KpKP13 Protein target profile

ATP-dependent DNA helicase recG

Accession: KP13_00162

Gene: recG AHE42082.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H4K6

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Length 693

Pocket druggability (P2Rank · AlphaFold DB model) 0.893

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 8 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 0.67. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.89. 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 (%): 37.975 Lower values reduce human off-target concern.
Human E-value: 4.92e-06
Gut microbiome similarity: 3.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 94.661 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 85.59 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.893

Structure A0A0H3H4K6

Pocket Pocket 1

Druggability (FPocket) 0.673

Structure A0A0H3H4K6

Pocket Pocket 25

ColabFold model

P2Rank 0.874 · Pocket 1

FPocket 0.881 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 185 / 4744 genomes with a hit

Prevalence 3.9%

Sequence

Primary amino-acid sequence viewer.

MSGRLLDAVPLSSLTGVGAAQSSKLAKIGLHTVQDLLLHLPLRYEDRTHLYPIAELLPGVYATVEGEVLNSNITFGGRRMMTCQISDGTGILTMRFFNFNAAMKNSLATGRRVLAYGEAKRGKYGAEMIHPEYRVQGDMSTPELQETLTPVYPTTEGIKQATLRKLTDQALELLETCAISELLPPELAQGMMSLPEALRTLHRPPPSLQLSELESGKHPAQQRLILEELLAHNLSMLALRAGAQRYHALPLGANDTLKNQLLASLPFKPTGAQARVTAEIEHDMALDVPMMRLVQGDVGSGKTLVAALAALRAIVHGKQVALMAPTELLAEQHANNFRSWFEPLGIEVGWLAGKQKGKARQAQQEAIASGEVQMIVGTHAIFQEQVQFNGLALVIIDEQHRFGVHQRLALWEKGQQQGFHPHQLIMTATPIPRTLAMTAYADLDTSIIDELPPGRTPVTTVAIPDTRRSDIIDRVRNACTHEGRQAYWVCTLIEESDLLEAQAAEATWEELKLALPELNIGLVHGRMKPAEKQAVMQAFKQGEMHLLVATTVIEVGVDVPNSSLMIIENPERLGLAQLHQLRGRVGRGAVASHCVLLYKSPLSKTAQKRLQVLRDSNDGFVIAQKDLEIRGPGELLGTRQTGNAEFKVADLLRDQAMIPDVQRIARHIHERYPLQAQALIERWMPETERYSNA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

5.6.2.4

Gene Ontology (GO)

GO:0003676 Binding to a nucleic acid.
GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
GO:0006310 Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0043138 Unwinding a DNA helix in the direction 5' to 3', 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:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
457	615	CDD	cd18811	SF2_C_RecG
208	450	FunFam	G3DSA:3.40.50.300:FF:000715	ATP-dependent DNA helicase RecG
617	672	Pfam	PF19833	ATP-dependent DNA helicase RecG, domain 3, C-terminal
617	672	InterPro	IPR045562	ATP-dependent DNA helicase RecG, domain 3, C-terminal
265	459	SMART	SM00487	ultradead3
265	459	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
482	628	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
482	628	InterPro	IPR001650	Helicase, C-terminal
480	588	Pfam	PF00271	Helicase conserved C-terminal domain
480	588	InterPro	IPR001650	Helicase, C-terminal
209	453	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
209	453	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
63	135	CDD	cd04488	RecG_wedge_OBF
15	171	Pfam	PF17191	RecG wedge domain
15	171	InterPro	IPR033454	RecG, wedge domain
292	653	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
292	653	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
224	452	CDD	cd17992	DEXHc_RecG
5	684	PANTHER	PTHR47964	ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC
5	684	InterPro	IPR047112	ATP-dependent DNA helicase RecG/Transcription-repair-coupling factor
505	589	SMART	SM00490	helicmild6
505	589	InterPro	IPR001650	Helicase, C-terminal
47	140	FunFam	G3DSA:2.40.50.140:FF:000134	ATP-dependent DNA helicase RecG
9	175	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
9	175	InterPro	IPR012340	Nucleic acid-binding, OB-fold
28	664	NCBIfam	TIGR00643	ATP-dependent DNA helicase RecG
28	664	InterPro	IPR004609	ATP-dependent DNA helicase RecG
457	630	FunFam	G3DSA:3.40.50.300:FF:000391	ATP-dependent DNA helicase RecG
208	450	Gene3D	G3DSA:3.40.50.300	-
208	450	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
47	140	Gene3D	G3DSA:2.40.50.140	-
47	140	InterPro	IPR012340	Nucleic acid-binding, OB-fold
293	433	Pfam	PF00270	DEAD/DEAH box helicase
293	433	InterPro	IPR011545	DEAD/DEAH box helicase domain
283	448	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
283	448	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
457	630	Gene3D	G3DSA:3.40.50.300	-
457	630	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.893

