KpATCC43816 Protein target profile

exodeoxyribonuclease V, beta subunit

Accession: VK055_4296

Gene: recB AIK82841.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GSM0

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Length 1178

Pocket druggability (P2Rank · AlphaFold DB model) 0.789

Direct ligand evidence 0 52 total records

Functional annotation 2 EC 12 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

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: No hit
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 75.424 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 90.05 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) 0.789

Structure A0A0H3GSM0

Pocket Pocket 1

Druggability (FPocket) 0.499

Structure A0A0H3GSM0

Pocket Pocket 5

ColabFold model

P2Rank 0.805 · Pocket 1

FPocket 0.229 · Pocket 102

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 110 / 4744 genomes with a hit

Prevalence 2.3%

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.

MTDTAESLDPLRLPLIGERLIEASAGTGKTFTIAALYLRLLLGLGGEAAYPRAISVEELLVVTFTEAATEELRGRIRSNIHELRIACLRGESDNPLYSALLAEIADKDDAAKTLLLAERQMDEAAVFTIHGFCQRMLSLNAFESGMLFEQQLIEDESRLRYQACADFWRRHCYPLTRDIAAVIHDVWKGPRDLLKSLDRWLQGEAPQLKSPPAPNETLAERHQQIIARIDSLKQQWREQVGEIEGVLENSGLDRRKFNRGNQGKWMEKVNAWAQEETLSYQLPDALEKFAQSFLLERTKAGGEPPVHPLFSAVESLLASSLTLTDLVLARAMVEIRDAVAREKRRRGELGFDDMLSRLDEALRGDSGETLASAIRQRFPVAMIDEFQDTDPQQYRIFRRIWRRQPETALLLIGDPKQAIYAFRGADIFTYMKARGDVAAHYTLDTNWRSSPGMVGSVNRLFSLSDNPFMFHEIPFLPVKAAAKNKGLRFTVDAADVPAMNVWLMPGDTVGSGDYQTFMAQLCATQIRDWLSAGQQGRALLWRGETSRPVQASDITVLVRNRLEAAQVREALQTLGIPSVYLSNRDSVFETLEAQELLWLLQAVLAPERENTLRSALATSMFGLTALDIENLNQDEQAWDALVEEFSEYRQIWRQRGVMPMLRALMTARHIAENLLATRGGERRLTDILHISELLQEAASQLESEHALVRWLAQHIAEPDSNAASQQMRLESDKHLVQIVTIHKSKGLEYPLVWLPFIARFRKQDQAFYHDRETFAAVLDLGQDEASLELAEAERLAEDLRLLYVALTRAVWHCSLGVAPLSSRKSGNSDFHLSALGRLLQAGEAMDAAGLAARLADFCHGDIALQIPGELDLTPWQAPAATIPRLSARELQRRIADDWRVTSYSGLQQHGFSGGQDLLPRLDVDAAGVGEVVEEPQLTPHQFPRGAAPGTFLHSLFEELDFTQPVPEGWMAEKLQLSGFDAQWAPVLTDWLGGVLKTRLPGPDIALNQLAARDKQVEMAFYLPIAQLLTAERLDALIRQYDPLSADTPPLDFRQVRGMLKGFIDLVFRHEGRYYLLDYKSNWLGEDREAYTRPAMEQAMRAHRYDLQYQLYSLALHRYLRHRLADYDYDRHFGGVIYLFLRGMDGQEGGQGIFTTRPVRPLIDGLDQLFAGETQEEAS

MTDTAESLDPLRLPLIGERLIEASAGTGKTFTIAALYLRLLLGLGGEAAYPRAISVEELLVVTFTEAATEELRGRIRSNIHELRIACLRGESDNPLYSALLAEIADKDDAAKTLLLAERQMDEAAVFTIHGFCQRMLSLNAFESGMLFEQQLIEDESRLRYQACADFWRRHCYPLTRDIAAVIHDVWKGPRDLLKSLDRWLQGEAPQLKSPPAPNETLAERHQQIIARIDSLKQQWREQVGEIEGVLENSGLDRRKFNRGNQGKWMEKVNAWAQEETLSYQLPDALEKFAQSFLLERTKAGGEPPVHPLFSAVESLLASSLTLTDLVLARAMVEIRDAVAREKRRRGELGFDDMLSRLDEALRGDSGETLASAIRQRFPVAMIDEFQDTDPQQYRIFRRIWRRQPETALLLIGDPKQAIYAFRGADIFTYMKARGDVAAHYTLDTNWRSSPGMVGSVNRLFSLSDNPFMFHEIPFLPVKAAAKNKGLRFTVDAADVPAMNVWLMPGDTVGSGDYQTFMAQLCATQIRDWLSAGQQGRALLWRGETSRPVQASDITVLVRNRLEAAQVREALQTLGIPSVYLSNRDSVFETLEAQELLWLLQAVLAPERENTLRSALATSMFGLTALDIENLNQDEQAWDALVEEFSEYRQIWRQRGVMPMLRALMTARHIAENLLATRGGERRLTDILHISELLQEAASQLESEHALVRWLAQHIAEPDSNAASQQMRLESDKHLVQIVTIHKSKGLEYPLVWLPFIARFRKQDQAFYHDRETFAAVLDLGQDEASLELAEAERLAEDLRLLYVALTRAVWHCSLGVAPLSSRKSGNSDFHLSALGRLLQAGEAMDAAGLAARLADFCHGDIALQIPGELDLTPWQAPAATIPRLSARELQRRIADDWRVTSYSGLQQHGFSGGQDLLPRLDVDAAGVGEVVEEPQLTPHQFPRGAAPGTFLHSLFEELDFTQPVPEGWMAEKLQLSGFDAQWAPVLTDWLGGVLKTRLPGPDIALNQLAARDKQVEMAFYLPIAQLLTAERLDALIRQYDPLSADTPPLDFRQVRGMLKGFIDLVFRHEGRYYLLDYKSNWLGEDREAYTRPAMEQAMRAHRYDLQYQLYSLALHRYLRHRLADYDYDRHFGGVIYLFLRGMDGQEGGQGIFTTRPVRPLIDGLDQLFAGETQEEAS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 12 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0008854 Catalysis of the exonucleolytic cleavage (in the presence of ATP) in either 5' to 3' or 3' to 5' direction to yield 5'-phosphooligonucleotides.
GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
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:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
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:0009338 An enzyme complex that catalyzes exonucleolytic cleavage (in the presence of ATP) in either 5' to 3' or 3' to 5' direction to yield 5'-phosphooligonucleotides. Exodeoxyribonuclease V shows a preference for double-stranded DNA and possesses DNA-dependent ATPase activity. It acts endonucleolytically on single-stranded circular DNA.
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:0000287 Binding to a magnesium (Mg) ion.
GO:0000724 The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
886	1177	Gene3D	G3DSA:3.90.320.10	-
886	1177	InterPro	IPR011604	PD-(D/E)XK endonuclease-like domain superfamily
19	833	PANTHER	PTHR11070	UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
19	833	InterPro	IPR000212	DNA helicase, UvrD/REP type
947	1140	Pfam	PF12705	PD-(D/E)XK nuclease superfamily
947	1140	InterPro	IPR038726	PD-(D/E)XK endonuclease-like domain, AddAB-type
2	450	ProSiteProfiles	PS51198	UvrD-like DNA helicase ATP-binding domain profile.
2	450	InterPro	IPR014016	UvrD-like helicase, ATP-binding domain
8	1169	NCBIfam	TIGR00609	exodeoxyribonuclease V subunit beta
8	1169	InterPro	IPR004586	RecBCD enzyme subunit RecB
445	843	Gene3D	G3DSA:3.40.50.300	-
445	843	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
19	826	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
19	826	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
898	1166	CDD	cd22352	RecB_C-like
15	436	Pfam	PF00580	UvrD/REP helicase N-terminal domain
15	436	InterPro	IPR014016	UvrD-like helicase, ATP-binding domain
480	746	ProSiteProfiles	PS51217	UvrD-like DNA helicase C-terminal domain profile.
480	746	InterPro	IPR014017	UvrD-like DNA helicase, C-terminal
886	1176	FunFam	G3DSA:3.90.320.10:FF:000003	RecBCD enzyme subunit RecB
896	1171	SUPERFAMILY	SSF52980	Restriction endonuclease-like
896	1171	InterPro	IPR011335	Restriction endonuclease type II-like
441	809	Pfam	PF13361	UvrD-like helicase C-terminal domain
441	809	InterPro	IPR014017	UvrD-like DNA helicase, C-terminal
155	349	Gene3D	G3DSA:1.10.3170.10	Recbcd, chain B, domain 2
736	816	CDD	cd18807	SF1_C_UvrD
782	809	Coils	Coil	Coil
215	235	Coils	Coil	Coil
5	1170	Hamap	MF_01485	RecBCD enzyme subunit RecB [recB].
5	1170	InterPro	IPR004586	RecBCD enzyme subunit RecB
8	436	Gene3D	G3DSA:3.40.50.300	-
8	436	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
583	728	Gene3D	G3DSA:1.10.486.10	PCRA; domain 4

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

0.789

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Surrounding area

Pocket 2 P2Rank #2

0.779

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Surrounding area

Pocket 3 P2Rank #3

0.705

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Surrounding area

Pocket 4 P2Rank #4

0.479

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Surrounding area

Pocket 5 P2Rank #5

0.28

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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 #5

0.499

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Surrounding area

Residue sets

UniProt: Active site:1077-1077 For nuclease activity

UniProt: Binding site:1064-1064

UniProt: Binding site:1077-1077

UniProt: Binding site:23-30

UniProt: Binding site:953-953

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.805

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Surrounding area

Pocket 2 P2Rank #2

0.802

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Surrounding area

Pocket 3 P2Rank #3

0.755

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Surrounding area

Pocket 4 P2Rank #4

0.465

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Surrounding area

Pocket 5 P2Rank #5

0.175

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Surrounding area

Residue sets

UniProt: Active site:1077-1077 For nuclease activity

UniProt: Binding site:1064-1064

UniProt: Binding site:1077-1077

UniProt: Binding site:23-30

UniProt: Binding site:953-953

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_A0A0H3GSM0	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4296	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ANP PDB via homolog 506.2 Da · LogP -2.06 · TPSA 281.9 Open detail RCSB PDB

MGF PDB via homolog Detail RCSB PDB

ZINC12360002 ZINC proposed compound · Tanimoto 0.810 Detail ZINC

ZINC12360703 ZINC proposed compound · Tanimoto 0.810 Detail ZINC

ZINC12503599 ZINC proposed compound · Tanimoto 0.810 Detail ZINC

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
ANP RCSB PDB	2IS4	P03018	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)…`
MGF RCSB PDB	2IS6	P03018	81.3 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-](F)F`

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
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(=…`
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…`
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@@…`
ZINC12503850 ZINC	0.726	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	0.726	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	0.726	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	0.726	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	0.712	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	0.712	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	0.712	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	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.703	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC105469665 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC5615251 ZINC	0.677	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615253 ZINC	0.677	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC5615258 ZINC	0.677	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615263 ZINC	0.677	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC31516918 ZINC	0.672	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC1582675 ZINC	0.667	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730 ZINC	0.667	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486734 ZINC	0.667	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC5486740 ZINC	0.667	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`

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 A0A0H3GSM0