KpATCC43816 Protein target profile

ribonuclease E

Accession: VK055_1382

Gene: AIK80005.1 rne 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GLF7

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Length 1077

Pocket druggability (P2Rank · AlphaFold DB model) 0.761

Direct ligand evidence 0 51 total records

Functional annotation 1 EC 14 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

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.76, FPocket 0.83). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Strong predicted binding pocket FPocket selected-pocket score 0.83. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.76. 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: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 75.068 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 61.58 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) 0.761

Structure A0A0H3GLF7

Pocket Pocket 1

Druggability (FPocket) 0.832

Structure A0A0H3GLF7

Pocket Pocket 68

ColabFold model

P2Rank 0.763 · Pocket 1

FPocket 0.21 · Pocket 71

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 107 / 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.

MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPANYNAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLELPDGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIQKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESSHHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTKEVHAIVPVPIASYLLNEKRAAVSAIESRQGDVRVIIVPNDEMQTPHYSVLRVRKGEETSTLSYLLPKLHEEEMALPGDDEPAERKRPEQPALAAFVMPDAPPAPMLEEPAAAPVAAAAPVAAAAPAQPGLLSRFFSALKNIFSGAEEAKPAEVQVEKKAEEKPERQQERRKPRANNRRDRNDRRDNRDNRDNRDNRDNRDTRADNAEGREPRESREENRRNRREKPSQNVEARDVRQTSGDDAEKAKSRDEQQPRRERTRRRNDDKRQAQQEAKAQTREEPVVQETEQEERVQTLPRRKPRQLAQKVRVESAVVEPVAEIVPEAVVAEVIAPHSEPVKAELPAGVESVADQDENGESREANGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPEMASGKVWIRYPVVRPQDQQPEEVQVQDASVAKTVEAVAAPVAVVETVTAAPVTVEPATMEPVTAEPVVVEPVAAAEPLVVDAAEVVAPAAVEPAPQEPVTEAPAVEAPQAIAPVTLDPEPVVVEPEAVETTPVVAAPVETIAPVAETVEQAPVTEAAPAEPVKAEPPVSKPVVVAGHRHATAPMTRAPAPDYVPEAPRHSTWVRPPFAFEGKGAAGGHSATHKATAEPTRPQPVE

MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPANYNAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLELPDGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIQKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESSHHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTKEVHAIVPVPIASYLLNEKRAAVSAIESRQGDVRVIIVPNDEMQTPHYSVLRVRKGEETSTLSYLLPKLHEEEMALPGDDEPAERKRPEQPALAAFVMPDAPPAPMLEEPAAAPVAAAAPVAAAAPAQPGLLSRFFSALKNIFSGAEEAKPAEVQVEKKAEEKPERQQERRKPRANNRRDRNDRRDNRDNRDNRDNRDNRDTRADNAEGREPRESREENRRNRREKPSQNVEARDVRQTSGDDAEKAKSRDEQQPRRERTRRRNDDKRQAQQEAKAQTREEPVVQETEQEERVQTLPRRKPRQLAQKVRVESAVVEPVAEIVPEAVVAEVIAPHSEPVKAELPAGVESVADQDENGESREANGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPEMASGKVWIRYPVVRPQDQQPEEVQVQDASVAKTVEAVAAPVAVVETVTAAPVTVEPATMEPVTAEPVVVEPVAAAEPLVVDAAEVVAPAAVEPAPQEPVTEAPAVEAPQAIAPVTLDPEPVVVEPEAVETTPVVAAPVETIAPVAETVEQAPVTEAAPAEPVKAEPPVSKPVVVAGHRHATAPMTRAPAPDYVPEAPRHSTWVRPPFAFEGKGAAGGHSATHKATAEPTRPQPVE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 14 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.1.26.12

Gene Ontology (GO)

GO:0006396 Any process involved in the conversion of one or more primary RNA transcripts into one or more mature RNA molecules.
GO:0003676 Binding to a nucleic acid.
GO:0008995 Catalysis of the cleavage of single-stranded RNA that is monophosphorylated at its 5'-end; cleavage occurs predominantly at 5 nucleotides from the 5'-end and in A + U-rich regions, and is blocked by the presence of a 5'-triphosphate group.
GO:0004540 Catalysis of the cleavage of phosphodiester bonds in chains of RNA.
GO:0003723 Binding to an RNA molecule or a portion thereof.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0009898 The leaflet of the plasma membrane that faces the cytoplasm, including any protein embedded in, attached to, or peripherally associated with it.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0019843 Binding to a ribosomal RNA.
GO:0000049 Binding to a transfer RNA.
GO:0008270 Binding to a zinc ion (Zn).
GO:0006402 The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
GO:0006364 Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules.
GO:0008033 The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
1050	1077	MobiDBLite	mobidb-lite	consensus disorder prediction
36	118	Pfam	PF00575	S1 RNA binding domain
36	118	InterPro	IPR003029	S1 domain
39	119	ProSiteProfiles	PS50126	S1 domain profile.
39	119	InterPro	IPR003029	S1 domain
13	425	NCBIfam	TIGR00757	Rne/Rng family ribonuclease
13	425	InterPro	IPR004659	Ribonuclease E/G
590	734	MobiDBLite	mobidb-lite	consensus disorder prediction
693	713	Coils	Coil	Coil
401	510	Gene3D	G3DSA:3.40.1260.20	Ribonuclease E, catalytic domain
37	119	SMART	SM00316	S1_6
37	119	InterPro	IPR022967	RNA-binding domain, S1
121	391	Pfam	PF10150	Ribonuclease E/G family
121	391	InterPro	IPR019307	RNA-binding protein AU-1/Ribonuclease E/G
1	517	PANTHER	PTHR30001	RIBONUCLEASE
1	517	InterPro	IPR004659	Ribonuclease E/G
590	742	MobiDBLite	mobidb-lite	consensus disorder prediction
1038	1074	Pfam	PF12111	Polyribonucleotide phosphorylase C terminal
1038	1074	InterPro	IPR021968	Polyribonucleotide phosphorylase C-terminal
401	510	FunFam	G3DSA:3.40.1260.20:FF:000002	Ribonuclease E
1	1063	Hamap	MF_00970	Ribonuclease E [rne].
1	1063	InterPro	IPR028878	Ribonuclease E
778	827	MobiDBLite	mobidb-lite	consensus disorder prediction
508	524	MobiDBLite	mobidb-lite	consensus disorder prediction
32	124	CDD	cd04453	S1_RNase_E
31	125	Gene3D	G3DSA:2.40.50.140	-
31	125	InterPro	IPR012340	Nucleic acid-binding, OB-fold
788	803	MobiDBLite	mobidb-lite	consensus disorder prediction
40	124	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
40	124	InterPro	IPR012340	Nucleic acid-binding, OB-fold
31	125	FunFam	G3DSA:2.40.50.140:FF:000040	Ribonuclease E
508	537	MobiDBLite	mobidb-lite	consensus disorder prediction

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

0.761

Likely same site as FPocket 32 0.9 Å 18 shared residues 95% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.291

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Surrounding area

Pocket 3 P2Rank #3

0.06

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Surrounding area

Pocket 4 P2Rank #4

0.057

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Surrounding area

Pocket 5 P2Rank #5

0.025

Likely same site as FPocket 68 4.5 Å 7 shared residues 100% 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 #68

0.832

Likely same site as P2Rank 5 4.5 Å 7 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #32

0.811

Likely same site as P2Rank 1 0.9 Å 18 shared residues 95% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:303-303

UniProt: Binding site:346-346

UniProt: Binding site:404-404

UniProt: Binding site:407-407

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.763

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Surrounding area

Pocket 2 P2Rank #2

0.312

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Surrounding area

Pocket 3 P2Rank #3

0.212

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Surrounding area

Pocket 4 P2Rank #4

0.108

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Surrounding area

Pocket 5 P2Rank #5

0.098

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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_A0A0H3GLF7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1382	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.

51 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 1 records from similar proteins

Structural ligands 1 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

U PDB via homolog 324.2 Da · LogP -2.73 · TPSA 171.3 Open detail RCSB PDB

ZINC12503831 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC12503833 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC13512000 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC1532538 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
U RCSB PDB	6G63	P21513	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)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
ZINC12503831 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC12503833 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC13512000 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC1532538 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC2026984 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC2123545 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC2606131 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC36377965 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC3870257 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC3870258 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC3870259 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC3870260 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC9235501 ZINC	1.000	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H…`
ZINC35636069 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)OP(=O)(O)O)[…`
ZINC40655887 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)OP(=O)(O)O)[…`
ZINC40655889 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC44460318 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC4490939 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585026 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585028 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC8585030 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585032 ZINC	0.830	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC12959005 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC12959016 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O…`
ZINC13548378 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726233 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC3861755 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875255 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875256 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)…`
ZINC3875257 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875258 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)…`
ZINC88466482 ZINC	0.796	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC13517211 ZINC	0.787	340.2 Da LogP -1.37 TPSA 154.2	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC207686398 ZINC	0.745	438.2 Da LogP -1.91 TPSA 208.6	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)C(F)(F)P(=O)…`
ZINC71766855 ZINC	0.717	393.3 Da LogP -2.39 TPSA 163.5	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)N3CCOCC3)[C@…`
ZINC13514392 ZINC	0.694	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)…`
ZINC1532629 ZINC	0.694	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c…`
ZINC3869888 ZINC	0.694	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC3869889 ZINC	0.694	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869890 ZINC	0.694	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC4228260 ZINC	0.694	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC6524723 ZINC	0.694	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC102211562 ZINC	0.691	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC110347779 ZINC	0.691	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC110347782 ZINC	0.691	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC97976147 ZINC	0.691	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC231393132 ZINC	0.688	287.2 Da LogP -2.75 TPSA 156.9	✓ Ro5	✓ Clean	`NC(=O)OC[C@@H]1O[C@H](n2ccc(=O)[nH]c2=O)[C@H](O…`
ZINC5104173 ZINC	0.688	287.2 Da LogP -2.75 TPSA 156.9	✓ Ro5	✓ Clean	`NC(=O)OC[C@@H]1O[C@@H](n2ccc(=O)[nH]c2=O)[C@H](…`
ZINC5104174 ZINC	0.688	287.2 Da LogP -2.75 TPSA 156.9	✓ Ro5	✓ Clean	`NC(=O)OC[C@@H]1O[C@H](n2ccc(=O)[nH]c2=O)[C@@H](…`
ZINC5104175 ZINC	0.688	287.2 Da LogP -2.75 TPSA 156.9	✓ Ro5	✓ Clean	`NC(=O)OC[C@@H]1O[C@@H](n2ccc(=O)[nH]c2=O)[C@@H]…`

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 A0A0H3GLF7