Protein target profile

KP13_32254

glycerol uptake facilitator protein

Genome: KpKP13 Gene: AHE42596.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GVU6

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Length 267

Pocket druggability 0.969

Direct ligand evidence 0 63 total records

Functional annotation 0 EC 5 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 0.97, P2Rank 0.56). 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 0.97. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.56. 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 (%): 44.131 Lower values reduce human off-target concern.
Human E-value: 2.07e-45
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 96.01 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 0.969

Structure A0A0H3GVU6

Pocket Pocket 1

P2Rank 0.563

Structure A0A0H3GVU6

Pocket Pocket 1

ColabFold model

FPocket 0.929 · Pocket 1

P2Rank 0.687 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 144 / 4744 genomes with a hit

Prevalence 3.0%

Cross-references

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

Sequence

UniProt A0A0H3GVU6

Chemistry

ChEMBL AZM ChEMBL CHEMBL121 ChEMBL CHEMBL128 ChEMBL CHEMBL16 ChEMBL CHEMBL536151 ChEMBL CHEMBL687 ChEMBL CHEMBL741 ChEMBL EZL ChEMBL FOK ChEMBL TOR ChEMBL ZON

Sequence

Primary amino-acid sequence viewer.

MNQTSTLTGQCVAEFLGTGLLIFFGAGCVAALRVAGASFGQWEISIIWGLGVAMAIYLTAGVSGAHLNPAVTIALWLFACFERRKVLPFIVAQTAGAFCAAALVYGLYRQLFLDLEQSQHIVRGTAASLNLAGVFSTYPHPHITFIQAFAVETTITAILMAMIMALTDDGNGIPRGPLAPLLIGLLIAVIGASMGPLTGFALNPARDFGPKLFTSLAGWGSIAFTGGLAIPYFLVPLLAPVVGAIIGAFLYRKLIGRHLPCECGIDE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0015267 Enables the energy-independent facilitated diffusion of a solute through a transmembrane aqueous pore or channel. Stereospecificity is not exhibited but this transport may be specific for a particular molecular species or class of molecules.
GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0015254 Enables the energy-independent facilitated diffusion of glycerol through a transmembrane aqueous pore or channel.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

44 records

Show feature table

Start	End	DB	Term	Name
203	221	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
178	200	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
10	254	CDD	cd00333	MIP
10	254	InterPro	IPR000425	Major intrinsic protein
80	85	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
13	251	NCBIfam	TIGR00861	MIP family channel protein
13	251	InterPro	IPR000425	Major intrinsic protein
1	259	Gene3D	G3DSA:1.20.1080.10	Glycerol uptake facilitator protein.
1	259	InterPro	IPR023271	Aquaporin-like
229	251	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
222	251	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
178	202	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
167	177	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
66	74	ProSitePatterns	PS00221	MIP family signature.
66	74	InterPro	IPR022357	Major intrinsic protein, conserved site
143	165	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
12	34	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
44	66	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
46	79	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
12	34	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
9	28	PRINTS	PR00783	Major intrinsic protein family signature
9	28	InterPro	IPR000425	Major intrinsic protein
234	254	PRINTS	PR00783	Major intrinsic protein family signature
234	254	InterPro	IPR000425	Major intrinsic protein
151	169	PRINTS	PR00783	Major intrinsic protein family signature
151	169	InterPro	IPR000425	Major intrinsic protein
48	72	PRINTS	PR00783	Major intrinsic protein family signature
48	72	InterPro	IPR000425	Major intrinsic protein
184	206	PRINTS	PR00783	Major intrinsic protein family signature
184	206	InterPro	IPR000425	Major intrinsic protein
85	104	PRINTS	PR00783	Major intrinsic protein family signature
85	104	InterPro	IPR000425	Major intrinsic protein
1	11	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
35	45	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
86	108	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
252	267	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
3	251	Pfam	PF00230	Major intrinsic protein
3	251	InterPro	IPR000425	Major intrinsic protein
145	166	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
86	108	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
109	144	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
8	257	SUPERFAMILY	SSF81338	Aquaporin-like
8	257	InterPro	IPR023271	Aquaporin-like
7	260	PANTHER	PTHR43829	AQUAPORIN OR AQUAGLYCEROPORIN 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

0.969

Likely same site as P2Rank 3 2.3 Å 17 shared residues 100% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #2

0.664

Likely same site as P2Rank 4 5.9 Å 7 shared residues 78% of smaller site

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Surrounding area

Site 3 FPocket #5

0.228

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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

0.563

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Surrounding area

Site 2 P2Rank #2

0.391

Likely same site as FPocket 1 6.5 Å 13 shared residues 93% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.39

Likely same site as FPocket 1 2.3 Å 17 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.021

Likely same site as FPocket 2 5.9 Å 7 shared residues 78% of smaller site

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #1

0.929

Likely same site as P2Rank 1 2.1 Å 22 shared residues 92% of smaller site

Unusual size

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Surrounding area

Site 2 FPocket #9

0.798

Likely same site as P2Rank 4 5.8 Å 9 shared residues 90% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #4

0.38

Likely same site as P2Rank 5 2.5 Å 9 shared residues 100% 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

0.687

Likely same site as FPocket 1 2.1 Å 22 shared residues 92% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.532

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Surrounding area

Site 3 P2Rank #3

0.094

Likely same site as FPocket 1 7.6 Å 9 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.035

Likely same site as FPocket 9 5.8 Å 9 shared residues 90% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.028

Likely same site as FPocket 4 2.5 Å 9 shared residues 100% 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_A0A0H3GVU6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_32254	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.

63 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 13 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 11 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3PE PDB via homolog 748.1 Da · LogP 12.06 · TPSA 134.4 Open detail RCSB PDB

PS6 PDB via homolog Detail RCSB PDB

AZM ChEMBL via homolog Detail ChEMBL

CHEMBL121 ChEMBL via homolog Detail ChEMBL

CHEMBL128 ChEMBL via homolog 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
3PE RCSB PDB	3M9I	Q6J8I9	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
PS6 RCSB PDB	3D9S	P55064	567.7 Da LogP 5.27 TPSA 171.7	2 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OC[C@H…`

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
AZM ChEMBL	P55088	—	222.3 Da LogP -0.86 TPSA 115.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(s1)S(=O)(=O)N`
CHEMBL121 ChEMBL	P41181	—	357.4 Da LogP 2.49 TPSA 71.5	✓ Ro5	✓ Clean	`CN(CCOc1ccc(CC2SC(=O)NC2=O)cc1)c1ccccn1`
CHEMBL128 ChEMBL	P55088	—	295.4 Da LogP 1.32 TPSA 65.2	✓ Ro5	✓ Clean	`CNS(=O)(=O)Cc1ccc2[nH]cc(CCN(C)C)c2c1`
CHEMBL16 ChEMBL	P55088	—	252.3 Da LogP 1.77 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)C(c2ccccc2)(c2ccccc2)N1`
CHEMBL536151 ChEMBL	P55087	—	383.7 Da LogP 5.34 TPSA 49.3	1 viol.	✓ Clean	`O=C(Nc1cc(C(F)(F)F)cc(C(F)(F)F)c1)c1cc(Cl)ccc1O`
CHEMBL687 ChEMBL	P55088	—	214.2 Da LogP 0.29 TPSA 89.3	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(S(N)(=O)=O)cc1`
CHEMBL741 ChEMBL	P55088	—	256.1 Da LogP 2.01 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1nnc(-c2cccc(Cl)c2Cl)c(N)n1`
EZL ChEMBL	P55088	—	258.3 Da LogP 1.34 TPSA 82.3	✓ Ro5	✓ Clean	`CCOc1ccc2c(c1)sc(n2)S(=O)(=O)N`
FOK ChEMBL	P41181	—	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1[C@H]([C@H]2C(CC[C@@H]([C@@]2([C@@…`
TOR ChEMBL	P55088	—	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(O[C@@H]2CO[C@@]3([C@H]([C@@H]2O1)OC(O3)(C)C…`
ZON ChEMBL	P55087	—	212.2 Da LogP 0.62 TPSA 86.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(no2)CS(=O)(=O)N`

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
ZINC102190506 ZINC	1.000	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	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC13156 ZINC	1.000	256.1 Da LogP 2.01 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1nnc(-c2cccc(Cl)c2Cl)c(N)n1`
ZINC134036 ZINC	1.000	214.2 Da LogP 0.29 TPSA 89.3	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(S(N)(=O)=O)cc1`
ZINC13612334 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2CO[C@]3(COS(N)(=O)=O)OC(C)(C)O[C@@…`
ZINC13783471 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@H](OC(C)…`
ZINC13783493 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2CO[C@]3(COS(N)(=O)=O)OC(C)(C)O[C@…`
ZINC14360 ZINC	1.000	295.4 Da LogP 1.32 TPSA 65.2	✓ Ro5	✓ Clean	`CNS(=O)(=O)Cc1ccc2[nH]cc(CCN(C)C)c2c1`
ZINC144827766 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@@](C)(O1)[C@@H](O…`
ZINC1543366 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2CO[C@@]3(COS(N)(=O)=O)OC(C)(C)O[C@…`
ZINC23586802 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2CO[C@@]3(COS(N)(=O)=O)OC(C)(C)O[C@…`
ZINC248102933 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@@]2(O)[C@]3(C)[C@@H](O)CCC(…`
ZINC248102936 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@@]2(O)[C@]3(C)[C@H](O)CCC(C…`
ZINC2510358 ZINC	1.000	252.3 Da LogP 1.77 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)C(c2ccccc2)(c2ccccc2)N1`
ZINC36385190 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@H](OC(C)…`
ZINC3813042 ZINC	1.000	222.3 Da LogP -0.86 TPSA 115.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC3831557 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2CO[C@@]3(COS(N)(=O)=O)OC(C)(C)O[C…`
ZINC3831559 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2CO[C@]3(COS(N)(=O)=O)OC(C)(C)O[C@…`
ZINC3872620 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@H](OC(…`
ZINC3872621 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](OC…`
ZINC3872622 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@H](OC(…`
ZINC3872623 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](OC…`
ZINC3977779 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](OC…`
ZINC4321 ZINC	1.000	212.2 Da LogP 0.62 TPSA 86.2	✓ Ro5	✓ Clean	`NS(=O)(=O)Cc1noc2ccccc12`
ZINC43574047 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2[C@@H]3OC(C)(C)O[C@@]3(COS(N)(=O)…`
ZINC4544736 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@]2(O)[C@@](C)(O1)[C@H](OC(C…`
ZINC56721 ZINC	1.000	258.3 Da LogP 1.34 TPSA 82.3	✓ Ro5	✓ Clean	`CCOc1ccc2nc(S(N)(=O)=O)sc2c1`
ZINC56863626 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2[C@@H](CO[C@]3(COS(N)(=O)=O)OC(C)(…`
ZINC71789673 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@@H](OC(…`
ZINC71789674 ZINC	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@@H](OC(…`
ZINC95616603 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2CO[C@@]3(COS(N)(=O)=O)OC(C)(C)O[C…`
ZINC96085732 ZINC	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2[C@@H]3OC(C)(C)O[C@]3(COS(N)(=O)=…`
ZINC968328 ZINC	1.000	357.4 Da LogP 2.49 TPSA 71.5	✓ Ro5	✓ Clean	`CN(CCOc1ccc(C[C@@H]2SC(=O)NC2=O)cc1)c1ccccn1`
ZINC968330 ZINC	1.000	357.4 Da LogP 2.49 TPSA 71.5	✓ Ro5	✓ Clean	`CN(CCOc1ccc(C[C@H]2SC(=O)NC2=O)cc1)c1ccccn1`
ZINC27416437 ZINC	0.976	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	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC12970899 ZINC	0.889	290.3 Da LogP 1.96 TPSA 89.3	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(-c2ccc(S(N)(=O)=O)cc2)cc1`
ZINC2382316250 ZINC	0.887	452.5 Da LogP 2.09 TPSA 119.4	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@@H](OC(…`
ZINC27553862 ZINC	0.887	452.5 Da LogP 2.09 TPSA 119.4	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](OC…`
ZINC13111092 ZINC	0.852	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](O)…`
ZINC2069563917 ZINC	0.852	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@@H](O)[…`
ZINC71766833 ZINC	0.852	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](O)…`
ZINC6116337 ZINC	0.815	270.3 Da LogP 1.91 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@](c2ccccc2)(c2ccc(F)cc2)N1`
ZINC6116537 ZINC	0.815	270.3 Da LogP 1.91 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@](c2ccccc2)(c2ccc(F)cc2)N1`
ZINC2165131 ZINC	0.800	369.4 Da LogP 1.09 TPSA 135.4	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(S(=O)(=O)Nc2ccc(S(N)(=O)=O)cc2)cc1`
ZINC242063 ZINC	0.800	333.4 Da LogP 1.54 TPSA 118.4	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(C(=O)Nc2ccc(S(N)(=O)=O)cc2)cc1`
ZINC114897182 ZINC	0.788	495.7 Da LogP 3.50 TPSA 84.2	✓ Ro5	Alert	`CNS(=O)(=O)Cc1ccc2[nH]c(Cc3ccc4[nH]cc(CCN(C)C)c…`
ZINC22061272 ZINC	0.787	355.4 Da LogP -1.42 TPSA 135.8	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2[C@@H]3O[C@](C)(CO)O[C@@H]3CO[C@@]…`
ZINC119642 ZINC	0.786	268.3 Da LogP 1.48 TPSA 78.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@](c2ccccc2)(c2ccc(O)cc2)N1`
ZINC2048546 ZINC	0.786	286.7 Da LogP 2.42 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@](c2ccccc2)(c2ccc(Cl)cc2)N1`

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.