KpATCC43816 Protein target profile

hybrid sensory histidine kinase, in two-component regulatory system with UvrY

Accession: VK055_4386

Gene: barA AIK82929.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GUH1

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Length 916

Pocket druggability (P2Rank · AlphaFold DB model) 0.876

Direct ligand evidence 0 53 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

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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.88. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

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: 2.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 37.069 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 81.3 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) 0.876

Structure A0A0H3GUH1

Pocket Pocket 1

Druggability (FPocket) 0.563

Structure A0A0H3GUH1

Pocket Pocket 53

ColabFold model

P2Rank 0.936 · Pocket 1

FPocket 0.945 · Pocket 23

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 101 / 4744 genomes with a hit

Prevalence 2.1%

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.

MTNYSLRARMMILILAPTVLIGLLLSIFFVAHRYNDLQRQLEDAGASIIEPLAVSSEYGMNLQNRESIGQLISVLHRRHSEIVRAISVYDSHNRLFVTSNYQLNPSELQIPKGEAFPRHLSVIRDGDMMILRTPIVSESYSPDESPESDAKMPGNMLGYVALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNVDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTDLNATQRDHLTTIERSANNLLAIINDVLDFSKLEAGKLILESIPFLLRTSLDEVVTLLAHSAHDKGLELTLNIKNNVPDNVIGDPLRLQQIVTNLVGNAIKFTEHGNIDVLVEQRAISNSRVQIEIQIHDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQRLVKEMGGDISFHSQPNRGSTFWFHISLDLNPNAIPDTLNTDGLVGKRLAYVEANATAAQCTLEMLAATPLEVIYSPTFSSLAEAQYDILLVGIPVSMRDLSPHREKLAKACAMSDNVLLALPCHAQVSAEALKRDGVAACLLKPLTTTRLLPALVATSHALASAPLMQIDSHKLPMTVMAVDDNPANLKLIGALLDDLVQQVILCDSGQQAVDKAKQLQMDLILMDIQMPDMDGIRACELIHHLSHHQQTPVIAVTAHALEGQREKLLSAGMNDYLAKPIEEEKLHALLLRYQPGLHSVVPASLPPTEPIVDHNQTLDWQLALRQAAMKPDLAREMLQMLIAFMPEVRNKVEEQLVGEQPEGLVDLIHKLHGSCSYSGVPRLKKLCHTLESQLRAGTAAEDLEPELLELLDEMDNVAREACRMGV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

2.7.13.3

Gene Ontology (GO)

GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0000155 Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response.
GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
GO:0000160 A conserved series of molecular signals found in prokaryotes and eukaryotes; involves autophosphorylation of a histidine kinase and the transfer of the phosphate group to an aspartate that then acts as a phospho-donor to response regulator proteins.
GO:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

