Protein target profile

VK055_2094

htpG

Genome: KpATCC43816 Gene: htpG AIK80699.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GSX3

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Length 624

Pocket druggability 0.501

Direct ligand evidence 0 84 total records

Functional annotation 0 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.50. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.87. Structure available AlphaFold DB model + ColabFold model 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 (%): 65.789 Lower values reduce human off-target concern.
Human E-value: 2.16e-10
Gut microbiome similarity: 4.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 93.429 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 89.25 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 0.501

Structure A0A0H3GSX3

Pocket Pocket 27

P2Rank 0.867

Structure A0A0H3GSX3

Pocket Pocket 1

ColabFold model

FPocket 0.467 · Pocket 3

P2Rank 0.888 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 227 / 4744 genomes with a hit

Prevalence 4.8%

Cross-references

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

Sequence

UniProt A0A0H3GSX3

Chemistry

ChEMBL CHEMBL424811 ChEMBL BSM ChEMBL RDC ChEMBL CHEMBL190182 ChEMBL CHEMBL366215 ChEMBL CHEMBL191074

Sequence

Primary amino-acid sequence viewer.

MKGQETRGFQSEVKQLLHLMIHSLYSNKEIFLRELISNASDAADKLRFRALSQPDLYEGDGELRVRVSFDKDNRTLTIADNGIGMNREEVIDHLGTIAKSGTKAFLESMGSDQAKDSQLIGQFGVGFYSAFIVADKVTVRTRAAGDKPENGVFWESAGEGEYTVADITKADRGTEITLHLREGEDDFLNDWRVRSIISKYSDHIALPVEIEKREEKDGETVISWEKINKAQALWTRSKSEVNDDEYKEFYKHIAHDYSDPLTWSHNRVEGKQEYTSLLYIPSQAPWDMWNRDHKHGLKLYVQRVFIMDDAEQFMPNYLRFVRGLIDSNDLPLNVSREILQDSSVTRNLRTALTKRALQMLDKLAKDDAEKYQTFWKQFGLVLKEGPAEDPSNQEAIAKLLRFATTHTDSSAQTVSLEEYVSRMKEGQEKIYYITADSYAAAKSSPHLELLRKKGIEVLLLSDRIDEWMMSYLTEFDGKAFQSVAKADESLDKLADEVDESTKEAEKALEPFVERVKNLLGDRVKEVRLTHRLTDTPAIVTTDADEMSTQMAKLFAAAGQAAPEVKYIFELNPAHQLVKRAADTQDDAQFGEWVELLLDQALLAERGTLEDPNQFIRRMNQLLAS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
GO:0140662 Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
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:0051082 Binding to an unfolded protein.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

47 records

Show feature table

Start	End	DB	Term	Name
27	184	SMART	SM00387	HKATPase_4
27	184	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
229	396	FunFam	G3DSA:3.30.230.80:FF:000002	Molecular chaperone HtpG
1	220	FunFam	G3DSA:3.30.565.10:FF:000009	Molecular chaperone HtpG
1	624	PIRSF	PIRSF002583	HSP90_HTPG
1	624	InterPro	IPR001404	Heat shock protein Hsp90 family
25	34	ProSitePatterns	PS00298	Heat shock hsp90 proteins family signature.
25	34	InterPro	IPR019805	Heat shock protein Hsp90, conserved site
510	622	SUPERFAMILY	SSF110942	HSP90 C-terminal domain
510	622	InterPro	IPR037196	HSP90, C-terminal domain
14	204	CDD	cd16927	HATPase_Hsp90-like
14	204	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
93	110	PRINTS	PR00775	90kDa heat shock protein signature
93	110	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
120	142	PRINTS	PR00775	90kDa heat shock protein signature
120	142	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
26	48	PRINTS	PR00775	90kDa heat shock protein signature
26	48	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
190	208	PRINTS	PR00775	90kDa heat shock protein signature
190	208	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
172	189	PRINTS	PR00775	90kDa heat shock protein signature
172	189	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
75	92	PRINTS	PR00775	90kDa heat shock protein signature
75	92	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
5	25	PRINTS	PR00775	90kDa heat shock protein signature
5	25	InterPro	IPR020575	Heat shock protein Hsp90, N-terminal
483	503	Coils	Coil	Coil
211	623	Pfam	PF00183	Hsp90 protein
211	623	InterPro	IPR001404	Heat shock protein Hsp90 family
491	623	Gene3D	G3DSA:1.20.120.790	-
491	623	InterPro	IPR037196	HSP90, C-terminal domain
1	215	Gene3D	G3DSA:3.30.565.10	-
1	215	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
229	396	Gene3D	G3DSA:3.30.230.80	-
4	213	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
4	213	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
5	622	PANTHER	PTHR11528	HEAT SHOCK PROTEIN 90 FAMILY MEMBER
5	622	InterPro	IPR001404	Heat shock protein Hsp90 family
27	182	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
27	182	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
397	489	FunFam	G3DSA:3.40.50.11260:FF:000002	Molecular chaperone HtpG
397	489	Gene3D	G3DSA:3.40.50.11260	-
491	624	FunFam	G3DSA:1.20.120.790:FF:000002	Molecular chaperone HtpG
230	485	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
230	485	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold
2	623	Hamap	MF_00505	Chaperone protein HtpG [htpG].
2	623	InterPro	IPR001404	Heat shock protein Hsp90 family

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 #27

0.501

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Surrounding area

Site 2 FPocket #39

0.305

Likely same site as P2Rank 1 4.4 Å 20 shared residues 87% of smaller site

Unusual size

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Surrounding area

Site 3 FPocket #60

0.253

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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

0.867

Likely same site as FPocket 39 4.4 Å 20 shared residues 87% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.697

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Surrounding area

Site 3 P2Rank #3

0.479

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Surrounding area

Site 4 P2Rank #4

0.279

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Surrounding area

Site 5 P2Rank #5

0.067

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Surrounding area

Residue sets

UniProt: Binding site:100-101

UniProt: Binding site:122-127

UniProt: Binding site:174-174

UniProt: Binding site:336-336

UniProt: Binding site:34-34

UniProt: Binding site:38-38

UniProt: Binding site:80-80

UniProt: Binding site:85-85

UniProt: Binding site:99-99

Binding pockets · FPocket

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

Site 1 FPocket #3

0.467

Unusual size

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Surrounding area

Site 2 FPocket #33

0.207

Likely same site as P2Rank 1 7.2 Å 16 shared residues 64% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.888

Likely same site as FPocket 33 7.2 Å 16 shared residues 64% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.594

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Surrounding area

Site 3 P2Rank #3

0.515

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Surrounding area

Site 4 P2Rank #4

0.037

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Surrounding area

Site 5 P2Rank #5

0.036

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Surrounding area

Residue sets

UniProt: Binding site:100-101

UniProt: Binding site:122-127

UniProt: Binding site:174-174

UniProt: Binding site:336-336

UniProt: Binding site:34-34

UniProt: Binding site:38-38

UniProt: Binding site:80-80

UniProt: Binding site:85-85

UniProt: Binding site:99-99

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_A0A0H3GSX3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2094	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.

84 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 34 records from similar proteins

