Protein target profile

PA2516

toluate 1,2-dioxygenase electron transfer subunit

Genome: NC_002516.2

Gene: PA2516 xylZ 3D evidence: AlphaFold DB model UniProt Q9I0W6

Export view

Length 337

Pocket druggability 0.732

Ligand records 57

EC / GO 0 / 3

Target summary

Promising target candidate with multiple supporting evidence streams.

5 signals

Strengths

Risks / watch

No major risk signal surfaced in the loaded evidence.

Missing evidence

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

How to read 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 TPW 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.

Overview

Basic information about this protein and its source genome.

Accession: PA2516
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2516 xylZ
Status: annotated
Amino acids: 337
3D evidence: AlphaFold DB model

GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

Selected pocket 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 0.732

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MNHRIALNFEDGVTRFIHAAPGETVADAAYRQGINIPLDCRDGACGTCKCLAEAGRYALGQDYIDDALSAEEAARGYVLTCQMRAESDCVLRVPASSTLCRTGQARYEARISEVRQLSPSTIGLSLRGEALASLAFLPGQYVNLQVPGSEQRRAYSFSSLAKDGEVSFLIRNVPGGLMSGFLSGTARAGDSLAMDGPLGSFYLREIHRPLLMLAGGTGLAPFTAMLERIAEQGSAHPLHLVYGVTHDVDLVGLERLEAFAERIPGFTWSACVASADSDYPRKGYVTEHIAAQHLHEGDVDIYLCGPPPMVEAVERYLREQGVRPANFYYEKFAASAA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
10	85	Pfam	PF00111	2Fe-2S iron-sulfur cluster binding domain
10	85	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
1	100	Gene3D	G3DSA:3.10.20.30	-
1	100	InterPro	IPR012675	Beta-grasp domain superfamily
204	333	SUPERFAMILY	SSF52343	Ferredoxin reductase-like, C-terminal NADP-linked domain
204	333	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
104	204	ProSiteProfiles	PS51384	Ferredoxin reductase-type FAD binding domain profile.
104	204	InterPro	IPR017927	FAD-binding domain, ferredoxin reductase-type
40	48	ProSitePatterns	PS00197	2Fe-2S ferredoxin-type iron-sulfur binding region signature.
40	48	InterPro	IPR006058	2Fe-2S ferredoxin, iron-sulphur binding site
3	335	NCBIfam	NF040810	benzoate 1,2-dioxygenase electron transfer component BenC
196	205	PRINTS	PR00410	Phenol hydroxylase reductase family signature
211	230	PRINTS	PR00410	Phenol hydroxylase reductase family signature
136	148	PRINTS	PR00410	Phenol hydroxylase reductase family signature
153	160	PRINTS	PR00410	Phenol hydroxylase reductase family signature
236	245	PRINTS	PR00410	Phenol hydroxylase reductase family signature
300	308	PRINTS	PR00410	Phenol hydroxylase reductase family signature
106	333	CDD	cd06209	BenDO_FAD_NAD
106	333	InterPro	IPR047683	Benzoate 1,2-dioxygenase reductase, FAD/NAD binding domain
3	97	ProSiteProfiles	PS51085	2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
3	97	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
101	199	Gene3D	G3DSA:2.40.30.10	Translation factors
153	160	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
153	160	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
236	245	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
236	245	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
211	230	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
211	230	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
300	308	PRINTS	PR00371	Flavoprotein pyridine nucleotide cytochrome reductase signature
300	308	InterPro	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase
17	92	CDD	cd00207	fer2
17	92	InterPro	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain
109	202	Pfam	PF00970	Oxidoreductase FAD-binding domain
109	202	InterPro	IPR008333	Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
1	98	SUPERFAMILY	SSF54292	2Fe-2S ferredoxin-like
1	98	InterPro	IPR036010	2Fe-2S ferredoxin-like superfamily
76	204	SUPERFAMILY	SSF63380	Riboflavin synthase domain-like
76	204	InterPro	IPR017938	Riboflavin synthase-like beta-barrel
200	332	Gene3D	G3DSA:3.40.50.80	-
200	332	InterPro	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
212	314	Pfam	PF00175	Oxidoreductase NAD-binding domain
212	314	InterPro	IPR001433	Oxidoreductase FAD/NAD(P)-binding
17	91	PANTHER	PTHR47354	NADH OXIDOREDUCTASE HCR

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.

Loading 3D structure...

Legend High Medium Low

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 PA2516	AlphaFold DB	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.732

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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 57 via homologs

Structural ligands 7 0 loaded crystals

Bioactive compounds 0 50 ZINC proposed compounds

Drug-like & clean 48 5 PAINS alerts

Best available ligand signal

BTB PDB via homolog 209.2 Da · LogP -3.01 · TPSA 104.4 Open detail RCSB PDB

Detail RCSB PDB BTB PDB via homolog

Detail RCSB PDB DGG PDB via homolog

Detail RCSB PDB ECN PDB via homolog

Detail RCSB PDB FDA PDB via homolog

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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
BTB RCSB PDB	4WQM	Q03304	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
DGG RCSB PDB	1CQX	P39662	735.0 Da LogP 9.75 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@…`
ECN RCSB PDB	3OZV	P39662	381.7 Da LogP 5.80 TPSA 27.1	1 viol.	✓ Clean	`c1cc(ccc1COC(Cn2ccnc2)c3ccc(cc3Cl)Cl)Cl`
FDA RCSB PDB	1TVC	P22868	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
FES RCSB PDB	5OGX	A0A076MZ01	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
KKK RCSB PDB	3OZW	P39662	531.4 Da LogP 4.21 TPSA 69.1	1 viol.	Alert	`CC(=O)N1CCN(CC1)c2ccc(cc2)OC[C@H]3CO[C@](O3)(Cn…`
X89 RCSB PDB	3OZU	P39662	416.1 Da LogP 6.45 TPSA 27.1	1 viol.	✓ Clean	`c1cc(c(cc1Cl)Cl)CO[C@@H](Cn2ccnc2)c3ccc(cc3Cl)Cl`

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
ZINC1615342 ZINC	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC102191119 ZINC	0.824	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551 ZINC	0.824	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC28568236 ZINC	0.795	489.4 Da LogP 3.95 TPSA 60.8	✓ Ro5	Alert	`Clc1ccc([C@@]2(Cn3ccnc3)OC[C@H](COc3ccc(N4CCNCC…`
ZINC31416683 ZINC	0.795	489.4 Da LogP 3.95 TPSA 60.8	✓ Ro5	Alert	`Clc1ccc([C@]2(Cn3ccnc3)OC[C@@H](COc3ccc(N4CCNCC…`
ZINC38944078 ZINC	0.795	489.4 Da LogP 3.95 TPSA 60.8	✓ Ro5	Alert	`Clc1ccc([C@]2(Cn3ccnc3)OC[C@H](COc3ccc(N4CCNCC4…`
ZINC38944080 ZINC	0.795	489.4 Da LogP 3.95 TPSA 60.8	✓ Ro5	Alert	`Clc1ccc([C@@]2(Cn3ccnc3)OC[C@@H](COc3ccc(N4CCNC…`
ZINC1532199 ZINC	0.729	297.2 Da LogP 4.13 TPSA 27.1	✓ Ro5	✓ Clean	`C=CCO[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC1532200 ZINC	0.729	297.2 Da LogP 4.13 TPSA 27.1	✓ Ro5	✓ Clean	`C=CCO[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC95918118 ZINC	0.673	312.8 Da LogP 4.49 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccc(CO[C@H](Cn2ccnc2)c2ccccc2)cc1`
ZINC95918119 ZINC	0.673	312.8 Da LogP 4.49 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccc(CO[C@@H](Cn2ccnc2)c2ccccc2)cc1`
ZINC102191158 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC14880760 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OC[C…`
ZINC53683910 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[…`
ZINC62592202 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC62592203 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC62592204 ZINC	0.660	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`
ZINC96094841 ZINC	0.660	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC849188212 ZINC	0.654	327.2 Da LogP 4.13 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)C(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188213 ZINC	0.654	327.2 Da LogP 4.13 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)C(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC38334168 ZINC	0.649	407.3 Da LogP 2.43 TPSA 79.7	✓ Ro5	✓ Clean	`CS(=O)(=O)OC[C@@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc…`
ZINC198375289 ZINC	0.635	299.2 Da LogP 3.49 TPSA 44.1	✓ Ro5	✓ Clean	`CC(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC198375301 ZINC	0.635	299.2 Da LogP 3.49 TPSA 44.1	✓ Ro5	✓ Clean	`CC(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC5349880 ZINC	0.628	433.3 Da LogP 4.32 TPSA 62.6	✓ Ro5	✓ Clean	`O=C(OC[C@@H]1CO[C@@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O…`
ZINC5349883 ZINC	0.628	433.3 Da LogP 4.32 TPSA 62.6	✓ Ro5	✓ Clean	`O=C(OC[C@H]1CO[C@@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1…`
ZINC638711 ZINC	0.628	433.3 Da LogP 4.32 TPSA 62.6	✓ Ro5	✓ Clean	`O=C(OC[C@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1)…`
ZINC638717 ZINC	0.628	433.3 Da LogP 4.32 TPSA 62.6	✓ Ro5	✓ Clean	`O=C(OC[C@@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1…`
ZINC297645 ZINC	0.620	329.2 Da LogP 2.45 TPSA 56.5	✓ Ro5	✓ Clean	`OC[C@@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC297649 ZINC	0.620	329.2 Da LogP 2.45 TPSA 56.5	✓ Ro5	✓ Clean	`OC[C@@H]1CO[C@@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC297652 ZINC	0.620	329.2 Da LogP 2.45 TPSA 56.5	✓ Ro5	✓ Clean	`OC[C@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC297656 ZINC	0.620	329.2 Da LogP 2.45 TPSA 56.5	✓ Ro5	✓ Clean	`OC[C@H]1CO[C@@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC102190506 ZINC	0.614	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	0.614	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC4217243 ZINC	0.605	367.2 Da LogP 3.11 TPSA 45.5	✓ Ro5	✓ Clean	`C#CCOC[C@H]1CO[C@](Cn2ccnc2)(c2ccc(Cl)cc2Cl)O1`
ZINC390893 ZINC	0.604	257.1 Da LogP 2.92 TPSA 38.0	✓ Ro5	✓ Clean	`O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC390894 ZINC	0.604	257.1 Da LogP 2.92 TPSA 38.0	✓ Ro5	✓ Clean	`O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC21988957 ZINC	0.600	483.4 Da LogP 4.17 TPSA 79.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@H]2CO[C@](Cn3ccnc3)(c3ccc(…`
ZINC22057057 ZINC	0.600	483.4 Da LogP 4.17 TPSA 79.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@@H]2CO[C@@](Cn3ccnc3)(c3cc…`
ZINC22057060 ZINC	0.600	483.4 Da LogP 4.17 TPSA 79.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@@H]2CO[C@](Cn3ccnc3)(c3ccc…`
ZINC6088320 ZINC	0.600	483.4 Da LogP 4.17 TPSA 79.7	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@H]2CO[C@@](Cn3ccnc3)(c3ccc…`
ZINC849187659 ZINC	0.600	325.2 Da LogP 3.88 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl)C1CC1`
ZINC849187660 ZINC	0.600	325.2 Da LogP 3.88 TPSA 44.1	✓ Ro5	✓ Clean	`O=C(O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl)C1CC1`
ZINC27416437 ZINC	0.596	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.596	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC36178999 ZINC	0.593	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	0.593	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC849188227 ZINC	0.589	341.2 Da LogP 4.52 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)CC(=O)O[C@@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188228 ZINC	0.589	341.2 Da LogP 4.52 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)CC(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`
ZINC849188301 ZINC	0.589	355.3 Da LogP 4.91 TPSA 44.1	✓ Ro5	✓ Clean	`CCC(CC)C(=O)O[C@H](Cn1ccnc1)c1ccc(Cl)cc1Cl`

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.