KpATCC43816 Protein target profile

aerobic respiration control sensor protein arcB

Accession: VK055_3858

Gene: AIK82408.1 arcB 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GZ10

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Length 779

Pocket druggability (P2Rank · AlphaFold DB model) 0.932

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 11 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 0.93. 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: 2.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 39.623 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 82.15 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) 0.932

Structure A0A0H3GZ10

Pocket Pocket 1

Druggability (FPocket) 0.869

Structure A0A0H3GZ10

Pocket Pocket 21

ColabFold model

P2Rank 0.954 · Pocket 1

FPocket 0.835 · Pocket 13

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 123 / 4744 genomes with a hit

Prevalence 2.6%

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.

MKQIRMLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVDKLEEMRERDLKLNVQLKDNIAQLNQEIGEREKAEAERETTLEQLKIEMKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLIHLKPQDVYSEEAAEKVLETDEKVFRHNVSLTYEQWLDYPDGRKACFEIRKVPYYDRVGKRRGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTSEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFLADLENLSGLQAQQKGLRFVLEPSLPLPHKVITDGTRLRQILWNLISNAVKFTPQGGGVNVRVRYDEGDILHFEVEDSGIGIPEAEQDKIFAMYYQVKDSHGGKPATGTGIGLAVSRRLARNMGGDISVTSQPGKGATFTLTVHAPAIAEEVEDTLAEDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFEPGEYDLVLLDIQLPDMTGLDISRELKQRFAADELPPLVALTANVLKNKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDAPDEEAQEAPAADLHKAEAVLDTDMLEQYIELVGPKLINDGLAVFEKMMPGYMSVLESNLTARDQKGIVEEGHKIKGAAGSIGLRHIQQLGQQIQTPDLPAWSDNVAEWVEEMKSEWQNDVAVLKAWVAKASKK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 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:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
GO:0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine.
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.
GO:0009927 Serves as a phospho-His intermediate enabling the transfer of phospho group between a hybrid kinase and a response regulator.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

85 records

Show feature table

Start	End	DB	Term	Name
394	508	SMART	SM00387	HKATPase_4
394	508	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
1	89	FunFam	G3DSA:1.10.287.970:FF:000001	Aerobic respiration control sensor protein
663	774	SUPERFAMILY	SSF47226	Histidine-containing phosphotransfer domain, HPT domain
663	774	InterPro	IPR036641	HPT domain superfamily
142	267	SUPERFAMILY	SSF55785	PYP-like sensor domain (PAS domain)
142	267	InterPro	IPR035965	PAS domain superfamily
77	153	Coils	Coil	Coil
679	772	ProSiteProfiles	PS50894	Histidine-containing phosphotransfer (HPt) domain profile.
679	772	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
510	647	Gene3D	G3DSA:3.40.50.2300	-
282	347	SMART	SM00388	HisKA_10
282	347	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
289	508	ProSiteProfiles	PS50109	Histidine kinase domain profile.
289	508	InterPro	IPR005467	Histidine kinase domain
348	509	Gene3D	G3DSA:3.30.565.10	-
348	509	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
153	223	ProSiteProfiles	PS50112	PAS repeat profile.
153	223	InterPro	IPR000014	PAS domain
55	77	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
155	221	SMART	SM00091	pas_2
155	221	InterPro	IPR000014	PAS domain
527	640	SMART	SM00448	REC_2
527	640	InterPro	IPR001789	Signal transduction response regulator, receiver domain
348	509	FunFam	G3DSA:3.30.565.10:FF:000025	Aerobic respiration control sensor protein
20	42	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
676	773	SMART	SM00073	hpt_2
676	773	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
395	505	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
395	505	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
529	640	Pfam	PF00072	Response regulator receiver domain
529	640	InterPro	IPR001789	Signal transduction response regulator, receiver domain
280	341	CDD	cd00082	HisKA
280	341	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
140	278	Gene3D	G3DSA:3.30.450.20	PAS domain
527	645	SUPERFAMILY	SSF52172	CheY-like
527	645	InterPro	IPR011006	CheY-like superfamily
128	645	PANTHER	PTHR43047	TWO-COMPONENT HISTIDINE PROTEIN KINASE
279	346	Gene3D	G3DSA:1.10.287.130	-
164	266	CDD	cd00130	PAS
164	266	InterPro	IPR000014	PAS domain
283	346	Pfam	PF00512	His Kinase A (phospho-acceptor) domain
283	346	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
336	504	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
336	504	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
226	278	ProSiteProfiles	PS50113	PAC domain profile.
226	278	InterPro	IPR000700	PAS-associated, C-terminal
687	761	Pfam	PF01627	Hpt domain
687	761	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
267	345	FunFam	G3DSA:1.10.287.130:FF:000016	Aerobic respiration control sensor protein
78	779	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
492	505	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
492	505	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
450	460	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
450	460	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
468	486	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
468	486	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
432	446	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
432	446	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
15	89	Pfam	PF18415	Histidine kinase receptor ArcB trans-membrane domain
15	89	InterPro	IPR040642	Histidine kinase receptor ArcB, transmembrane domain
1	779	PIRSF	PIRSF003182	HK_hybr_ArcB
1	779	InterPro	IPR014409	Signal transduction histidine kinase, hybrid-type, aerobic respiration control ArcB
151	266	FunFam	G3DSA:3.30.450.20:FF:000032	Aerobic respiration control sensor protein
269	347	SUPERFAMILY	SSF47384	Homodimeric domain of signal transducing histidine kinase
269	347	InterPro	IPR036097	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
1	89	Gene3D	G3DSA:1.10.287.970	His Kinase A (phosphoacceptor) domain
1	89	InterPro	IPR027460	Aerobic respiration control sensor protein ArcB, transmembrane domain superfamily
47	57	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
152	276	NCBIfam	TIGR00229	PAS domain S-box protein
152	276	InterPro	IPR000014	PAS domain
58	77	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	19	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
510	651	FunFam	G3DSA:3.40.50.2300:FF:000107	Aerobic respiration control sensor protein
156	266	Pfam	PF00989	PAS fold
156	266	InterPro	IPR013767	PAS fold
399	505	CDD	cd16922	HATPase_EvgS-ArcB-TorS-like
656	779	Gene3D	G3DSA:1.20.120.160	HPT domain
656	779	InterPro	IPR036641	HPT domain superfamily
20	46	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
683	763	CDD	cd00088	HPT
683	763	InterPro	IPR008207	Signal transduction histidine kinase, phosphotransfer (Hpt) domain
529	640	CDD	cd17546	REC_hyHK_CKI1_RcsC-like
528	644	ProSiteProfiles	PS50110	Response regulatory domain profile.
528	644	InterPro	IPR001789	Signal transduction response regulator, receiver 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

0.932

Likely same site as FPocket 21 1.9 Å 25 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.011

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Surrounding area

Pocket 3 P2Rank #3

0.004

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Surrounding area

Pocket 4 P2Rank #4

0.001

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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 #21

0.869 Unusual size

Likely same site as P2Rank 1 1.9 Å 25 shared residues 96% 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

0.954

Likely same site as FPocket 13 0.6 Å 33 shared residues 97% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.023

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Surrounding area

Pocket 3 P2Rank #3

0.0

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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 #13

0.835 Unusual size

Likely same site as P2Rank 1 0.6 Å 33 shared residues 97% of smaller site

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Surrounding area

Pocket 2 FPocket #71

0.591

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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_A0A0H3GZ10	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3858	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.

55 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 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

MBN PDB via homolog Detail RCSB PDB

XBZ 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
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`
MBN RCSB PDB	5HWV	A5W4E3	92.1 Da LogP 2.00 TPSA 0.0	✓ Ro5	✓ Clean	`Cc1ccccc1`
XBZ RCSB PDB	5HWW	A5W4E3	120.2 Da LogP 2.61 TPSA 0.0	✓ Ro5	✓ Clean	`Cc1ccc(c(c1)C)C`

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…`
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 A0A0H3GZ10