Structural ligands 28 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

13C PDB via homolog 337.8 Da · LogP 3.11 · TPSA 86.6 Open detail RCSB PDB

13I PDB via homolog Detail RCSB PDB

13N PDB via homolog Detail RCSB PDB

2GJ PDB via homolog Detail RCSB PDB

4QS 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
13C RCSB PDB	2XX2	P02829	337.8 Da LogP 3.11 TPSA 86.6	✓ Ro5	✓ Clean	`c1c(c2c(c(c1O)Cl)CC(=O)CCCCC=CCCNC2=O)O`
13I RCSB PDB	2XX4	P02829	411.9 Da LogP 2.69 TPSA 116.1	✓ Ro5	✓ Clean	`CCO[C@H]([C@H]1CCC\C=C\CCNC(=O)c2c(cc(c(c2CC1=O…`
13N RCSB PDB	2XX5	P02829	471.0 Da LogP 3.66 TPSA 115.7	✓ Ro5	✓ Clean	`c1ccc(cc1)CNC(=O)[C@@H]2CCC\C=C\CCNC(=O)c3c(cc(…`
2GJ RCSB PDB	7K9S	J9VVA4	465.6 Da LogP 4.13 TPSA 108.1	✓ Ro5	✓ Clean	`CCNC(=O)c1c(c(on1)c2cc(c(cc2O)O)C(C)C)c3ccc(cc3…`
4QS RCSB PDB	4AS9	P02829	574.7 Da LogP 2.80 TPSA 163.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@@H](C=C([C@H]([C@H](/C…`
59C RCSB PDB	4ASA	P02829	599.7 Da LogP 2.93 TPSA 166.3	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@@H](C=C([C@H]([C@H](/C…`
62U RCSB PDB	4ASF	P02829	626.7 Da LogP 3.53 TPSA 176.6	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H](C(C=C([C@H]([C@H](C=CC=C(…`
7FK RCSB PDB	4CE1	P02829	379.9 Da LogP 4.24 TPSA 77.8	✓ Ro5	✓ Clean	`CN1CC/C=C/CCCCCCC(=O)Cc2c(c(cc(c2Cl)O)O)C1=O`
814 RCSB PDB	4ASG	P02829	636.7 Da LogP 3.94 TPSA 163.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@@H](C=C(C([C@H](/C=C\C…`
8TO RCSB PDB	4ASB	P02829	630.8 Da LogP 2.30 TPSA 169.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@@H](C=C([C@H]([C@H](C=…`
ACP RCSB PDB	4XC0	P54651	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
AGS RCSB PDB	6XLH	P15108	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	6XLC	P15108	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)…`
BC6 RCSB PDB	2VW5	P02829	502.7 Da LogP 4.70 TPSA 131.1	1 viol.	✓ Clean	`C[C@H]1CC\C=C(\C(=O)Nc2cc(cc(c2)O)C[C@H](C[C@@H…`
BO5 RCSB PDB	4CE2	P02829	365.9 Da LogP 3.85 TPSA 77.8	✓ Ro5	✓ Clean	`CN1CC/C=C/CCCCCC(=O)Cc2c(c(cc(c2Cl)O)O)C1=O`
D1S RCSB PDB	3Q5J	Q4Q4I6	630.8 Da LogP 2.30 TPSA 169.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@H](/C=C(/[C@@H]([C@H](…`
D1U RCSB PDB	3Q5K	Q4Q4I6	440.5 Da LogP 3.92 TPSA 90.0	✓ Ro5	✓ Clean	`CC1(Cc2c(c(nn2c3ccc(c(c3)NCCSC)C(=O)N)C(F)(F)F)…`
GDM RCSB PDB	4XDM	P54651	560.6 Da LogP 2.41 TPSA 163.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@H](\C=C(\[C@@H]([C@H](…`
H64 RCSB PDB	1ZW9	P02829	465.4 Da LogP 3.44 TPSA 100.1	✓ Ro5	✓ Clean	`CC(C)NCCCn1c2c(c(ncn2)N)nc1Sc3cc4c(cc3Br)OCO4`
KX2 RCSB PDB	3Q5L	Q4Q4I6	642.8 Da LogP 2.45 TPSA 169.5	1 viol.	Alert	`C[C@H]1C[C@@H]([C@@H]([C@H](/C=C(/[C@@H]([C@H](…`
L4V RCSB PDB	4CE3	P02829	351.8 Da LogP 3.46 TPSA 77.8	✓ Ro5	✓ Clean	`CN1CCC/C=C\CCCC(=O)Cc2c(c(cc(c2Cl)O)O)C1=O`
RDA RCSB PDB	2FXS	P02829	411.8 Da LogP 2.53 TPSA 145.6	✓ Ro5	✓ Clean	`COc1cc(c(cc1O)NC(=O)CCc2c(c(cc(c2Cl)O)O)C(=O)OC…`
RDE RCSB PDB	1ZWH	P02829	397.8 Da LogP 2.76 TPSA 120.5	✓ Ro5	✓ Clean	`COc1cc(c(c(c1OC)CCOC(=O)c2cc(c(cc2O)O)Cl)OC)N`
TAM RCSB PDB	4XKA	P54651	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`
W8S RCSB PDB	7K9W	J9VVA4	456.5 Da LogP 4.41 TPSA 99.9	✓ Ro5	✓ Clean	`Cn1c(cc(n1)c2cccc(c2)OC)Nc3cc(cc(c3C(=O)N4Cc5cc…`
W8V RCSB PDB	7K9V	J9VVA4	440.5 Da LogP 4.71 TPSA 90.6	✓ Ro5	✓ Clean	`Cc1ccccc1c2cc(n(n2)C)Nc3cc(cc(c3C(=O)N4Cc5ccccc…`
W8Y RCSB PDB	7K9U	J9VVA4	427.5 Da LogP 3.79 TPSA 103.5	✓ Ro5	✓ Clean	`Cn1c(cc(n1)c2ccccc2)Nc3cc(cc(c3C(=O)N4Cc5cccnc5…`
XD6 RCSB PDB	2XD6	P02829	366.8 Da LogP 3.11 TPSA 100.9	✓ Ro5	✓ Clean	`c1c(c2c(c(c1O)Cl)CC(=O)CCCC/C(=C/CCOC2=O)/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
CHEMBL424811 ChEMBL	P15108	6.96 ~109.6 nM	373.8 Da LogP 3.18 TPSA 107.5	✓ Ro5	✓ Clean	`CNC(=O)c1[nH]nc(-c2cc(Cl)c(O)cc2O)c1-c1ccc(OC)c…`
BSM ChEMBL	P15108	6.85 ~141.3 nM	387.8 Da LogP 3.57 TPSA 107.5	✓ Ro5	✓ Clean	`CCNC(=O)c1c(c([nH]n1)c2cc(c(cc2O)O)Cl)c3ccc(cc3…`
RDC ChEMBL	P15108	6.70 ~199.5 nM	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2[C@H](O2)\C=C/C=C/C(=O)Cc3c(c(c…`
CHEMBL190182 ChEMBL	P15108	6.41 ~389.0 nM	432.3 Da LogP 3.68 TPSA 107.5	✓ Ro5	✓ Clean	`CCNC(=O)c1[nH]nc(-c2cc(Br)c(O)cc2O)c1-c1ccc(OC)…`
CHEMBL366215 ChEMBL	P15108	6.38 ~416.9 nM	359.8 Da LogP 2.92 TPSA 121.5	✓ Ro5	✓ Clean	`COc1ccc(-c2c(-c3cc(Cl)c(O)cc3O)n[nH]c2C(N)=O)cc1`
CHEMBL191074 ChEMBL	P15108	6.19 ~645.7 nM	358.8 Da LogP 3.89 TPSA 87.6	✓ Ro5	✓ Clean	`Cc1[nH]nc(-c2cc(Cl)c(O)cc2O)c1-c1ccc2c(c1)OCCO2`

