KpKP13 Protein target profile

Sensor protein kdpD

Accession: KP13_03298

Gene: AHE45677.1 kdpD 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GK10

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Length 895

Pocket druggability (P2Rank · AlphaFold DB model) 0.926

Direct ligand evidence 0 54 total records

Functional annotation 1 EC 12 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

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: 2.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 81.57 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) 0.926

Structure A0A0H3GK10

Pocket Pocket 1

Druggability (FPocket) 0.334

Structure A0A0H3GK10

Pocket Pocket 69

ColabFold model

P2Rank 0.941 · Pocket 1

FPocket 0.916 · Pocket 62

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 103 / 4744 genomes with a hit

Prevalence 2.2%

Sequence

Primary amino-acid sequence viewer.

MSDEPLRPDPDRLLQHTAAPHRGKLKVFFGACAGVGKTWAMLAEAQRLRAQGLDILIGVAETHGRKETAAMLQGLSTLPPRRLAHRGRYVYEFDLDAALARRPALILVDELAHSNAPGSRHPKRWQDVDELLEAGIDVFTTVNVQHLESLNDVVSGITGVQVRETVPDPFFDAADDVVLVDLPPDDLRQRLNEGKVYIGGQAERAIENFFRKGNLIALRELALRRTADRVDEQMRAWRDRQGQEKVWHTRDAILLCIGHNTGSEKLVRAAARLAARLGSVWHAVYVETPSLHRLPEARRRAILAALRLAQELGAETATLSDPSEEKAVLHYAREHNLGKIVIGRQSKRRGWDRSGFADRLARHAPDLDLVVIALDEKPSPLPARGNDSRTALEKWRLQLQGCAVAVALCAIITLVAMQWLMAFEAANLVMLYLLGVVLIALVYGRWPSVLATVINVISFDLFFVAPRGTLAVSDVQYLLTFGVMLTVGLLIGNLTAGVRYQARVARYRERRTRHLYEMSKALAVGRSQQDIATTSERFIASTFQARSQLLLPDAQGKLLPLTHQPGLTPWDDAIARWSFDKGQPAGAGTDTLPGVPYQILPLKSAARTWGLLVVEPENLRQLMIPEQQRLLETFTLLVASALERLTLTASEEQARLTSERESLRNSLLAALSHDLRTPLTVLFGQAEILTLDLASEGSKHAPQANEIRQHVLNTTRLVNNLLDMARIQSGGFNLHKEWLTLEEVVGSALRMLEPSLGGQHIQLDLPDPLQLVHVDGPLFERVLINLLENAHKYAGARASIGIRAEADARQLSLEVWDNGPGIPAGQEQTIFDKFARGNKESAIPGVGLGLAICQAIVDVHGGTISASNRPEGGASFRVTLPGETPPELEELPEEL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

2.7.13.3

Gene Ontology (GO)

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:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
GO:0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0005515 Binding to a protein.
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: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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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:0042802 Binding to an identical protein or proteins.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

63 records

Show feature table

Start	End	DB	Term	Name
779	880	CDD	cd00075	HATPase
512	656	FunFam	G3DSA:3.30.450.40:FF:000038	Two-component sensor histidine kinase KdpD
1	398	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
253	365	SUPERFAMILY	SSF52402	Adenine nucleotide alpha hydrolases-like
253	373	CDD	cd01987	USP_OKCHK
719	886	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
719	886	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
428	445	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
661	726	CDD	cd00082	HisKA
661	726	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
448	465	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
19	229	Gene3D	G3DSA:3.40.50.300	-
19	229	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
21	230	Pfam	PF02702	Osmosensitive K+ channel His kinase sensor domain
21	230	InterPro	IPR003852	Signal transduction histidine kinase, osmosensitive K+ channel sensor, N-terminal
501	895	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
466	476	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
829	839	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
829	839	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
868	881	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
868	881	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
844	862	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
844	862	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
811	825	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
811	825	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
19	229	FunFam	G3DSA:3.40.50.300:FF:000483	Sensor histidine kinase KdpD
477	500	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
403	507	Pfam	PF13493	Domain of unknown function (DUF4118)
403	507	InterPro	IPR025201	Sensor protein KdpD, transmembrane domain
658	731	SUPERFAMILY	SSF47384	Homodimeric domain of signal transducing histidine kinase
658	731	InterPro	IPR036097	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
734	886	FunFam	G3DSA:3.30.565.10:FF:000042	Two-component sensor histidine kinase KdpD
658	732	Gene3D	G3DSA:1.10.287.130	-
232	372	Gene3D	G3DSA:3.40.50.620	HUPs
232	372	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
444	447	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
399	419	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	885	PANTHER	PTHR45569	SENSOR PROTEIN KDPD
670	884	ProSiteProfiles	PS50109	Histidine kinase domain profile.
670	884	InterPro	IPR005467	Histidine kinase domain
665	730	Pfam	PF00512	His Kinase A (phospho-acceptor) domain
665	730	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
774	884	SMART	SM00387	HKATPase_4
774	884	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
733	883	Gene3D	G3DSA:3.30.565.10	-
733	883	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
529	644	Pfam	PF13492	GAF domain
529	644	InterPro	IPR003018	GAF domain
401	423	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
420	424	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
396	502	Gene3D	G3DSA:1.20.120.620	Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd,
396	502	InterPro	IPR038318	KdpD, transmembrane domain superfamily
512	657	Gene3D	G3DSA:3.30.450.40	-
512	657	InterPro	IPR029016	GAF-like domain superfamily
449	471	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
778	883	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
778	883	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
425	443	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
397	502	FunFam	G3DSA:1.20.120.620:FF:000001	Two-component sensor histidine kinase KdpD
478	500	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
663	730	SMART	SM00388	HisKA_10
663	730	InterPro	IPR003661	Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
239	372	FunFam	G3DSA:3.40.50.620:FF:000169	Two-component system sensor histidine kinase KdbD