71 records

Show feature table

Start	End	DB	Term	Name
653	786	Gene3D	G3DSA:3.40.50.2300	-
669	779	Pfam	PF00072	Response regulator receiver domain
669	779	InterPro	IPR001789	Signal transduction response regulator, receiver domain
409	518	CDD	cd16922	HATPase_EvgS-ArcB-TorS-like
293	357	Pfam	PF00512	His Kinase A (phospho-acceptor) domain
293	357	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
277	358	SUPERFAMILY	SSF47384	Homodimeric domain of signal transducing histidine kinase
277	358	InterPro	IPR036097	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
299	520	ProSiteProfiles	PS50109	Histidine kinase domain profile.
299	520	InterPro	IPR005467	Histidine kinase domain
200	249	SUPERFAMILY	SSF158472	HAMP domain-like
177	199	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
257	355	FunFam	G3DSA:1.10.287.130:FF:000003	Histidine kinase
200	916	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
667	780	SMART	SM00448	REC_2
667	780	InterPro	IPR001789	Signal transduction response regulator, receiver domain
1	11	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
32	177	Pfam	PF09984	Single cache domain 4
32	177	InterPro	IPR019247	Histidine kinase BarA, N-terminal
666	785	SUPERFAMILY	SSF52172	CheY-like
666	785	InterPro	IPR011006	CheY-like superfamily
292	357	SMART	SM00388	HisKA_10
292	357	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
12	31	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
820	887	CDD	cd00088	HPT
820	887	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
10	32	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
356	522	FunFam	G3DSA:3.30.565.10:FF:000020	Histidine kinase
826	906	Pfam	PF01627	Hpt domain
826	906	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
669	780	CDD	cd17546	REC_hyHK_CKI1_RcsC-like
200	252	ProSiteProfiles	PS50885	HAMP domain profile.
200	252	InterPro	IPR003660	HAMP domain
168	256	Gene3D	G3DSA:6.10.340.10	-
257	355	Gene3D	G3DSA:1.10.287.130	-
804	914	Gene3D	G3DSA:1.20.120.160	HPT domain
804	914	InterPro	IPR036641	HPT domain superfamily
668	784	ProSiteProfiles	PS50110	Response regulatory domain profile.
668	784	InterPro	IPR001789	Signal transduction response regulator, receiver domain
817	912	SMART	SM00073	hpt_2
817	912	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
198	247	Pfam	PF00672	HAMP domain
198	247	InterPro	IPR003660	HAMP domain
251	289	Coils	Coil	Coil
820	915	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
820	915	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
177	199	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
404	520	SMART	SM00387	HKATPase_4
404	520	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
763	907	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
763	907	InterPro	IPR036641	HPT domain superfamily
346	517	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
346	517	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
463	473	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
463	473	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
445	459	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
445	459	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
480	498	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
480	498	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
504	517	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
504	517	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
32	176	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
404	519	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
404	519	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
203	247	CDD	cd06225	HAMP
291	353	CDD	cd00082	HisKA
291	353	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
237	783	PANTHER	PTHR45339	HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J
200	252	SMART	SM00304	HAMP_11
356	522	Gene3D	G3DSA:3.30.565.10	-
356	522	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily

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

0.876

Likely same site as FPocket 53 5.7 Å 18 shared residues 62% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.747

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Surrounding area

Pocket 3 P2Rank #3

0.406

Likely same site as FPocket 3 0.5 Å 17 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.035

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Surrounding area

Pocket 5 P2Rank #5

0.024

Likely same site as FPocket 67 3.4 Å 7 shared residues 88% 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 #53

0.563 Unusual size

Likely same site as P2Rank 1 5.7 Å 18 shared residues 62% of smaller site

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Surrounding area

Pocket 2 FPocket #3

0.333

Likely same site as P2Rank 3 0.5 Å 17 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #67

0.256

Likely same site as P2Rank 5 3.4 Å 7 shared residues 88% 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

0.936

Likely same site as FPocket 23 1.8 Å 31 shared residues 94% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.3

Likely same site as FPocket 81 5.9 Å 13 shared residues 87% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.179

Likely same site as FPocket 4 3.4 Å 16 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.105

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Surrounding area

Pocket 5 P2Rank #5

0.093

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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 #23

0.945 Unusual size

Likely same site as P2Rank 1 1.8 Å 31 shared residues 94% of smaller site

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Surrounding area

Pocket 2 FPocket #4

0.542 Unusual size

Likely same site as P2Rank 3 3.4 Å 16 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #81

0.215 Unusual size

Likely same site as P2Rank 2 5.9 Å 13 shared residues 87% of smaller site

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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_A0A0H3GUH1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4386	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 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

BEF PDB via homolog Detail RCSB PDB

BTB PDB via homolog Detail RCSB PDB

ZINC1615342 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC12360002 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	6QRJ	Q9ABT2	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)…`
BEF RCSB PDB	5N2N	O22267	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
BTB RCSB PDB	3IQT	P0AEC6	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`

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
ZINC1615342 ZINC	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
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)…`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)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)[…`

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 A0A0H3GUH1