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
ZINC100006925 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C\C=C/C(=O)Cc2c(Cl)c(…`
ZINC100013319 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O…`
ZINC100013323 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@H]2O[C@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O)…`
ZINC100015656 ZINC	1.000	465.6 Da LogP 4.13 TPSA 108.1	✓ Ro5	✓ Clean	`CCNC(=O)c1noc(-c2cc(C(C)C)c(O)cc2O)c1-c1ccc(CN2…`
ZINC100152234 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C/C=C/C(=O)Cc2c(Cl)c(…`
ZINC13521629 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C\C=C\C(=O)Cc2c(Cl)c(…`
ZINC2061000778 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)cc…`
ZINC253952046 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)c…`
ZINC253987424 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2C=CC=CC(=O)Cc2c(Cl)c(O)c…`
ZINC253987427 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)cc…`
ZINC253987428 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@@H]2C=CC=CC(=O)Cc2c(Cl)c(O)…`
ZINC33838895 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2/C=C\C=C/C(=O)Cc2c(Cl)c(O…`
ZINC45789132 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(…`
ZINC45789135 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@H]2O[C@@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O…`
ZINC5492965 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@H]2/C=C\C=C\C(=O)Cc2c(Cl)c(…`
ZINC12360002 ZINC	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC4617893 ZINC	0.796	387.8 Da LogP 3.57 TPSA 107.5	✓ Ro5	✓ Clean	`CCNC(=O)c1[nH]nc(-c2cc(Cl)c(O)cc2O)c1-c1ccc(OC)…`
ZINC13518964 ZINC	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	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	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224 ZINC	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC238855217 ZINC	0.750	560.6 Da LogP 2.41 TPSA 163.5	1 viol.	Alert	`COC1=C2C[C@@H](C)C[C@H](OC)[C@H](O)[C@@H](C)/C=…`

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.