Protein target profile

VK055_0098

ribosomal RNA small subunit methyltransferase F

Genome: KpATCC43816 Gene: AIK78726.1 rsmF 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GQ38

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Length 462

Pocket druggability 0.477

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 9 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 isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.48. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.55. 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: Hit
Human identity (%): 39.205 Lower values reduce human off-target concern.
Human E-value: 6.19e-26
Gut microbiome similarity: 1.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 32.42 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 94.54 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.477

Structure A0A0H3GQ38

Pocket Pocket 9

P2Rank 0.551

Structure A0A0H3GQ38

Pocket Pocket 1

ColabFold model

FPocket 0.548 · Pocket 1

P2Rank 0.301 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 88 / 4744 genomes with a hit

Prevalence 1.9%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Metabolic context

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

Explore metabolic network

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MRAAMPAHLSFDDFIAACQRPLRRSIRVNTLKIGVDDFLSLVAPYGWQLAPVPWCAEGFWIEREDDDALPLGSTAEHLSGLFYIQEASSMLPVAALFADNRQPERVMDVAAAPGSKTTQIAARMGNAGGILANEFSASRVKVLHANISRCGISNVALTHFDGRVFGAALPETFDAILLDAPCSGEGVVRKDADALKNWSPESNLDIAATQRELIDSAFHALRPGGTLVYSTCTLNREENQSVIEWLLSRYPQAVEILPLGELFPGAADALTAEGFLHVFPQIYDCEGFFVARLRKTAAIDPLPAPGYKVGKFPFTPLKDREAAAVTAAARAVGLEWDAGHTLWQRDKELWLFPLALEPLFGKVRFSRIGVRLAELHNKGYRWQHEAVIAFAAPQRAFELSQEEAEEWYRGRDVYPQTAPGQDETIVTFQGVPLGLAKRVGSRLKNSYPRELVRDGKLFAGKV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

2.1.1.178

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:0008649 Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a nucleoside residue in an rRNA molecule. The methyl group can be transfered to the nucleobase or to the ribose group of the nucleoside.
GO:0001510 Posttranscriptional addition of a methyl group to either a nucleotide or 2'-O ribose in a polyribonucleotide. Usually uses S-adenosylmethionine as a cofactor.
GO:0008757 Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate.
GO:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
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:0009383 Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to cytosine to form 5-methylcytosine in small subunit ribosomal RNA.
GO:0070475 The addition of a methyl group to an atom in the nucleoside base portion of a nucleotide residue in an rRNA molecule.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
14	296	ProSiteProfiles	PS51686	SAM-dependent MTase RsmB/NOP-type domain profile.
14	296	InterPro	IPR001678	SAM-dependent methyltransferase RsmB/NOP2-type
105	230	CDD	cd02440	AdoMet_MTases
26	295	NCBIfam	TIGR00446	NOL1/NOP2/sun family putative RNA methylase
26	295	InterPro	IPR011023	Nop2p
1	458	Hamap	MF_01579	Ribosomal RNA small subunit methyltransferase F [rsmF].
1	458	InterPro	IPR023545	rRNA small subunit methyltransferase F
296	462	Gene3D	G3DSA:3.10.450.720	-
173	184	ProSitePatterns	PS01153	NOL1/NOP2/sun family signature.
173	184	InterPro	IPR018314	Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p, conserved site
107	117	PRINTS	PR02008	RNA (C5-cytosine) methyltransferase signature
107	117	InterPro	IPR023267	RNA (C5-cytosine) methyltransferase
76	90	PRINTS	PR02008	RNA (C5-cytosine) methyltransferase signature
76	90	InterPro	IPR023267	RNA (C5-cytosine) methyltransferase
174	186	PRINTS	PR02008	RNA (C5-cytosine) methyltransferase signature
174	186	InterPro	IPR023267	RNA (C5-cytosine) methyltransferase
278	295	PRINTS	PR02008	RNA (C5-cytosine) methyltransferase signature
278	295	InterPro	IPR023267	RNA (C5-cytosine) methyltransferase
224	240	PRINTS	PR02008	RNA (C5-cytosine) methyltransferase signature
224	240	InterPro	IPR023267	RNA (C5-cytosine) methyltransferase
6	297	PANTHER	PTHR22807	NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING
6	297	InterPro	IPR023267	RNA (C5-cytosine) methyltransferase
404	453	Pfam	PF13636	RNA-binding PUA-like domain of methyltransferase RsmF
404	453	InterPro	IPR027391	rRNA small subunit methyltransferase F, RNA-binding PUA-like domain
1	295	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
1	295	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1	90	Pfam	PF17125	N-terminal domain of 16S rRNA methyltransferase RsmF
1	90	InterPro	IPR031341	Ribosomal RNA small subunit methyltransferase F, N-terminal
10	295	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
10	295	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1	295	FunFam	G3DSA:3.40.50.150:FF:000079	Ribosomal RNA small subunit methyltransferase F
296	462	FunFam	G3DSA:3.10.450.720:FF:000001	Ribosomal RNA small subunit methyltransferase F
100	294	Pfam	PF01189	16S rRNA methyltransferase RsmB/F
100	294	InterPro	IPR001678	SAM-dependent methyltransferase RsmB/NOP2-type

