KpATCC43816 Protein target profile

ATP-dependent RNA helicase, specific for 23S rRNA

Accession: VK055_1062

Gene: AIK79685.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GSK5

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Length 457

Pocket druggability (P2Rank · AlphaFold DB model) 0.67

Direct ligand evidence 0 56 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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.67. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 6 structural and 0 bioactivity records.

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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 (%): 50.538 Lower values reduce human off-target concern.
Human E-value: 6.67e-20
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 43.62 Higher values support similarity to known essential genes.
DEG E-value: 1.16e-80 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 93.6 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) 0.67

Structure A0A0H3GSK5

Pocket Pocket 1

Druggability (FPocket) 0.797

Structure A0A0H3GSK5

Pocket Pocket 2

ColabFold model

P2Rank 0.801 · Pocket 1

FPocket 0.422 · Pocket 37

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 142 / 4744 genomes with a hit

Prevalence 3.0%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTAFSTLTVLPAAQLANLNELGYLSMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQHIDPARFETQSLVLCPTRELADQVAGELRRLARCLPNIKILMLCGGQPFGAQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALQTLVMDEADRMLDMGFSDAIDEVIRFAPADRQTLLFSATWPAAIAAISGRVQRNPQTIEIDTVDALPAIEQQFFEVSRHGKIALLQRLLSQHQPASCVVFCNTKRDCQAVCDALNAAGQSALSLHGDLEQRDRDQTLVRFANGSVRVLVATDVAARGLDIKSLALVVNFELAWDPEVHVHRIGRTARAGEQGLAISFCAPEEAQRATILADMLQLSLNWLPAPTGNTIAPLTAEMATLCIDGGKKAKMRPGDVLGALTGDMGFDGADIGKITVHPAHVYVAIRQNMAQKAYKQLQNGKIKGKSCRVRLLK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.6.4.13

Gene Ontology (GO)

GO:0000027 The aggregation, arrangement and bonding together of constituent RNAs and proteins to form the large ribosomal subunit.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0003676 Binding to a nucleic acid.
GO:0003724 Unwinding of an RNA helix, driven by ATP hydrolysis.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0034458 Unwinding of an RNA helix in the 3' to 5' direction, 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:0003723 Binding to an RNA molecule or a portion thereof.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

37 records

Show feature table

Start	End	DB	Term	Name
255	336	SMART	SM00490	helicmild6
255	336	InterPro	IPR001650	Helicase, C-terminal
216	345	CDD	cd18787	SF2_C_DEAD
15	206	CDD	cd00268	DEADc
1	208	Gene3D	G3DSA:3.40.50.300	-
1	208	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
32	457	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
3	13	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
384	454	Pfam	PF03880	DbpA RNA binding domain
384	454	InterPro	IPR005580	DEAD box helicase DbpA/CsdA, RNA-binding domain
231	375	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
231	375	InterPro	IPR001650	Helicase, C-terminal
27	190	Pfam	PF00270	DEAD/DEAH box helicase
27	190	InterPro	IPR011545	DEAD/DEAH box helicase domain
5	457	Hamap	MF_00965	ATP-dependent RNA helicase DbpA [dbpA].
5	457	InterPro	IPR028619	ATP-dependent RNA helicase DbpA
3	358	PANTHER	PTHR47959	ATP-DEPENDENT RNA HELICASE RHLE-RELATED
228	336	Pfam	PF00271	Helicase conserved C-terminal domain
228	336	InterPro	IPR001650	Helicase, C-terminal
151	159	ProSitePatterns	PS00039	DEAD-box subfamily ATP-dependent helicases signature.
151	159	InterPro	IPR000629	ATP-dependent RNA helicase DEAD-box, conserved site
34	205	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
34	205	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
72	350	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
72	350	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
384	456	FunFam	G3DSA:3.30.70.330:FF:000254	ATP-dependent RNA helicase DbpA
384	456	CDD	cd12501	RRM_EcDbpA_like
14	31	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
212	379	FunFam	G3DSA:3.40.50.300:FF:001245	ATP-dependent RNA helicase DbpA
1	31	Phobius	SIGNAL_PEPTIDE	Signal peptide region
384	456	Gene3D	G3DSA:3.30.70.330	-
384	456	InterPro	IPR012677	Nucleotide-binding alpha-beta plait domain superfamily
212	365	Gene3D	G3DSA:3.40.50.300	-
212	365	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
22	219	SMART	SM00487	ultradead3
22	219	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain

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

0.67

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Surrounding area

Pocket 2 P2Rank #2

0.351

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Surrounding area

Pocket 3 P2Rank #3

0.328

Likely same site as FPocket 2 2.3 Å 17 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.099

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Surrounding area

Pocket 5 P2Rank #5

0.038

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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 #2

0.797 Unusual size

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

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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

0.801

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Surrounding area

Pocket 2 P2Rank #2

0.643

Likely same site as FPocket 37 5.7 Å 18 shared residues 78% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.046

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Surrounding area

Pocket 4 P2Rank #4

0.01

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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_A0A0H3GSK5	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1062	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

8OD PDB via homolog 443.2 Da · LogP -2.45 · TPSA 252.6 Open detail RCSB PDB

8OP PDB via homolog Detail RCSB PDB

8OX PDB via homolog Detail RCSB PDB

AF3 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
8OD RCSB PDB	3NBF	Q72GF3	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`c1nc(c2c(n1)N(C(=O)N2)[C@H]3[C@@H]([C@@H]([C@H]…`
8OP RCSB PDB	3MWK	Q72GF3	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`c1nc(c2c(n1)N(C(=O)N2)[C@H]3[C@@H]([C@@H]([C@H]…`
8OX RCSB PDB	3MWL	Q72GF3	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)N(C(=O)N2)[C@H]3[C@@H]([C@@H]([C@H]…`
AF3 RCSB PDB	3EX7	P38919	84.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al](F)F`
ANP RCSB PDB	4D25	O01378	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)…`
LMR RCSB PDB	5GVR	Q9UJV9	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)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).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC17376093 ZINC	1.000	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=O)n2[C@@H]1O[C@H](CO)[C@@H](O)…`
ZINC5163021 ZINC	1.000	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=O)n2[C@@H]1O[C@H](CO)[C@@H](O)…`
ZINC80023117 ZINC	1.000	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=O)n2[C@@H]1O[C@H](CO)[C@H](O)[…`
ZINC80023118 ZINC	1.000	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=O)n2[C@@H]1O[C@H](CO)[C@H](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)(…`
ZINC104199549 ZINC	0.771	265.2 Da LogP -1.64 TPSA 131.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=O)n2[C@H]1O[C@@H](CO)[C@@H]2O[…`
ZINC104199552 ZINC	0.771	265.2 Da LogP -1.64 TPSA 131.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=O)n2[C@@H]1O[C@@H](CO)[C@@H]2O…`
ZINC1566227 ZINC	0.771	265.2 Da LogP -1.64 TPSA 131.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=O)n2[C@H]1O[C@@H](CO)[C@@H]2O[…`
ZINC5389846 ZINC	0.771	265.2 Da LogP -1.64 TPSA 131.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=O)n2[C@@H]1O[C@@H](CO)[C@@H]2O…`
ZINC17376092 ZINC	0.755	299.3 Da LogP -1.32 TPSA 142.4	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=S)n2[C@@H]1O[C@H](CO)[C@@H](O)…`
ZINC33837666 ZINC	0.755	299.3 Da LogP -1.32 TPSA 142.4	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=S)n2[C@@H]1O[C@H](CO)[C@H](O)[…`
ZINC4823533 ZINC	0.755	299.3 Da LogP -1.32 TPSA 142.4	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=S)n2[C@H]1O[C@@H](CO)[C@@H](O)…`
ZINC4823535 ZINC	0.755	299.3 Da LogP -1.32 TPSA 142.4	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=S)n2[C@H]1O[C@@H](CO)[C@@H](O)…`
ZINC4823537 ZINC	0.755	299.3 Da LogP -1.32 TPSA 142.4	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=S)n2[C@@H]1O[C@@H](CO)[C@@H](O…`
