Protein target profile

KP13_03382

Methylthioribose-1-phosphate isomerase

Genome: KpKP13 Gene: mtnA AHE45761.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GPS7

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Length 342

Pocket druggability 0.86

Direct ligand evidence 0 55 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: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.86, P2Rank 0.85). 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 0.86. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.85. 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 (%): 41.16 Lower values reduce human off-target concern.
Human E-value: 8.36e-71
Gut microbiome similarity: 1.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 48.308 Higher values support similarity to known essential genes.
DEG E-value: 4.32e-83 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.02 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 0.86

Structure A0A0H3GPS7

Pocket Pocket 1

P2Rank 0.851

Structure A0A0H3GPS7

Pocket Pocket 1

ColabFold model

FPocket 0.495 · Pocket 7

P2Rank 0.851 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 76 / 4744 genomes with a hit

Prevalence 1.6%

Cross-references

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

Sequence

UniProt A0A0H3GPS7

Sequence

Primary amino-acid sequence viewer.

MQTLQTTSLRVSENQLFILDQQALPQEKRWLAADNVALLVDHIHTLRVRGAPLIGLSASLLLALLAQRGLNRDALQQALETLRAARPTAVNLMNNLDRMKQALAREDYPQALEAEALRLVEEDKQLCDRIAEAGSALVKPGSRLLTHCNTGGLATAGVGTALGVIALAHRQGKVTNVWVDETRPLLQGGRLTAWELGELGVPYQLIADSMAASLMAQGQVDAVWVGADRIAANGDVANKIGTYSLAVLAHYHQIPFYVAAPQTTLDRHCPNGAAIPIEQRAAAEVTGVAGSFGAVQWAPTGAAVYNPAFDVTPAGLISGWVLDSGVVTPAQVAAGAFAPDNG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

5.3.1.23

Gene Ontology (GO)

GO:0044249 OBSOLETE. The chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.
GO:0046523 Catalysis of the reaction: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate.
GO:0019509 OBSOLETE. The generation of L-methionine (2-amino-4-(methylthio)butanoic acid) from methylthioadenosine.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
6	337	PANTHER	PTHR43475	METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE
8	328	NCBIfam	TIGR00512	S-methyl-5-thioribose-1-phosphate isomerase
8	328	InterPro	IPR005251	Methylthioribose-1-phosphate isomerase
6	336	Hamap	MF_01678	Putative methylthioribose-1-phosphate isomerase [mtnA].
6	336	InterPro	IPR005251	Methylthioribose-1-phosphate isomerase
1	174	Gene3D	G3DSA:1.20.120.420	-
1	174	InterPro	IPR027363	Methylthioribose-1-phosphate isomerase, N-terminal
175	335	Gene3D	G3DSA:3.40.50.10470	-
175	335	InterPro	IPR042529	Initiation factor 2B-like, C-terminal
140	336	FunFam	G3DSA:3.40.50.10470:FF:000006	Methylthioribose-1-phosphate isomerase
8	332	SUPERFAMILY	SSF100950	NagB/RpiA/CoA transferase-like
8	332	InterPro	IPR037171	NagB/RpiA transferase-like
39	329	NCBIfam	TIGR00524	S-methyl-5-thioribose-1-phosphate isomerase
39	329	InterPro	IPR011559	Initiation factor 2B alpha/beta/delta
48	329	Pfam	PF01008	Initiation factor 2 subunit family
48	329	InterPro	IPR000649	Initiation factor 2B-related

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 #1

0.86

Likely same site as P2Rank 1 0.5 Å 21 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #11

0.431

Likely same site as P2Rank 2 3.5 Å 8 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #8

0.401

Likely same site as P2Rank 2 7.3 Å 3 shared residues 38% 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

0.851

Likely same site as FPocket 1 0.5 Å 21 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.031

Likely same site as FPocket 11 3.5 Å 8 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.011

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Surrounding area

Residue sets

UniProt: Active site:228-228 Proton donor

UniProt: Binding site:187-187

UniProt: Binding site:238-239

UniProt: Binding site:49-51

UniProt: Binding site:86-86

UniProt: Site:148-148 Transition state stabilizer

Binding pockets · FPocket

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

Site 1 FPocket #7

0.495

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #12

0.316

Unusual size

Show in viewer

Surrounding area

Site 3 FPocket #1

0.219

Likely same site as P2Rank 1 2.1 Å 22 shared residues 100% of smaller site

Show in viewer

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_A0A0H3GPS7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03382	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.

55 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

C7B PDB via homolog 451.4 Da · LogP 3.99 · TPSA 76.7 Open detail RCSB PDB

M6P PDB via homolog Detail RCSB PDB

MRU PDB via homolog Detail RCSB PDB

RI2 PDB via homolog Detail RCSB PDB

RUB 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
C7B RCSB PDB	6CAJ	P49770	451.4 Da LogP 3.99 TPSA 76.7	✓ Ro5	✓ Clean	`c1cc(ccc1OCC(=O)NC2CCC(CC2)NC(=O)COc3ccc(cc3)Cl…`
M6P RCSB PDB	7KMA	Q14232	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@@H]([C@H](O1)O)O)O)O)O…`
MRU RCSB PDB	2YVK	O31662	260.2 Da LogP -1.25 TPSA 124.3	✓ Ro5	✓ Clean	`CSC[C@H]([C@H](C(=O)COP(=O)(O)O)O)O`
RI2 RCSB PDB	5YFS	O57947	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@H](O1)OP(=O)(O)O)O)O)OP…`
RUB RCSB PDB	5YFJ	O57947	310.1 Da LogP -2.50 TPSA 191.0	1 viol.	✓ Clean	`C([C@H]([C@H](C(=O)COP(=O)(O)O)O)O)OP(=O)(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).

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
ZINC100081898 ZINC	1.000	451.4 Da LogP 3.99 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)N[C@H]1CC[C@H](NC(=O)COc2ccc…`
ZINC100351935 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@…`
ZINC1529564 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@…`
ZINC1532533 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC1532857 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC245239931 ZINC	1.000	451.4 Da LogP 3.99 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)N[C@H]1CC[C@H](NC(=O)COc2ccc…`
ZINC3581460 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC38276879 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC38276880 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H…`
ZINC3869397 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C…`
ZINC3870277 ZINC	1.000	310.1 Da LogP -2.50 TPSA 191.0	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3875374 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC3875375 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@…`
ZINC4095545 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC4095546 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H…`
ZINC4096188 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@…`
ZINC4702158 ZINC	1.000	225.7 Da LogP 2.00 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CC1`
ZINC671772 ZINC	1.000	451.4 Da LogP 3.99 TPSA 76.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CCC(NC(=O)COc2ccc(Cl)cc2)…`
ZINC8551507 ZINC	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC12504154 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H]1O`
ZINC1532546 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H]1O`
ZINC4096190 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H]1O`
ZINC4228241 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H]1O`
ZINC4521831 ZINC	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H]1O`
ZINC146558 ZINC	0.909	253.7 Da LogP 2.78 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CCCC1`
ZINC3387598 ZINC	0.886	329.8 Da LogP 3.23 TPSA 55.4	✓ Ro5	✓ Clean	`O=C(COc1ccc(C(=O)c2ccc(Cl)cc2)cc1)NC1CC1`
ZINC1016959 ZINC	0.882	281.8 Da LogP 3.56 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CCCCCC1`
ZINC443437 ZINC	0.882	295.8 Da LogP 3.95 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CCCCCCC1`
ZINC68802 ZINC	0.882	267.8 Da LogP 3.17 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CCCCC1`
ZINC51172603 ZINC	0.861	281.8 Da LogP 3.41 TPSA 38.3	✓ Ro5	✓ Clean	`CC1CCC(NC(=O)COc2ccc(Cl)cc2)CC1`
ZINC7035958 ZINC	0.838	357.8 Da LogP 4.01 TPSA 55.4	✓ Ro5	✓ Clean	`O=C(COc1ccc(C(=O)c2ccc(Cl)cc2)cc1)NC1CCCC1`
ZINC3402618 ZINC	0.811	283.7 Da LogP 1.54 TPSA 64.6	✓ Ro5	✓ Clean	`O=C(COC(=O)COc1ccc(Cl)cc1)NC1CC1`
ZINC36880012 ZINC	0.811	281.7 Da LogP 2.35 TPSA 55.4	✓ Ro5	✓ Clean	`O=C1CCC(NC(=O)COc2ccc(Cl)cc2)CC1`
ZINC12502210 ZINC	0.793	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@@H](O)COP(=O…`
ZINC12502212 ZINC	0.793	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC12502214 ZINC	0.793	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@@H](O)COP(=…`
ZINC12502216 ZINC	0.793	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@H](O)COP(=O…`
ZINC4523251 ZINC	0.793	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@@H](O)COP(…`
ZINC4523255 ZINC	0.793	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@H](O)COP(=…`
ZINC4523257 ZINC	0.793	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@@H](O)COP(=…`
ZINC4523259 ZINC	0.793	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@H](O)COP(=O…`
ZINC253405977 ZINC	0.789	317.8 Da LogP 1.41 TPSA 72.5	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CCS(=O)(=O)CC1`
ZINC12376161 ZINC	0.775	343.9 Da LogP 4.56 TPSA 38.3	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CCC(c2ccccc2)CC1`
ZINC16605351 ZINC	0.769	282.8 Da LogP 1.93 TPSA 41.6	✓ Ro5	✓ Clean	`CN1CCC(NC(=O)COc2ccc(Cl)cc2)CC1`
ZINC14162823 ZINC	0.750	308.8 Da LogP 2.46 TPSA 41.6	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)NC1CCN(C2CC2)CC1`
ZINC14187435 ZINC	0.750	310.8 Da LogP 1.85 TPSA 58.6	✓ Ro5	✓ Clean	`CC(=O)N1CCC(NC(=O)COc2ccc(Cl)cc2)CC1`
ZINC3219531 ZINC	0.744	311.8 Da LogP 2.32 TPSA 64.6	✓ Ro5	✓ Clean	`O=C(COC(=O)COc1ccc(Cl)cc1)NC1CCCC1`
ZINC13516910 ZINC	0.733	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC2562340 ZINC	0.733	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC13715791 ZINC	0.732	358.8 Da LogP 3.18 TPSA 67.4	✓ Ro5	✓ Clean	`O=C(COc1ccc(Cl)cc1)Nc1ccc(CC(=O)NC2CC2)cc1`

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.