Protein target profile

KP13_04195

Lipid A export ATP-binding/permease protein msbA

Genome: KpKP13 Gene: AHE45426.1 msbA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GV05

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Length 582

Pocket druggability 0.97

Direct ligand evidence 0 59 total records

Functional annotation 0 EC 9 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

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. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 6 structural and 3 bioactivity records.

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 (%): 61.039 Lower values reduce human off-target concern.
Human E-value: 2.5399999999999998e-24
Gut microbiome similarity: 3.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 92.955 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 89.38 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 0.97

Structure A0A0H3GV05

Pocket Pocket 1

P2Rank 0.372

Structure A0A0H3GV05

Pocket Pocket 1

ColabFold model

FPocket 0.727 · Pocket 9

P2Rank 0.432 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 145 / 4744 genomes with a hit

Prevalence 3.1%

Cross-references

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

Sequence

UniProt A0A0H3GV05

Chemistry

ChEMBL CHEMBL490985 ChEMBL A ChEMBL CHEMBL1551724

Sequence

Primary amino-acid sequence viewer.

MQNDKDLSTWQTFRRLWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEGTRVIERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLHKMQFGE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Gene Ontology (GO)

GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0034040 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + lipid(in) = ADP + phosphate + lipid(out).
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
GO:0140359 Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane.
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:0015421 Catalysis of the reaction: ATP + H2O + oligopeptide(out) = ADP + phosphate + oligopeptide(in).
GO:0042802 Binding to an identical protein or proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

46 records

Show feature table

Start	End	DB	Term	Name
13	35	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
481	495	ProSitePatterns	PS00211	ABC transporters family signature.
481	495	InterPro	IPR017871	ABC transporter-like, conserved site
12	582	NCBIfam	TIGR02203	lipid A export permease/ATP-binding protein MsbA
12	582	InterPro	IPR011917	ABC transporter, lipid A-core flippase, MsbA
333	582	FunFam	G3DSA:3.40.50.300:FF:000140	Lipid A export ATP-binding/permease protein MsbA
27	316	CDD	cd18552	ABC_6TM_MsbA_like
142	163	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
332	582	Gene3D	G3DSA:3.40.50.300	-
332	582	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
245	267	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	330	FunFam	G3DSA:1.20.1560.10:FF:000008	Lipid A export ATP-binding/permease protein MsbA
1	330	Gene3D	G3DSA:1.20.1560.10	ABC transporter type 1, transmembrane domain
1	330	InterPro	IPR036640	ABC transporter type 1, transmembrane domain superfamily
144	163	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
71	93	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
94	141	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
342	578	ProSiteProfiles	PS50893	ATP-binding cassette, ABC transporter-type domain profile.
342	578	InterPro	IPR003439	ABC transporter-like, ATP-binding domain
164	168	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
342	576	CDD	cd03251	ABCC_MsbA
368	555	SMART	SM00382	AAA_5
368	555	InterPro	IPR003593	AAA+ ATPase domain
14	325	SUPERFAMILY	SSF90123	ABC transporter transmembrane region
14	325	InterPro	IPR036640	ABC transporter type 1, transmembrane domain superfamily
273	277	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
359	509	Pfam	PF00005	ABC transporter
359	509	InterPro	IPR003439	ABC transporter-like, ATP-binding domain
331	580	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
331	580	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
296	582	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
187	253	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
27	297	Pfam	PF00664	ABC transporter transmembrane region
27	297	InterPro	IPR011527	ABC transporter type 1, transmembrane domain
65	93	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
278	295	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	20	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
21	45	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
28	310	ProSiteProfiles	PS50929	ABC transporter integral membrane type-1 fused domain profile.
28	310	InterPro	IPR011527	ABC transporter type 1, transmembrane domain
5	579	PANTHER	PTHR43394	ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL
5	579	InterPro	IPR039421	Type 1 protein exporter
169	186	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
254	272	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
167	186	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
46	64	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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

0.97

Likely same site as P2Rank 1 2.2 Å 13 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #27

0.371

Likely same site as P2Rank 1 8.0 Å 2 shared residues 20% of smaller site

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Surrounding area

Site 3 FPocket #8

0.317

Likely same site as P2Rank 3 1.6 Å 8 shared residues 89% of smaller site

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Surrounding area

Site 4 FPocket #7

0.213

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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

0.372

Likely same site as FPocket 1 2.2 Å 13 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.285

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Surrounding area

Site 3 P2Rank #3

0.243

Likely same site as FPocket 8 1.6 Å 8 shared residues 89% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.094

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Surrounding area

Site 5 P2Rank #5

0.042

Likely same site as FPocket 1 6.5 Å 2 shared residues 40% 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 #9

0.727

Likely same site as P2Rank 1 1.9 Å 13 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #38

0.452

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Surrounding area

Site 3 FPocket #35

0.301

Likely same site as P2Rank 4 7.7 Å 2 shared residues 33% 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

0.432

Likely same site as FPocket 9 1.9 Å 13 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.275

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Surrounding area

Site 3 P2Rank #3

0.157

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Surrounding area

Site 4 P2Rank #4

0.046

Likely same site as FPocket 35 7.7 Å 2 shared residues 33% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.043

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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_A0A0H3GV05	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04195	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.

59 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 3 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0JZ PDB via homolog 687.4 Da · LogP 1.74 · TPSA 126.0 Open detail RCSB PDB

2J8 PDB via homolog Detail RCSB PDB

4C8 PDB via homolog Detail RCSB PDB

AGS PDB via homolog Detail RCSB PDB

ANP 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
0JZ RCSB PDB	3G60	P21447	687.4 Da LogP 1.74 TPSA 126.0	1 viol.	✓ Clean	`CC(C)[C@@H]1c2nc(c[se]2)C(=O)N[C@@H](c3nc(c[se]…`
2J8 RCSB PDB	3G61	P21447	687.4 Da LogP 1.74 TPSA 126.0	1 viol.	✓ Clean	`CC(C)[C@H]1c2nc(c[se]2)C(=O)N[C@H](c3nc(c[se]3)…`
4C8 RCSB PDB	4XWK	P21447	564.7 Da LogP 7.29 TPSA 9.2	2 viol.	✓ Clean	`c1cc(c(cc1Br)Br)Oc2c(cc(cc2Br)Br)Br`
AGS RCSB PDB	6QUZ	Q9WYC4	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP RCSB PDB	3B60	P63359	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
Z5G RCSB PDB	7MET	A0A0B9X4I2	335.8 Da LogP 4.23 TPSA 66.4	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)Nc2c(c3c(s2)CCCC3)C(=O)O)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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL490985 ChEMBL	P08183	6.77 ~169.8 nM	453.4 Da LogP -0.46 TPSA 179.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COC(=O)c2ccc(S(=O)(…`
A ChEMBL	P08183	—	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CHEMBL1551724 ChEMBL	P08183	—	258.2 Da LogP -2.82 TPSA 156.9	✓ Ro5	✓ Clean	`NC(=O)c1ncn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c…`

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
ZINC2922863 ZINC	1.000	335.8 Da LogP 4.23 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCC2)c1ccc(Cl)cc1`
ZINC20334905 ZINC	0.974	349.8 Da LogP 4.62 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCCC2)c1ccc(Cl)cc1`
ZINC4899186 ZINC	0.947	321.8 Da LogP 3.84 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCC2)c1ccc(Cl)cc1`
ZINC12360002 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC78111 ZINC	0.800	301.4 Da LogP 3.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCC2)c1ccccc1`
ZINC127403 ZINC	0.786	319.4 Da LogP 3.72 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCC2)c1ccc(F)cc1`
ZINC188404 ZINC	0.786	315.4 Da LogP 3.89 TPSA 66.4	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)Nc2sc3c(c2C(=O)O)CCCC3)cc1`
ZINC2591233 ZINC	0.786	334.8 Da LogP 3.63 TPSA 72.2	✓ Ro5	✓ Clean	`NC(=O)c1c(NC(=O)c2ccc(Cl)cc2)sc2c1CCCC2`
ZINC8387400 ZINC	0.786	427.3 Da LogP 4.18 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCC2)c1ccc(I)cc1`
ZINC210056 ZINC	0.780	315.4 Da LogP 3.97 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCCC2)c1ccccc1`
ZINC1218717 ZINC	0.767	362.9 Da LogP 4.41 TPSA 72.2	✓ Ro5	✓ Clean	`NC(=O)c1c(NC(=O)c2ccc(Cl)cc2)sc2c1CCCCCC2`
ZINC2158336 ZINC	0.767	357.5 Da LogP 4.87 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C(=O)Nc2sc3c(c2C(=O)O)CCCC3)cc1`
ZINC35587 ZINC	0.767	348.9 Da LogP 4.02 TPSA 72.2	✓ Ro5	✓ Clean	`NC(=O)c1c(NC(=O)c2ccc(Cl)cc2)sc2c1CCCCC2`
ZINC4348733 ZINC	0.767	348.9 Da LogP 3.89 TPSA 58.2	✓ Ro5	✓ Clean	`CNC(=O)c1c(NC(=O)c2ccc(Cl)cc2)sc2c1CCCC2`
ZINC125918 ZINC	0.756	287.3 Da LogP 3.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCC2)c1ccccc1`
ZINC124138 ZINC	0.750	349.8 Da LogP 4.32 TPSA 55.4	✓ Ro5	✓ Clean	`COC(=O)c1c(NC(=O)c2ccc(Cl)cc2)sc2c1CCCC2`
ZINC146439 ZINC	0.744	320.8 Da LogP 3.24 TPSA 72.2	✓ Ro5	✓ Clean	`NC(=O)c1c(NC(=O)c2ccc(Cl)cc2)sc2c1CCC2`
ZINC2157576 ZINC	0.744	366.2 Da LogP 3.95 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCC2)c1ccc(Br)cc1`
ZINC349870 ZINC	0.744	305.3 Da LogP 3.33 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCC2)c1ccc(F)cc1`
ZINC8387402 ZINC	0.744	413.2 Da LogP 3.79 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCC2)c1ccc(I)cc1`
ZINC13518964 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC888095786 ZINC	0.739	350.8 Da LogP 3.39 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCNC2)c1ccc(Cl)cc1`
ZINC1200205 ZINC	0.733	363.9 Da LogP 4.71 TPSA 55.4	✓ Ro5	✓ Clean	`COC(=O)c1c(NC(=O)c2ccc(Cl)cc2)sc2c1CCCCC2`
ZINC227470 ZINC	0.733	335.8 Da LogP 4.23 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCC2)c1cccc(Cl)c1`
ZINC3148790 ZINC	0.733	331.4 Da LogP 3.59 TPSA 75.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)Nc2sc3c(c2C(=O)O)CCCC3)cc1`
ZINC315655645 ZINC	0.733	336.8 Da LogP 3.63 TPSA 79.3	✓ Ro5	✓ Clean	`O=C(Nc1sc2c(c1C(=O)O)CCCC2)c1ccc(Cl)cn1`
ZINC4096224 ZINC	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC2483604 ZINC	0.727	343.4 Da LogP 4.48 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C(=O)Nc2sc3c(c2C(=O)O)CCC3)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.