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Surrounding area

Pocket 2 P2Rank #2

0.838

Likely same site as FPocket 49 5.7 Å 15 shared residues 62% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.377

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Surrounding area

Pocket 4 P2Rank #4

0.089

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Surrounding area

Pocket 5 P2Rank #5

0.079

Likely same site as FPocket 6 2.2 Å 10 shared residues 83% of smaller site

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #25

0.673 Unusual size

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Surrounding area

Pocket 2 FPocket #6

0.455

Likely same site as P2Rank 5 2.2 Å 10 shared residues 83% of smaller site

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Surrounding area

Pocket 3 FPocket #49

0.391 Unusual size

Likely same site as P2Rank 2 5.7 Å 15 shared residues 62% of smaller site

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Surrounding area

Pocket 4 FPocket #37

0.375

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.874

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Surrounding area

Pocket 2 P2Rank #2

0.485

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Surrounding area

Pocket 3 P2Rank #3

0.424

Likely same site as FPocket 4 0.7 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.223

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Surrounding area

Pocket 5 P2Rank #5

0.082

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #4

0.881 Unusual size

Likely same site as P2Rank 3 0.7 Å 15 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #9

0.212

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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_A0A0H3H4K6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00162	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.

57 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 5 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AGS PDB via homolog 523.2 Da · LogP -1.51 · TPSA 262.1 Open detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

CHEMBL1471192 ChEMBL via homolog · pchembl 7.25 (~56.2 nM) Detail ChEMBL

CHEMBL1560762 ChEMBL via homolog · pchembl 6.85 (~141.3 nM) Detail ChEMBL

CHEMBL1446521 ChEMBL via homolog · pchembl 6.50 (~316.2 nM) 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
AGS RCSB PDB	6QV4	G0S0B9	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	6L5N	Q9NR30	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)…`

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
CHEMBL1471192 ChEMBL	P46063	7.25 ~56.2 nM	451.6 Da LogP 1.73 TPSA 104.8	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)NCC(=O)N(CC(=O)NC2CCCCC2)CC2CCC…`
CHEMBL1560762 ChEMBL	P46063	6.85 ~141.3 nM	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NCC1CCCO1`
CHEMBL1446521 ChEMBL	P46063	6.50 ~316.2 nM	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NCC3CCCO3)n2C)cc1`
CHEMBL1448630 ChEMBL	P46063	6.05 ~891.3 nM	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NCC2CCCO2)cc1`
CHEMBL1057 ChEMBL	P46063	—	332.3 Da LogP 3.67 TPSA 76.0	✓ Ro5	✓ Clean	`O=C1OC2(c3ccc(O)cc3Oc3cc(O)ccc32)c2ccccc21`

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
ZINC316109 ZINC	1.000	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NC[C@H]2CCCO2)cc1`
ZINC316110 ZINC	1.000	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NC[C@@H]2CCCO2)cc1`
ZINC3286414 ZINC	1.000	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)cc1`
ZINC3286415 ZINC	1.000	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)cc1`
ZINC3860453 ZINC	1.000	332.3 Da LogP 3.67 TPSA 76.0	✓ Ro5	✓ Clean	`O=C1OC2(c3ccc(O)cc3Oc3cc(O)ccc32)c2ccccc21`
ZINC798668 ZINC	1.000	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@H]1CCCO1`
ZINC798669 ZINC	1.000	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@@H]1CCC…`
ZINC804908 ZINC	0.979	382.5 Da LogP 1.58 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCC2)cc1)NC[C@H]1CCCO1`
ZINC804909 ZINC	0.979	382.5 Da LogP 1.58 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCC2)cc1)NC[C@@H]1CCCO1`
ZINC3485814 ZINC	0.870	366.9 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(Cl)cc1`
ZINC3485816 ZINC	0.870	366.9 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(Cl)cc1`
ZINC6914139 ZINC	0.870	350.4 Da LogP 2.01 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(F)cc1`
ZINC6914143 ZINC	0.870	350.4 Da LogP 2.01 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(F)cc1`
ZINC3402375 ZINC	0.855	388.5 Da LogP 3.17 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(C(C)(C)C)c…`
ZINC3402380 ZINC	0.855	388.5 Da LogP 3.17 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(C(C)(C)C)…`
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…`
ZINC43199396 ZINC	0.842	331.3 Da LogP 3.54 TPSA 81.8	✓ Ro5	✓ Clean	`Nc1ccc2c(c1)Oc1cc(O)ccc1[C@]21OC(=O)c2ccccc21`
ZINC43199397 ZINC	0.842	331.3 Da LogP 3.54 TPSA 81.8	✓ Ro5	✓ Clean	`Nc1ccc2c(c1)Oc1cc(O)ccc1[C@@]21OC(=O)c2ccccc21`
ZINC880963 ZINC	0.839	362.5 Da LogP 1.88 TPSA 78.3	✓ Ro5	✓ Clean	`COc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)cc1`
ZINC880965 ZINC	0.839	362.5 Da LogP 1.88 TPSA 78.3	✓ Ro5	✓ Clean	`COc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)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)(…`
ZINC2207000 ZINC	0.810	403.5 Da LogP 2.22 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(=O)Nc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)c…`
ZINC2207001 ZINC	0.810	403.5 Da LogP 2.22 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(=O)Nc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)…`
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)…`
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(=…`
ZINC3286424 ZINC	0.786	422.6 Da LogP 3.94 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2-c2ccc(C)c…`
ZINC3286426 ZINC	0.786	422.6 Da LogP 3.94 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2-c2ccc(C)…`
ZINC15020070 ZINC	0.780	346.3 Da LogP 3.97 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc2c(c1)Oc1cc(O)ccc1[C@@]21OC(=O)c2ccccc21`
ZINC15020073 ZINC	0.780	346.3 Da LogP 3.97 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc2c(c1)Oc1cc(O)ccc1[C@]21OC(=O)c2ccccc21`
ZINC9193273 ZINC	0.780	386.5 Da LogP 2.75 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc2c(c1)CCCC2`
ZINC9193274 ZINC	0.780	386.5 Da LogP 2.75 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc2c(c1)CCCC2`
ZINC335097 ZINC	0.778	235.3 Da LogP 1.60 TPSA 47.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC[C@H]2CCCO2)cc1`
ZINC335098 ZINC	0.778	235.3 Da LogP 1.60 TPSA 47.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC[C@@H]2CCCO2)cc1`
ZINC301598 ZINC	0.766	278.4 Da LogP 1.78 TPSA 50.4	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)NC(=S)NC[C@H]2CCCO2)cc1`
ZINC301599 ZINC	0.766	278.4 Da LogP 1.78 TPSA 50.4	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)NC(=S)NC[C@@H]2CCCO2)cc1`
ZINC14183634 ZINC	0.763	333.4 Da LogP 1.26 TPSA 81.9	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1cccnc1`
ZINC14183635 ZINC	0.763	333.4 Da LogP 1.26 TPSA 81.9	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1cccnc1`
ZINC5861269 ZINC	0.754	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccccc1-c1nnc(SCC(=O)NC[C@@H]2CCCO2)n1C`
ZINC5861281 ZINC	0.754	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccccc1-c1nnc(SCC(=O)NC[C@H]2CCCO2)n1C`
ZINC358808 ZINC	0.750	320.5 Da LogP 2.77 TPSA 50.4	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C(=O)NC(=S)NC[C@H]2CCCO2)cc1`
ZINC358809 ZINC	0.750	320.5 Da LogP 2.77 TPSA 50.4	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C(=O)NC(=S)NC[C@@H]2CCCO2)cc1`
ZINC798731 ZINC	0.745	356.4 Da LogP 1.05 TPSA 93.7	✓ Ro5	✓ Clean	`CC(C)NS(=O)(=O)c1ccc(OCC(=O)NC[C@@H]2CCCO2)cc1`
ZINC810031 ZINC	0.745	394.5 Da LogP 2.53 TPSA 84.5	✓ Ro5	✓ Clean	`O=C(CCc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@@H]1CCC…`

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.

Cross-references

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

Sequence

UniProt A0A0H3H4K6

Chemistry

ChEMBL CHEMBL1471192 ChEMBL CHEMBL1560762 ChEMBL CHEMBL1446521 ChEMBL CHEMBL1448630 ChEMBL CHEMBL1057