KpKP13 Protein target profile

Replicative DNA helicase

Accession: KP13_00389

Gene: dnaB AHE46873.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GQ64

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Length 471

Pocket druggability (P2Rank · AlphaFold DB model) 0.085

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 10 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

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.54. This supports review but is not experimental validation. 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: No hit
Gut microbiome similarity: 4.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.514 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 89.27 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) 0.085

Structure A0A0H3GQ64

Pocket Pocket 1

Druggability (FPocket) 0.535

Structure A0A0H3GQ64

Pocket Pocket 14

ColabFold model

P2Rank 0.269 · Pocket 1

FPocket 0.598 · Pocket 17

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 203 / 4744 genomes with a hit

Prevalence 4.3%

Sequence

Primary amino-acid sequence viewer.

MAGNKPFNKPQTETRERDPQLAGLKVPPHSIEAEQSVLGGLMLDNERWDDVAERVVADDFYTRPHRHIFTEMARLQESGSPIDLITLAESLERQGQLDSVGGFAYLAELSKNTPSAANISAYADIVRERAVVREMISVANEIAEAGFDPQGRTSEDLLDLAESRVFKIAESRANKDEGPKNIADVLDATVARIEQLFQQPHDGVTGVNTGYDDLNKKTAGLQPSDLIIVAARPSMGKTTFAMNLVENAAMLQDKPVLIFSLEMPSEQIMMRSLASLSRVDQTRIRTGQLDDEDWARISGTMGILLEKRNIYIDDSSGLTPTEVRSRARRIAREHGGIGLIMIDYLQLMRVPSLSDNRTLEIAEISRSLKALAKELQVPVVALSQLNRSLEQRADKRPVNSDLRESGSIEQDADLIMFIYRDEVYHENSDLKGIAEIIIGKQRNGPIGTVRLTFNGQWSRFDNYAGPQYDDE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

5.6.2.3

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:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:1990077 Any of a family of protein complexes that form at the origin of replication or stalled replication forks and function in replication primer synthesis in all organisms. Early complexes initiate double-stranded DNA unwinding. The core unit consists of a replicative helicase and a primase. The helicase further unwinds the DNA and recruits the polymerase machinery. The primase synthesizes RNA primers that act as templates for complementary stand replication by the polymerase machinery. The primosome contains a number of associated proteins and protein complexes and contributes to the processes of replication initiation, lagging strand elongation, and replication restart.
GO:0043139 Unwinding a DNA helix in the 5' to 3' direction, driven by ATP hydrolysis.
GO:0042802 Binding to an identical protein or proteins.
GO:0006269 The synthesis of a short nucleotide polymer using one strand of unwound DNA as a template. The product is usually a RNA molecule between 4-15 nucleotides long that provides a free 3'-OH that can be extended by DNA-directed DNA polymerases. In certain conditions, for example in response to DNA damage, some primases synthesize a DNA primer.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
21	183	Gene3D	G3DSA:1.10.860.10	DNAb Helicase; Chain A
21	183	InterPro	IPR016136	DNA helicase DnaB, N-terminal/DNA primase DnaG, C-terminal
25	136	SUPERFAMILY	SSF48024	N-terminal domain of DnaB helicase
25	136	InterPro	IPR036185	DNA helicase, DnaB-like, N-terminal domain superfamily
1	25	MobiDBLite	mobidb-lite	consensus disorder prediction
27	128	Pfam	PF00772	DnaB-like helicase N terminal domain
27	128	InterPro	IPR007693	DNA helicase, DnaB-like, N-terminal
206	462	Pfam	PF03796	DnaB-like helicase C terminal domain
206	462	InterPro	IPR007694	DNA helicase, DnaB-like, C-terminal
24	466	PANTHER	PTHR30153	REPLICATIVE DNA HELICASE DNAB
184	463	Gene3D	G3DSA:3.40.50.300	-
184	463	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
27	464	NCBIfam	TIGR00665	replicative DNA helicase
27	464	InterPro	IPR007692	DNA helicase, DnaB type
206	462	CDD	cd00984	DnaB_C
223	429	SMART	SM00382	AAA_5
223	429	InterPro	IPR003593	AAA+ ATPase domain
20	183	FunFam	G3DSA:1.10.860.10:FF:000002	Replicative DNA helicase
185	468	FunFam	G3DSA:3.40.50.300:FF:000076	Replicative DNA helicase
200	467	ProSiteProfiles	PS51199	Superfamily 4 helicase domain profile.
200	467	InterPro	IPR007694	DNA helicase, DnaB-like, C-terminal
204	456	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
204	456	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

0.085

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Surrounding area

Pocket 2 P2Rank #2

0.034

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Surrounding area

Pocket 3 P2Rank #3

0.018

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Surrounding area

Pocket 4 P2Rank #4

0.003

Likely same site as FPocket 14 7.3 Å 2 shared residues 50% 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 #14

0.535

Likely same site as P2Rank 4 7.3 Å 2 shared residues 50% 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

0.269

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Surrounding area

Pocket 2 P2Rank #2

0.018

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Surrounding area

Pocket 3 P2Rank #3

0.011

Likely same site as FPocket 17 7.4 Å 1 shared residue 25% 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 #17

0.598

Likely same site as P2Rank 3 7.4 Å 1 shared residue 25% of smaller site

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Surrounding area

Pocket 2 FPocket #2

0.433

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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_A0A0H3GQ64	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00389	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 ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

08T PDB via homolog Open detail RCSB PDB

ALF PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

DTP PDB via homolog Detail RCSB PDB

FLC 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
08T RCSB PDB	6QEM	P0ACB0	—	—	—	`[Be](OP(=O)(O)OP(=O)(O)OC[C@@H]1[C@H]([C@H]([C@…`
ALF RCSB PDB	4ESV	Q9X4C9	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
ANP RCSB PDB	1E0J	P03692	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)…`
DTP RCSB PDB	1CR2	P03692	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO[P@]…`
FLC RCSB PDB	4A1F	O25916	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
TTP RCSB PDB	1CR1	P03692	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@]…`
TYD RCSB PDB	1CR4	P03692	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@]…`

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
ZINC13434879 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC13434881 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](=O)(…`
ZINC13434883 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@@](=O…`
ZINC13434884 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@](=O)…`
ZINC13507072 ZINC	1.000	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC33979251 ZINC	1.000	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC8215662 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)…`
ZINC8664605 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO[P@@](=O…`
ZINC12495199 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO[P@@](=O…`
ZINC13434873 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC13434875 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](=O)(…`
ZINC13434876 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@](=O)…`
ZINC13434878 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@](=O)…`
ZINC8215728 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)…`
ZINC12503053 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC33979243 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC33979244 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O)…`
ZINC33979245 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=…`
ZINC33979246 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC8215882 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC196576711 ZINC	0.842	490.2 Da LogP -0.63 TPSA 264.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](N)[C@H](CO[P@@](=O)…`
ZINC111459735 ZINC	0.836	481.2 Da LogP -1.20 TPSA 249.9	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](N)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC138164075 ZINC	0.836	498.2 Da LogP 0.21 TPSA 227.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC12958401 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@@H](COP(=O)(O)…`
ZINC13538980 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@@H](COP(=O)(O…`
ZINC13538982 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](COP(=O)(O)…`
ZINC1532626 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](COP(=O)(O)…`
ZINC1713574 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](COP(=O)(O)O…`
ZINC3869813 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](COP(=O)(O)O…`
ZINC3869814 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](COP(=O)(O)O)…`
ZINC3869815 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](COP(=O)(O)O…`
ZINC142512519 ZINC	0.818	498.2 Da LogP 0.21 TPSA 227.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
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(=…`
ZINC8217141 ZINC	0.807	492.2 Da LogP -0.48 TPSA 253.1	2 viol.	✓ Clean	`O=P(O)(O)O[P@](=O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H…`
ZINC13523519 ZINC	0.804	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532628 ZINC	0.804	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC1678872 ZINC	0.804	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=O…`
ZINC2047010 ZINC	0.804	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870253 ZINC	0.804	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870254 ZINC	0.804	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O)…`

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 A0A0H3GQ64