc1`
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`
ZINC139245161 ZINC	0.681	247.3 Da LogP 2.38 TPSA 46.6	✓ Ro5	✓ Clean	`CC(=O)[C@@H]1CCCN1C(=O)OCc1ccccc1`
ZINC197339880 ZINC	0.681	247.3 Da LogP 2.38 TPSA 46.6	✓ Ro5	✓ Clean	`CC(=O)[C@H]1CCCN1C(=O)OCc1ccccc1`
ZINC95642228 ZINC	0.681	247.3 Da LogP 1.72 TPSA 79.4	✓ Ro5	✓ Clean	`N=C(N)[C@H]1CCCN1C(=O)OCc1ccccc1`
ZINC95642229 ZINC	0.681	247.3 Da LogP 1.72 TPSA 79.4	✓ Ro5	✓ Clean	`N=C(N)[C@@H]1CCCN1C(=O)OCc1ccccc1`
ZINC57122 ZINC	0.674	263.3 Da LogP 2.26 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCCN1C(=O)OCc1ccccc1`
ZINC57123 ZINC	0.674	263.3 Da LogP 2.26 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCCN1C(=O)OCc1ccccc1`
ZINC60399 ZINC	0.673	338.4 Da LogP 3.10 TPSA 58.6	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)[C@H]1CCCN1C(=O)OCc1ccccc1`
ZINC60400 ZINC	0.673	338.4 Da LogP 3.10 TPSA 58.6	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)[C@@H]1CCCN1C(=O)OCc1ccccc1`
ZINC34090537 ZINC	0.667	318.4 Da LogP 1.65 TPSA 59.1	✓ Ro5	✓ Clean	`O=C([C@H]1CCCN1C(=O)OCc1ccccc1)N1CCOCC1`
ZINC575432150 ZINC	0.667	344.4 Da LogP -0.89 TPSA 100.5	✓ Ro5	✓ Clean	`COCCOCCOCCS(=O)(=O)CCOCCOCCO`

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.

HT085_RS00125

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

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Localization

Binding-site evidence

Sequence

Functional annotations

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence