KpATCC43816 Protein target profile

ribonucleoside hydrolase 1

Accession: VK055_0569

Gene: AIK79192.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 6 reactions UniProt A0A0H3GTH3

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Length 311

Pocket druggability (P2Rank · AlphaFold DB model) 0.842

Metabolic reactions 6

Chokepoint No

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 7 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Central metabolic position More central than 97.6% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. 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. 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: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 42.395 Higher values support similarity to known essential genes.
DEG E-value: 3.89e-67 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.75 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) 0.842

Structure A0A0H3GTH3

Pocket Pocket 1

Druggability (FPocket) 0.662

Structure A0A0H3GTH3

Pocket Pocket 1

ColabFold model

P2Rank 0.857 · Pocket 1

FPocket 0.771 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 143 / 4744 genomes with a hit

Prevalence 3.0%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: more central than 97.6% of genes in this genome, no human homolog detected.

Relative network centrality 97.6% more central than 97.6% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MALPIMIDCDPGHDDAIALVLALASPELEVKAVTASAGNQTPEKTLRNVLRMLTLLNRPDIPVAGGAWKPLMRDLIIADNVHGESGLDGPSLPEPAFAPQNCTAVELMASVLRESQEPVTLVATGPQTNVALLLASHPELHAKIARIVIMGGAMGLGNWQPAAEFNIYVDPQAAEMVFQSGIPVVMAGLDVTHRAQILPADIERFRQIGNPVSTIVAELLDFFMAYHKDEKWGFDGAPLHDPCTIAWLLKPEIFTTIERWVGVETEGKYTQGMTVVDYYHLTGNRPNTTLMLDVDREAFVDLLAQRLAFYA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Unknown

Enzyme Commission (EC)

3.2.-.-

Gene Ontology (GO)

GO:0045437 Catalysis of the reaction: H2O + uridine = ribofuranose + uracil.
GO:0016799 Catalysis of the hydrolysis of any N-glycosyl bond.
GO:0015949 The chemical reactions and pathways by which a nucleobase, nucleoside or nucleotide small molecule is synthesized from another nucleobase, nucleoside or nucleotide small molecule.
GO:0006206 The chemical reactions and pathways involving pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0008477 Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
GO:0006152 The chemical reactions and pathways resulting in the breakdown of purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

14 records

Show feature table

Start	End	DB	Term	Name
8	18	ProSitePatterns	PS01247	Inosine-uridine preferring nucleoside hydrolase family signature.
8	18	InterPro	IPR015910	Inosine/uridine-preferring nucleoside hydrolase, conserved site
1	311	Gene3D	G3DSA:3.90.245.10	-
1	311	InterPro	IPR036452	Ribonucleoside hydrolase-like
4	307	SUPERFAMILY	SSF53590	Nucleoside hydrolase
4	307	InterPro	IPR036452	Ribonucleoside hydrolase-like
5	301	Pfam	PF01156	Inosine-uridine preferring nucleoside hydrolase
5	301	InterPro	IPR001910	Inosine/uridine-preferring nucleoside hydrolase domain
5	308	PANTHER	PTHR12304	INOSINE-URIDINE PREFERRING NUCLEOSIDE HYDROLASE
5	308	InterPro	IPR023186	Inosine/uridine-preferring nucleoside hydrolase
4	307	CDD	cd02651	nuc_hydro_IU_UC_XIUA
1	311	Hamap	MF_01431	Pyrimidine-specific ribonucleoside hydrolase RihA [rihA].
1	311	InterPro	IPR022975	Pyrimidine-specific ribonucleoside hydrolase RihA
1	311	FunFam	G3DSA:3.90.245.10:FF:000001	Pyrimidine-specific ribonucleoside hydrolase RihA

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

0.842

Likely same site as FPocket 1 1.6 Å 16 shared residues 89% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.002

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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 #1

0.662

Likely same site as P2Rank 1 1.6 Å 16 shared residues 89% of smaller site

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Surrounding area

Pocket 2 FPocket #2

0.44

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Surrounding area

Residue sets

UniProt: Active site:240-240

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_A0A0H3GTH3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0569	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.

57 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ADE PDB via homolog 135.1 Da · LogP -0.06 · TPSA 80.5 Open detail RCSB PDB

DNB PDB via homolog Detail RCSB PDB

IMH PDB via homolog Detail RCSB PDB

NOS PDB via homolog Detail RCSB PDB

PIR 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
ADE RCSB PDB	6ZK4	B6THD4	135.1 Da LogP -0.06 TPSA 80.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(ncn2)N`
DNB RCSB PDB	3MKN	C3T3U2	239.3 Da LogP -1.42 TPSA 124.8	1 viol.	✓ Clean	`c1cc(c(cc1[C@H]2[C@@H]([C@@H]([C@H](N2)CO)O)O)N…`
IMH RCSB PDB	6ZK2	B6THD4	266.3 Da LogP -2.02 TPSA 134.3	1 viol.	✓ Clean	`c1c(c2c([nH]1)C(=O)NC=N2)[C@H]3[C@@H]([C@@H]([C…`
NOS RCSB PDB	3B9X	P33022	268.2 Da LogP -2.27 TPSA 133.5	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO)O)O)N=…`
PIR RCSB PDB	2MAS	Q27546	224.3 Da LogP -1.00 TPSA 98.7	✓ Ro5	✓ Clean	`c1cc(ccc1[C@H]2[C@@H]([C@@H]([C@H](N2)CO)O)O)N`
TAM RCSB PDB	3B9X	P33022	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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
CHEMBL3827395 ChEMBL	Q27546	8.15 ~7.1 nM	265.3 Da LogP -2.09 TPSA 136.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1N=CC2[C@@H]1N[C@H](CO)[C@@H](O)[C@H]1O`

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
ZINC13492899 ZINC	1.000	266.3 Da LogP -2.02 TPSA 134.3	1 viol.	✓ Clean	`O=c1[nH]cnc2c([C@@H]3N[C@H](CO)[C@@H](O)[C@H]3O…`
ZINC104646465 ZINC	0.750	298.3 Da LogP -0.90 TPSA 113.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@H](O)[…`
ZINC104896921 ZINC	0.750	298.3 Da LogP -0.90 TPSA 113.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)…`
ZINC13508805 ZINC	0.750	298.3 Da LogP -0.90 TPSA 113.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O…`
ZINC13508807 ZINC	0.750	298.3 Da LogP -0.90 TPSA 113.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)…`
ZINC13508809 ZINC	0.750	298.3 Da LogP -0.90 TPSA 113.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)…`
ZINC225456440 ZINC	0.750	282.3 Da LogP -1.61 TPSA 122.5	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@H](O)[…`
ZINC230149202 ZINC	0.750	282.3 Da LogP -1.61 TPSA 122.5	✓ Ro5	✓ Clean	`COC[C@@H]1O[C@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)…`
ZINC28542039 ZINC	0.750	298.3 Da LogP -0.90 TPSA 113.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)…`
ZINC34328902 ZINC	0.750	298.3 Da LogP -0.90 TPSA 113.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O…`
ZINC8652317 ZINC	0.745	312.4 Da LogP -0.51 TPSA 113.3	✓ Ro5	✓ Clean	`CCS[C@@H]1[C@@H](O)[C@H](CO)O[C@@H]1n1cnc2c(=O)…`
ZINC16382907 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3c(=S)[nH]cnc32)[C@@H](O)[…`
ZINC16382910 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@H](n2cnc3c(=S)[nH]cnc32)[C@@H](O)[C…`
ZINC2158 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@H](n2cnc3c(=S)[nH]cnc32)[C@@H](O)[…`
ZINC3148526 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@H](n2cnc3c(=S)[nH]cnc32)[C@H](O)[C…`
ZINC4217548 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3c(=S)[nH]cnc32)[C@H](O)[C…`
ZINC5510729 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@H](n2cnc3c(=S)[nH]cnc32)[C@H](O)[C…`
ZINC5510732 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@H](n2cnc3c(=S)[nH]cnc32)[C@@H](O)[…`
ZINC5510735 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@@H](n2cnc3c(=S)[nH]cnc32)[C@H](O)[…`
ZINC5510738 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@@H](n2cnc3c(=S)[nH]cnc32)[C@@H](O)…`
ZINC65743212 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3c(=S)[nH]cnc32)[C@@H](O)[…`
ZINC80121649 ZINC	0.739	284.3 Da LogP -0.90 TPSA 116.4	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3c(=S)[nH]cnc32)[C@H](O)[C…`
ZINC14951284 ZINC	0.706	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC1532551 ZINC	0.706	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC16969369 ZINC	0.706	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC4228242 ZINC	0.706	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@…`
ZINC4353761 ZINC	0.706	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC8614392 ZINC	0.706	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC16926920 ZINC	0.702	282.3 Da LogP -1.88 TPSA 133.5	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)[…`
ZINC16926924 ZINC	0.702	282.3 Da LogP -1.88 TPSA 133.5	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)[C…`
ZINC4876777 ZINC	0.702	282.3 Da LogP -1.88 TPSA 133.5	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)[C…`
ZINC4876778 ZINC	0.702	282.3 Da LogP -1.88 TPSA 133.5	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](n2cnc3c(=O)[nH]cnc32)[C@@H](O)[…`
ZINC1532637 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c…`
ZINC1550030 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c…`
ZINC1570863 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(…`
ZINC1698205 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c…`
ZINC2020098 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(…`
ZINC3869967 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c…`
ZINC3869968 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)…`
ZINC3869969 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC3869970 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O…`
ZINC5605239 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c…`
ZINC6119283 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(…`
ZINC6585367 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC8613125 ZINC	0.694	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c…`
ZINC12655466 ZINC	0.686	308.3 Da LogP -0.47 TPSA 111.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2[C@H](O1)[C@@H](CO)O[C@H]2n1cnc2c(…`
ZINC15277561 ZINC	0.686	308.3 Da LogP -0.47 TPSA 111.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2[C@@H](CO)O[C@@H](n3cnc4c(=O)[nH]c…`
ZINC15277563 ZINC	0.686	308.3 Da LogP -0.47 TPSA 111.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2[C@H](CO)O[C@@H](n3cnc4c(=O)[nH]c…`
ZINC8892889 ZINC	0.686	308.3 Da LogP -0.47 TPSA 111.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2[C@H](CO)O[C@H](n3cnc4c(=O)[nH]cnc…`
ZINC8955192 ZINC	0.686	308.3 Da LogP -0.47 TPSA 111.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2[C@@H](CO)O[C@H](n3cnc4c(=O)[nH]cn…`

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.

ribonucleoside hydrolase 1

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways