KpATCC43816 Protein target profile

ribosomal protein S18

Accession: VK055_2867

Gene: rpsR AIK81456.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GHD3

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Length 75

Pocket druggability (FPocket · AlphaFold DB model) 0.58

Direct ligand evidence 0 62 total records

Functional annotation 0 EC 5 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. Moderate predicted binding pocket FPocket selected-pocket score 0.58. This supports review but is not experimental validation. 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: 33.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 100.0 Higher values support similarity to known essential genes.
DEG E-value: 3.22e-51 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 88.12 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)

Structure A0A0H3GHD3

Pocket No pockets

Druggability (FPocket) 0.58

Structure A0A0H3GHD3

Pocket Pocket 3

ColabFold model

FPocket 0.034 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1599 / 4744 genomes with a hit

Prevalence 33.7%

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.

MARYFRRRKFCRFTAEGVQEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
GO:0022627 The small subunit of a ribosome located in the cytosol.
GO:0070181 Binding to small ribosomal subunit RNA (SSU rRNA), a constituent of the small ribosomal subunit. In S. cerevisiae, this is the 18S rRNA.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
1	74	FunFam	G3DSA:4.10.640.10:FF:000001	30S ribosomal protein S18
2	73	Hamap	MF_00270	30S ribosomal protein S18 [rpsR].
2	73	InterPro	IPR001648	Ribosomal protein S18
3	74	SUPERFAMILY	SSF46911	Ribosomal protein S18
3	74	InterPro	IPR036870	Ribosomal protein S18 superfamily
8	73	PANTHER	PTHR13479	30S RIBOSOMAL PROTEIN S18
8	73	InterPro	IPR001648	Ribosomal protein S18
4	72	NCBIfam	TIGR00165	30S ribosomal protein S18
4	72	InterPro	IPR001648	Ribosomal protein S18
1	74	Gene3D	G3DSA:4.10.640.10	Ribosomal protein S18
1	74	InterPro	IPR036870	Ribosomal protein S18 superfamily
38	45	PRINTS	PR00974	Ribosomal protein S18 family signature
38	45	InterPro	IPR001648	Ribosomal protein S18
46	60	PRINTS	PR00974	Ribosomal protein S18 family signature
46	60	InterPro	IPR001648	Ribosomal protein S18
28	38	PRINTS	PR00974	Ribosomal protein S18 family signature
28	38	InterPro	IPR001648	Ribosomal protein S18
60	70	PRINTS	PR00974	Ribosomal protein S18 family signature
60	70	InterPro	IPR001648	Ribosomal protein S18
19	68	Pfam	PF01084	Ribosomal protein S18
19	68	InterPro	IPR001648	Ribosomal protein S18
21	44	ProSitePatterns	PS00057	Ribosomal protein S18 signature.
21	44	InterPro	IPR018275	Ribosomal protein S18, conserved site

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 · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #3

0.58

Show in viewer

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_A0A0H3GHD3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2867	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.

62 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 4 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AM2 PDB via homolog 539.6 Da · LogP -6.95 · TPSA 283.6 Open detail RCSB PDB

C PDB via homolog Detail RCSB PDB

FES PDB via homolog Detail RCSB PDB

GNP PDB via homolog Detail RCSB PDB

PAR 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
AM2 RCSB PDB	4AQY	Q5SLQ0	539.6 Da LogP -6.95 TPSA 283.6	3 viol.	✓ Clean	`CN[C@H]1[C@H]([C@@H]2[C@H](C[C@H]([C@H](O2)O[C@…`
C RCSB PDB	6CAO	Q5SLQ0	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
FES RCSB PDB	6RW4	Q9Y3D5	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
GNP RCSB PDB	6RW5	Q9Y3D5	522.2 Da LogP -2.76 TPSA 301.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
PAR RCSB PDB	4X62	Q5SLQ0	615.6 Da LogP -8.86 TPSA 347.3	3 viol.	✓ Clean	`C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…`
SRY RCSB PDB	6RW4	Q9Y3D5	581.6 Da LogP -7.74 TPSA 331.4	3 viol.	✓ Clean	`[H]/N=C(/N)\N[C@@H]1[C@H]([C@@H]([C@H]([C@@H]([…`
TAC RCSB PDB	1I97	Q5SLQ0	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`C[C@]1(c2cccc(c2C(=O)C3=C([C@]4([C@@H](C[C@@H]3…`
WO2 RCSB PDB	1I94	Q5SLQ0	—	—	—	`[O][W]1234O[W]567(O[W]89%10(O5[P]5%11O%12[W]%13…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
08D ChEMBL	P0A7T7	—	253.3 Da LogP 1.37 TPSA 98.2	✓ Ro5	✓ Clean	`Cc1cc(no1)NS(=O)(=O)c2ccc(cc2)N`
4AX ChEMBL	P0A7T7	—	102.1 Da LogP -1.62 TPSA 64.3	✓ Ro5	✓ Clean	`C1[C@H](C(=O)NO1)N`
SCM ChEMBL	P0A7T7	—	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`C[C@@H]1CC(=O)[C@]2([C@@H](O1)O[C@@H]3[C@H]([C@…`
TOP ChEMBL	P0A7T7	—	290.3 Da LogP 1.26 TPSA 105.5	✓ Ro5	✓ Clean	`COc1cc(cc(c1OC)OC)Cc2cnc(nc2N)N`

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
ZINC11525121 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC18202167 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC20410403 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC21984166 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC239173596 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC245256945 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@H…`
ZINC245256946 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@@H]2O[C@]3(O)C(=O)C[C@H](C)O[C@@H]3…`
ZINC245256947 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@@H]2O[C@]3(O)C(=O)C[C@H](C)O[C@@H]3…`
ZINC245256948 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@H](O)[C@H]2O[C@H]…`
ZINC4059755 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4215819 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3C…`
ZINC43771554 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4807269 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC5273778 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@@H](O)[C@@H]2O[C@H]3O[C@@H](C)CC(=O…`
ZINC53006806 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@H](O)[C@H]2O[C@@H…`
ZINC57406608 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@@…`
ZINC57406609 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@@…`
ZINC57406610 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@@…`
ZINC57406611 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@@…`
ZINC575338663 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…`
ZINC6627681 ZINC	1.000	290.3 Da LogP 1.26 TPSA 105.5	✓ Ro5	✓ Clean	`COc1cc(Cc2cnc(N)nc2N)cc(OC)c1OC`
ZINC71789713 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@H](O)[C@H]2O[C@@H]3O[C@@H](C)CC(=O)…`
ZINC71789714 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@H](O)[C@H]2O[C@H]3O[C@@H](C)CC(=O)[…`
ZINC71789715 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@H](O)[C@H]2O[C@@H]3O[C@@H](C)CC(=O)…`
ZINC71789716 ZINC	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@H](O)[C@H]2O[C@H]3O[C@@H](C)CC(=O)[…`
ZINC84441937 ZINC	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC89763 ZINC	1.000	253.3 Da LogP 1.37 TPSA 98.2	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2ccc(N)cc2)no1`
ZINC100052153 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC100223147 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@@H](O[C@@H]2[C@@H](O[C@@H]3O[C@H](…`
ZINC103649633 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC242575106 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575107 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575108 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575109 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC43664294 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664297 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664300 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664303 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC53255716 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC56874669 ZINC	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC77270915 ZINC	0.889	408.5 Da LogP 2.17 TPSA 144.4	✓ Ro5	✓ Clean	`Cc1cc(NS(=O)(=O)c2ccc(NS(=O)(=O)c3ccc(N)cc3)cc2…`
ZINC104869865 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC33494315 ZINC	0.825	339.2 Da LogP 2.01 TPSA 96.3	✓ Ro5	✓ Clean	`COc1cc(Cc2cnc(N)nc2N)cc(Br)c1OC`
ZINC28006201 ZINC	0.821	304.4 Da LogP 1.65 TPSA 105.5	✓ Ro5	✓ Clean	`CCOc1c(OC)cc(Cc2cnc(N)nc2N)cc1OC`

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 A0A0H3GHD3

Chemistry

ChEMBL 08D ChEMBL 4AX ChEMBL SCM ChEMBL TOP