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: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #9

0.477

Likely same site as P2Rank 2 2.3 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #7

0.323

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.551

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Surrounding area

Site 2 P2Rank #2

0.129

Likely same site as FPocket 9 2.3 Å 11 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.114

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Surrounding area

Site 4 P2Rank #4

0.065

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Surrounding area

Site 5 P2Rank #5

0.04

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Surrounding area

Residue sets

UniProt: Active site:247-247 Nucleophile

UniProt: Binding site:125-131

UniProt: Binding site:149-149

UniProt: Binding site:176-176

UniProt: Binding site:194-194

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.301

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Surrounding area

Site 2 P2Rank #2

0.161

Likely same site as FPocket 13 2.2 Å 10 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.095

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Surrounding area

Site 4 P2Rank #4

0.031

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Surrounding area

Site 5 P2Rank #5

0.031

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Surrounding area

Residue sets

UniProt: Active site:247-247 Nucleophile

UniProt: Binding site:125-131

UniProt: Binding site:149-149

UniProt: Binding site:176-176

UniProt: Binding site:194-194

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_A0A0H3GQ38	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0098	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 and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 1 0 loaded crystals

Measured bioactivity 4 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

SFG PDB via homolog 381.4 Da · LogP -2.06 · TPSA 208.7 Open detail RCSB PDB

DXH ChEMBL via homolog · pchembl 9.69 (~0.2 nM) Detail ChEMBL

DWT ChEMBL via homolog · pchembl 6.44 (~363.1 nM) Detail ChEMBL

CHEMBL5565987 ChEMBL via homolog Detail ChEMBL

CHEMBL5566600 ChEMBL via homolog Detail ChEMBL

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
SFG RCSB PDB	5ZVH	O57712	381.4 Da LogP -2.06 TPSA 208.7	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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
DXH ChEMBL	P46087	9.69 ~0.2 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cnn(c3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
DWT ChEMBL	P46087	6.44 ~363.1 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
CHEMBL5565987 ChEMBL	Q9H649	—	327.3 Da LogP 2.76 TPSA 110.9	✓ Ro5	✓ Clean	`O=C(Nc1ncc([N+](=O)[O-])s1)c1cccc(-c2ccccn2)n1`
CHEMBL5566600 ChEMBL	Q9H649	—	312.4 Da LogP 2.34 TPSA 88.0	✓ Ro5	✓ Clean	`O=C(Nc1nc(CO)cs1)c1cccc(-c2ccccn2)n1`

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
ZINC13650200 ZINC	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@H](N)…`
ZINC205994753 ZINC	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@H](N)…`
ZINC205994774 ZINC	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@H](N)…`
ZINC27723577 ZINC	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@H](N)…`
ZINC38192471 ZINC	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@H](N)CC[C@@H](N…`
ZINC38192472 ZINC	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@@H](N)CC[C@@H](…`
ZINC4217451 ZINC	1.000	381.4 Da LogP -2.06 TPSA 208.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[C@@H](N)CC[C@H](N…`
ZINC13522400 ZINC	0.737	400.4 Da LogP -2.42 TPSA 199.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[S@](=O)CC[C@H](N)…`
ZINC13522403 ZINC	0.737	400.4 Da LogP -2.42 TPSA 199.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C[S@@](=O)CC[C@H](N…`
ZINC13522378 ZINC	0.732	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC13522407 ZINC	0.732	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC256828117 ZINC	0.732	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC256828118 ZINC	0.732	370.4 Da LogP -1.83 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSC[C@H](N)C(=O)O)[…`
ZINC1775937521 ZINC	0.726	423.5 Da LogP -1.02 TPSA 194.7	2 viol.	✓ Clean	`CCCN[C@H](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc…`
ZINC95921230 ZINC	0.726	423.5 Da LogP -1.02 TPSA 194.7	2 viol.	✓ Clean	`CCCN[C@@H](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cn…`
ZINC12501055 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC13509082 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CSCC[C@@H](N)C(=O)O…`
ZINC13509104 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@@H](N)C(=O)O…`
ZINC1532516 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CSCC[C@H](N)C(=O)O)…`
ZINC33821012 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC33821013 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC4228232 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CSCC[C@H](N)C(=O)O)…`
ZINC45789230 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CSCC[C@H](N)C(=O)O…`
ZINC45789233 ZINC	0.724	384.4 Da LogP -1.44 TPSA 182.6	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CSCC[C@H](N)C(=O)O)[…`
ZINC49014951 ZINC	0.724	416.4 Da LogP -2.76 TPSA 216.8	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CS(=O)(=O)CC[C@H](N)…`
ZINC49014955 ZINC	0.724	416.4 Da LogP -2.76 TPSA 216.8	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CS(=O)(=O)CC[C@@H](N…`
ZINC100005972 ZINC	0.712	400.5 Da LogP -1.54 TPSA 182.6	1 viol.	✓ Clean	`C[S@@H](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC12371977 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC12371978 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`
ZINC13522357 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3…`
ZINC13522362 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC139339614 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3c…`
ZINC254297245 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3c(…`
ZINC254297254 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3c(…`
ZINC254297257 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3c(…`
ZINC33821030 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC33821031 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`
ZINC4214738 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC4228231 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`
ZINC71755544 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3c…`
ZINC71755557 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@@H](N)C(=O)O)C[C@@H]1O[C@H](n2cnc3…`
ZINC95644663 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
ZINC95644664 ZINC	0.700	399.5 Da LogP -1.92 TPSA 182.6	✓ Ro5	✓ Clean	`C[S@+](CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`
ZINC12523323 ZINC	0.674	282.3 Da LogP 2.85 TPSA 67.8	✓ Ro5	✓ Clean	`O=C(Nc1nc(-c2ccccn2)cs1)c1ccccn1`
ZINC5139067 ZINC	0.654	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CS)[C@@H](O)[C@H]1O`
ZINC4513750 ZINC	0.648	281.2 Da LogP -1.89 TPSA 156.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](C(=O)O)[C@@H](O)[C@…`
ZINC4513754 ZINC	0.648	281.2 Da LogP -1.89 TPSA 156.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](C(=O)O)[C@@H](O)[C…`
ZINC4513757 ZINC	0.648	281.2 Da LogP -1.89 TPSA 156.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](C(=O)O)[C@@H](O)[C@…`
ZINC4513760 ZINC	0.648	281.2 Da LogP -1.89 TPSA 156.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](C(=O)O)[C@@H](O)[C…`
ZINC5163034 ZINC	0.648	281.2 Da LogP -1.89 TPSA 156.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](C(=O)O)[C@@H](O)[C@…`

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.

VK055_0098

Promising target candidate with multiple supporting evidence streams.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Chemistry

Pathways

Metabolic context

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence