Protein target profile

KP13_03535

Coproporphyrinogen-III oxidase, aerobic

Genome: KpKP13 Gene: AHE43341.1 hemF 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GVY6

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Length 299

Pocket druggability 0.943

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 6 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: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.94, P2Rank 0.99). 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 0.94. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.99. 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 (%): 60.0 Lower values reduce human off-target concern.
Human E-value: 4.92e-11
Gut microbiome similarity: 3.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 73.579 Higher values support similarity to known essential genes.
DEG E-value: 1.91e-163 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.39 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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 0.943

Structure A0A0H3GVY6

Pocket Pocket 23

P2Rank 0.986

Structure A0A0H3GVY6

Pocket Pocket 1

ColabFold model

FPocket 0.553 · Pocket 20

P2Rank 0.987 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 165 / 4744 genomes with a hit

Prevalence 3.5%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GVY6

Chemistry

ChEMBL CHEMBL2270643

Sequence

Primary amino-acid sequence viewer.

MKPDAAQVKTFLLQLQDSLCQQLSAVDGAPFIEDAWQREGGGGGRSRVLREGRVFEQAGVNFSHVHGDAMPASATAHRPELAGRSFEAMGVSLVVHPLNPYVPTSHANVRFFIAEKPGADPVWWFGGGFDLTPYYGFEEDAVHWHRTARDLCLPFGEEVYPRYKKWCDDYFYLKHRQEQRGIGGLFFDDLNTPDFDHCFAFMQAVGNGYADAYLPIVERRKATPYGERERHFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPEPGSPEAALSEFIQVRDWL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1.3.3.3

Gene Ontology (GO)

GO:0006779 The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
GO:0004109 Catalysis of the reaction: coproporphyrinogen III + 2 H+ + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0046872 Binding to a metal ion.
GO:0042803 Binding to an identical protein to form a homodimer.
GO:0006782 The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

29 records

Show feature table

Start	End	DB	Term	Name
1	299	PIRSF	PIRSF000166	Coproporphyri_ox
1	299	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
1	299	Gene3D	G3DSA:3.40.1500.10	Coproporphyrinogen III oxidase, aerobic
1	299	InterPro	IPR036406	Oxygen-dependent coproporphyrinogen III oxidase superfamily
164	188	ProSitePatterns	PS01021	Coproporphyrinogen III oxidase signature.
164	188	InterPro	IPR018375	Coproporphyrinogen III oxidase, conserved site
5	299	PANTHER	PTHR10755	COPROPORPHYRINOGEN III OXIDASE, MITOCHONDRIAL
5	299	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
123	145	PRINTS	PR00073	Coprogen oxidase signature
123	145	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
46	67	PRINTS	PR00073	Coprogen oxidase signature
46	67	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
88	112	PRINTS	PR00073	Coprogen oxidase signature
88	112	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
29	45	PRINTS	PR00073	Coprogen oxidase signature
29	45	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
160	189	PRINTS	PR00073	Coprogen oxidase signature
160	189	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
260	286	PRINTS	PR00073	Coprogen oxidase signature
260	286	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
232	259	PRINTS	PR00073	Coprogen oxidase signature
232	259	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
4	298	SUPERFAMILY	SSF102886	Coproporphyrinogen III oxidase
4	298	InterPro	IPR036406	Oxygen-dependent coproporphyrinogen III oxidase superfamily
2	275	Hamap	MF_00333	Oxygen-dependent coproporphyrinogen-III oxidase [hemF].
2	275	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic
1	299	FunFam	G3DSA:3.40.1500.10:FF:000001	Oxygen-dependent coproporphyrinogen-III oxidase
7	298	Pfam	PF01218	Coproporphyrinogen III oxidase
7	298	InterPro	IPR001260	Coproporphyrinogen III oxidase, aerobic

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 #23

0.943

Unusual size

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Surrounding area

Site 2 FPocket #5

0.339

Likely same site as P2Rank 1 2.5 Å 34 shared residues 87% of smaller site

Unusual size

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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

0.986

Likely same site as FPocket 5 2.5 Å 34 shared residues 87% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.107

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Surrounding area

Site 3 P2Rank #3

0.078

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Surrounding area

Site 4 P2Rank #4

0.021

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Surrounding area

Residue sets

UniProt: Active site:106-106 Proton donor

UniProt: Binding site:106-106

UniProt: Binding site:108-110

UniProt: Binding site:145-145

UniProt: Binding site:175-175

UniProt: Binding site:258-260

UniProt: Binding site:92-92

UniProt: Binding site:96-96

UniProt: Site:175-175 Important for dimerization

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.987

Likely same site as FPocket 20 1.7 Å 45 shared residues 96% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.093

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Surrounding area

Site 3 P2Rank #3

0.033

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Surrounding area

Site 4 P2Rank #4

0.031

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Surrounding area

Site 5 P2Rank #5

0.002

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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_A0A0H3GVY6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03535	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.

53 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0PA PDB via homolog 128.2 Da · LogP 1.65 · TPSA 37.3 Open detail RCSB PDB

FIC PDB via homolog Detail RCSB PDB

CHEMBL2270643 ChEMBL via homolog · pchembl 8.52 (~3.0 nM) Detail ChEMBL

ZINC391863 ZINC proposed compound · Tanimoto 0.778 Detail ZINC

ZINC138516278 ZINC proposed compound · Tanimoto 0.730 Detail ZINC

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
0PA RCSB PDB	3DWR	P84155	128.2 Da LogP 1.65 TPSA 37.3	✓ Ro5	✓ Clean	`C1CCC(C1)CC(=O)O`
FIC RCSB PDB	3DWS	P84155	179.1 Da LogP 2.01 TPSA 53.1	✓ Ro5	✓ Clean	`c1cc2c(cc1F)cc([nH]2)C(=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
CHEMBL2270643 ChEMBL	Q42840	8.52 ~3.0 nM	357.3 Da LogP 3.91 TPSA 44.1	✓ Ro5	✓ Clean	`C#CCOc1cc(-n2nc(C(C)(C)C)sc2=O)c(Cl)cc1Cl`

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
ZINC391863 ZINC	0.778	200.2 Da LogP 1.74 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CC1CCC(CC(=O)O)CC1`
ZINC138516278 ZINC	0.730	337.3 Da LogP 3.74 TPSA 98.0	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(NC(=O)c3cc4cc(F)ccc4[nH]3)ccc2[nH…`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC12869789 ZINC	0.657	206.2 Da LogP 2.01 TPSA 36.1	✓ Ro5	✓ Clean	`CN(C)C(=O)c1cc2cc(F)ccc2[nH]1`
ZINC2582702 ZINC	0.656	205.2 Da LogP 1.56 TPSA 90.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc2[nH]c(C(=O)O)cc2c1`
ZINC402742 ZINC	0.656	240.1 Da LogP 2.63 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(Br)ccc2[nH]1`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC20028468 ZINC	0.649	232.3 Da LogP 2.54 TPSA 36.1	✓ Ro5	✓ Clean	`O=C(c1cc2cc(F)ccc2[nH]1)N1CCCC1`
ZINC5268899 ZINC	0.639	272.3 Da LogP 3.70 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(Nc1ccc(F)cc1)c1cc2cc(F)ccc2[nH]1`
ZINC2122566 ZINC	0.636	341.2 Da LogP 3.44 TPSA 57.3	✓ Ro5	✓ Clean	`C#CCOc1cc(-n2nc(C(C)(C)C)oc2=O)c(Cl)cc1Cl`
ZINC2432858 ZINC	0.636	287.1 Da LogP 2.47 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(I)ccc2[nH]1`
ZINC12888311 ZINC	0.632	260.3 Da LogP 3.32 TPSA 36.1	✓ Ro5	✓ Clean	`O=C(c1cc2cc(F)ccc2[nH]1)N1CCCCCC1`
ZINC32755156 ZINC	0.632	246.3 Da LogP 2.93 TPSA 36.1	✓ Ro5	✓ Clean	`O=C(c1cc2cc(F)ccc2[nH]1)N1CCCCC1`
ZINC11956231 ZINC	0.629	207.2 Da LogP 1.37 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(F)ccc2[nH]c1=O`
ZINC1420704 ZINC	0.629	207.2 Da LogP 1.37 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(O)c1cc(=O)c2cc(F)ccc2[nH]1`
ZINC2384078 ZINC	0.629	229.2 Da LogP 2.88 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(C(F)(F)F)ccc2[nH]1`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC398906 ZINC	0.619	200.2 Da LogP 1.74 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C[C@H]1CCCC[C@@H]1CC(=O)O`
ZINC13007430 ZINC	0.605	234.3 Da LogP 2.79 TPSA 36.1	✓ Ro5	✓ Clean	`CCN(CC)C(=O)c1cc2cc(F)ccc2[nH]1`
ZINC18736 ZINC	0.605	207.2 Da LogP 2.48 TPSA 42.1	✓ Ro5	✓ Clean	`CCOC(=O)c1cc2cc(F)ccc2[nH]1`
ZINC20028329 ZINC	0.605	220.2 Da LogP 2.45 TPSA 44.9	✓ Ro5	✓ Clean	`CC(C)NC(=O)c1cc2cc(F)ccc2[nH]1`
ZINC14985707 ZINC	0.600	203.2 Da LogP 2.07 TPSA 70.2	✓ Ro5	✓ Clean	`CC(=O)c1ccc2[nH]c(C(=O)O)cc2c1`
ZINC20028330 ZINC	0.600	261.3 Da LogP 1.69 TPSA 39.3	✓ Ro5	✓ Clean	`CN1CCN(C(=O)c2cc3cc(F)ccc3[nH]2)CC1`
ZINC2582700 ZINC	0.600	217.3 Da LogP 3.16 TPSA 53.1	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc2[nH]c(C(=O)O)cc2c1`
ZINC32003100 ZINC	0.600	237.3 Da LogP 3.53 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(-c3ccccc3)ccc2[nH]1`
ZINC40497239 ZINC	0.600	268.3 Da LogP 3.58 TPSA 36.1	✓ Ro5	✓ Clean	`CN(C(=O)c1cc2cc(F)ccc2[nH]1)c1ccccc1`
ZINC82862565 ZINC	0.600	210.2 Da LogP 2.83 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CC1CCC(C(F)(F)F)CC1`
ZINC5346714 ZINC	0.595	282.3 Da LogP 3.58 TPSA 36.1	✓ Ro5	✓ Clean	`CN(Cc1ccccc1)C(=O)c1cc2cc(F)ccc2[nH]1`
ZINC19685918 ZINC	0.593	225.3 Da LogP 2.51 TPSA 40.5	✓ Ro5	✓ Clean	`O=C(O)CC1CCN(C2CCCCC2)CC1`
ZINC584905838 ZINC	0.593	200.4 Da LogP 2.97 TPSA 37.3	✓ Ro5	✓ Clean	`C[Si]1(C)CCC[C@@H](CC(=O)O)CC1`
ZINC584905839 ZINC	0.593	200.4 Da LogP 2.97 TPSA 37.3	✓ Ro5	✓ Clean	`C[Si]1(C)CCC[C@H](CC(=O)O)CC1`
ZINC12946858 ZINC	0.590	218.2 Da LogP 2.20 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NC1CC1)c1cc2cc(F)ccc2[nH]1`
ZINC32779849 ZINC	0.590	222.2 Da LogP 1.94 TPSA 45.3	✓ Ro5	✓ Clean	`CON(C)C(=O)c1cc2cc(F)ccc2[nH]1`
ZINC13003350 ZINC	0.585	234.3 Da LogP 2.84 TPSA 44.9	✓ Ro5	✓ Clean	`CC[C@@H](C)NC(=O)c1cc2cc(F)ccc2[nH]1`
ZINC13003352 ZINC	0.585	234.3 Da LogP 2.84 TPSA 44.9	✓ Ro5	✓ Clean	`CC[C@H](C)NC(=O)c1cc2cc(F)ccc2[nH]1`
ZINC13957077 ZINC	0.585	344.4 Da LogP 4.83 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NC(c1ccccc1)c1ccccc1)c1cc2cc(F)ccc2[nH]1`
ZINC5267168 ZINC	0.585	268.3 Da LogP 3.24 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)c1cc2cc(F)ccc2[nH]1`
ZINC5345841 ZINC	0.585	341.4 Da LogP 3.41 TPSA 39.3	✓ Ro5	✓ Clean	`O=C(c1cc2cc(F)ccc2[nH]1)N1CCN(c2ccc(F)cc2)CC1`
ZINC95989650 ZINC	0.585	262.2 Da LogP 1.65 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(NC1(C(=O)O)CC1)c1cc2cc(F)ccc2[nH]1`
ZINC13821173 ZINC	0.583	207.2 Da LogP 1.37 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(O)c1cc(=O)c2ccc(F)cc2[nH]1`
ZINC3748658 ZINC	0.583	203.2 Da LogP 2.99 TPSA 53.1	✓ Ro5	✓ Clean	`CC(C)c1ccc2[nH]c(C(=O)O)cc2c1`
ZINC161561 ZINC	0.579	245.2 Da LogP 2.76 TPSA 62.3	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(OC(F)(F)F)ccc2[nH]1`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC12907968 ZINC	0.575	260.2 Da LogP 2.60 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NCC(F)(F)F)c1cc2cc(F)ccc2[nH]1`
ZINC12978339 ZINC	0.575	216.2 Da LogP 1.67 TPSA 44.9	✓ Ro5	✓ Clean	`C#CCNC(=O)c1cc2cc(F)ccc2[nH]1`

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.