ZINC5395342 ZINC	0.755	299.3 Da LogP -1.32 TPSA 142.4	✓ Ro5	✓ Clean	`Nc1ncnc2c1[nH]c(=S)n2[C@@H]1O[C@H](CO)[C@H](O)[…`
ZINC71773889 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891 ZINC	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC12360002 ZINC	0.651	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	0.651	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	0.651	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	0.651	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	0.651	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	0.651	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	0.651	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	0.651	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	0.651	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	0.651	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC5390312 ZINC	0.643	350.3 Da LogP -2.85 TPSA 192.4	1 viol.	✓ Clean	`Nc1ncnc2c1c1c(=O)[nH]c(=O)[nH]c1n2[C@H]1O[C@@H]…`
ZINC5390313 ZINC	0.643	350.3 Da LogP -2.85 TPSA 192.4	1 viol.	✓ Clean	`Nc1ncnc2c1c1c(=O)[nH]c(=O)[nH]c1n2[C@@H]1O[C@@H…`
ZINC5390314 ZINC	0.643	350.3 Da LogP -2.85 TPSA 192.4	1 viol.	✓ Clean	`Nc1ncnc2c1c1c(=O)[nH]c(=O)[nH]c1n2[C@H]1O[C@@H]…`
ZINC5390315 ZINC	0.643	350.3 Da LogP -2.85 TPSA 192.4	1 viol.	✓ Clean	`Nc1ncnc2c1c1c(=O)[nH]c(=O)[nH]c1n2[C@@H]1O[C@@H…`
ZINC12378687 ZINC	0.635	299.2 Da LogP -3.39 TPSA 179.5	1 viol.	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2O[C@H](CO)[C@H](O)[C@…`
ZINC8830749 ZINC	0.635	299.2 Da LogP -3.39 TPSA 179.5	1 viol.	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2O[C@H](CO)[C@H](O)[C@…`
ZINC8830750 ZINC	0.635	299.2 Da LogP -3.39 TPSA 179.5	1 viol.	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2O[C@@H](CO)[C@H](O)[C…`
ZINC8830751 ZINC	0.635	299.2 Da LogP -3.39 TPSA 179.5	1 viol.	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2O[C@H](CO)[C@@H](O)[C…`
ZINC8830752 ZINC	0.635	299.2 Da LogP -3.39 TPSA 179.5	1 viol.	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2O[C@@H](CO)[C@@H](O)[…`
ZINC8952459 ZINC	0.635	299.2 Da LogP -3.39 TPSA 179.5	1 viol.	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2O[C@H](CO)[C@@H](O)[C…`
ZINC5082171 ZINC	0.618	297.3 Da LogP -2.85 TPSA 149.4	✓ Ro5	✓ Clean	`Cn1cnc2c([nH]c(=O)n2[C@H]2O[C@@H](CO)[C@@H](O)[…`
ZINC5082172 ZINC	0.618	297.3 Da LogP -2.85 TPSA 149.4	✓ Ro5	✓ Clean	`Cn1cnc2c([nH]c(=O)n2[C@@H]2O[C@@H](CO)[C@@H](O)…`
ZINC17064639 ZINC	0.614	349.3 Da LogP -2.56 TPSA 198.4	2 viol.	✓ Clean	`Nc1nc(=O)c2c3c(N)ncnc3n([C@@H]3O[C@@H](CO)[C@@H…`
ZINC17064641 ZINC	0.614	349.3 Da LogP -2.56 TPSA 198.4	2 viol.	✓ Clean	`Nc1nc(=O)c2c3c(N)ncnc3n([C@H]3O[C@@H](CO)[C@@H]…`
ZINC5385128 ZINC	0.614	349.3 Da LogP -2.56 TPSA 198.4	2 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)c1c(N)ncnc1n2[C@H]1O[C@@H](C…`
ZINC5385129 ZINC	0.614	349.3 Da LogP -2.56 TPSA 198.4	2 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)c1c(N)ncnc1n2[C@@H]1O[C@@H](…`
ZINC4830734 ZINC	0.611	297.3 Da LogP -2.68 TPSA 148.7	✓ Ro5	✓ Clean	`Cn1c(=O)n([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c2n…`
ZINC4830735 ZINC	0.611	297.3 Da LogP -2.68 TPSA 148.7	✓ Ro5	✓ Clean	`Cn1c(=O)n([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c2…`
ZINC4830736 ZINC	0.611	297.3 Da LogP -2.68 TPSA 148.7	✓ Ro5	✓ Clean	`Cn1c(=O)n([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c2…`
ZINC4830737 ZINC	0.611	297.3 Da LogP -2.68 TPSA 148.7	✓ Ro5	✓ Clean	`Cn1c(=O)n([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c…`
ZINC4823726 ZINC	0.596	282.3 Da LogP -2.40 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1nc(N)n2[C@H]1O[C@@H](CO)[C@@H](O)[C@H…`
ZINC4823727 ZINC	0.596	282.3 Da LogP -2.40 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1nc(N)n2[C@@H]1O[C@@H](CO)[C@@H](O)[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.

Cross-references

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

Sequence

UniProt A0A0H3GSK5