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

0.926

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Surrounding area

Pocket 2 P2Rank #2

0.87

Likely same site as FPocket 69 1.5 Å 30 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.602

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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 #69

0.334 Unusual size

Likely same site as P2Rank 2 1.5 Å 30 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #51

0.289

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Surrounding area

Pocket 3 FPocket #80

0.275 Unusual size

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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

0.941

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Surrounding area

Pocket 2 P2Rank #2

0.913

Likely same site as FPocket 62 0.9 Å 29 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.476

Likely same site as FPocket 1 1.7 Å 18 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.08

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Surrounding area

Pocket 5 P2Rank #5

0.022

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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 #62

0.916 Unusual size

Likely same site as P2Rank 2 0.9 Å 29 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #1

0.425

Likely same site as P2Rank 3 1.7 Å 18 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #11

0.282

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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_A0A0H3GK10	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03298	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 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

EMC PDB via homolog Detail RCSB PDB

EMT PDB via homolog Detail RCSB PDB

RDC PDB via homolog Detail RCSB PDB

ZINC100006925 ZINC proposed compound · Tanimoto 1.000 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	4BIW	P0AE82	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)…`
EMC RCSB PDB	3A0W	Q9X180	229.7 Da LogP 0.97 TPSA 0.0	✓ Ro5	✓ Clean	`CC[Hg+]`
EMT RCSB PDB	3A0W	Q9X180	382.8 Da LogP 2.91 TPSA 37.3	✓ Ro5	✓ Clean	`CC[Hg]Sc1ccccc1C(=O)O`
RDC RCSB PDB	3CGY	P0DM80	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2[C@H](O2)\C=C/C=C/C(=O)Cc3c(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
ZINC100006925 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C\C=C/C(=O)Cc2c(Cl)c(…`
ZINC100013319 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O…`
ZINC100013323 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@H]2O[C@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O)…`
ZINC100152234 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C/C=C/C(=O)Cc2c(Cl)c(…`
ZINC13521629 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C\C=C\C(=O)Cc2c(Cl)c(…`
ZINC2061000778 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)cc…`
ZINC253952046 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)c…`
ZINC253987424 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2C=CC=CC(=O)Cc2c(Cl)c(O)c…`
ZINC253987427 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2C=CC=CC(=O)Cc2c(Cl)c(O)cc…`
ZINC253987428 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@@H]2C=CC=CC(=O)Cc2c(Cl)c(O)…`
ZINC33838895 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@H]2/C=C\C=C/C(=O)Cc2c(Cl)c(O…`
ZINC45789132 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@H]2O[C@@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(…`
ZINC45789135 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@H]1C[C@H]2O[C@@H]2/C=C/C=C\C(=O)Cc2c(Cl)c(O…`
ZINC5492965 ZINC	1.000	364.8 Da LogP 2.69 TPSA 96.4	✓ Ro5	✓ Clean	`C[C@@H]1C[C@@H]2O[C@H]2/C=C\C=C\C(=O)Cc2c(Cl)c(…`
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`

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 A0A0H3GK10