KpATCC43816 Protein target profile

methylated-DNA-[]-cysteine S-methyltransferase family protein

Accession: VK055_0973

Gene: AIK79596.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GSX7

Export view

Length 171

Pocket druggability (P2Rank · AlphaFold DB model) 0.1

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 6 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

Central metabolic position More central than 89.4% of genes in this genome. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 3 structural and 0 bioactivity records.

Risks to review

Human similarity Top human hit identity: 52.381%. Microbiome similarity 81 of 4744 screened genomes (1.7%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.07. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.10.

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 (%): 52.381 Lower values reduce human off-target concern.
Human E-value: 1.3100000000000003e-21
Gut microbiome similarity: 1.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 51.456 Higher values support similarity to known essential genes.
DEG E-value: 3.58e-32 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.65 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) 0.1

Structure A0A0H3GSX7

Pocket Pocket 1

Druggability (FPocket) 0.069

Structure A0A0H3GSX7

Pocket Pocket 9

ColabFold model

P2Rank 0.015 · Pocket 1

FPocket 0.103 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 81 / 4744 genomes with a hit

Prevalence 1.7%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 89.4% of genes in this genome.

Relative network centrality 89.4% more central than 89.4% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLTLLQDKMDTPLGPLWVLCDEQFNLRAVEWDEHRDRMETLLDVHYRREGYQRVDCRNPGGLSSKLSDYFAGDLAIIETLPTATAGTSFQRQVWQALREIPCGQVMHYGQLAEALGRPGAARAVGAANGANPVSIVVPCHRVIGRNGTMTGYAGGVQRKEWLLRHEGYLLL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.1.1.63

Gene Ontology (GO)

GO:0003908 Catalysis of the reaction: DNA (containing 6-O-methylguanine) + (protein)-L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0006307 The repair of alkylation damage in DNA, e.g. the removal of a non-physiological alkyl group from a nucleobase. This is usually mediated by DNA alkyltransferases.
GO:0032259 The process in which a methyl group is covalently attached to a molecule.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
7	92	SUPERFAMILY	SSF53155	Methylated DNA-protein cysteine methyltransferase domain
7	92	InterPro	IPR036631	Methylated DNA-protein cysteine methyltransferase domain superfamily
89	167	CDD	cd06445	ATase
89	167	InterPro	IPR014048	Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding
81	168	Gene3D	G3DSA:1.10.10.10	-
81	168	InterPro	IPR036388	Winged helix-like DNA-binding domain superfamily
88	167	Pfam	PF01035	6-O-methylguanine DNA methyltransferase, DNA binding domain
88	167	InterPro	IPR014048	Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding
87	166	NCBIfam	TIGR00589	methylated-DNA--[protein]-cysteine S-methyltransferase
87	166	InterPro	IPR014048	Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding
86	169	SUPERFAMILY	SSF46767	Methylated DNA-protein cysteine methyltransferase, C-terminal domain
86	169	InterPro	IPR036217	Methylated DNA-protein cysteine methyltransferase, DNA binding domain
8	167	Hamap	MF_00772	Methylated-DNA--protein-cysteine methyltransferase [ogt].
8	167	InterPro	IPR023546	Methylated-DNA--protein-cysteine methyltransferase
4	168	PANTHER	PTHR10815	METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE
137	143	ProSitePatterns	PS00374	Methylated-DNA--protein-cysteine methyltransferase active site.
137	143	InterPro	IPR001497	Methylated-DNA-[protein]-cysteine S-methyltransferase, active site
85	168	FunFam	G3DSA:1.10.10.10:FF:000337	Methylated-DNA--protein-cysteine methyltransferase
4	83	Pfam	PF02870	6-O-methylguanine DNA methyltransferase, ribonuclease-like domain
4	83	InterPro	IPR008332	Methylguanine DNA methyltransferase, ribonuclease-like domain

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.1

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.009

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:139-139 Nucleophile; methyl group acceptor

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_A0A0H3GSX7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0973	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ETW PDB via homolog 479.5 Da · LogP 5.21 · TPSA 116.8 Open detail RCSB PDB

OGQ PDB via homolog Detail RCSB PDB

PBO PDB via homolog Detail RCSB PDB

ZINC100071118 ZINC proposed compound · Tanimoto 0.758 Detail ZINC

ZINC100071122 ZINC proposed compound · Tanimoto 0.758 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
ETW RCSB PDB	6GA0	Q97VW7	479.5 Da LogP 5.21 TPSA 116.8	1 viol.	✓ Clean	`Cc1ccc(cc1)CNC(=O)c2ccc(c(c2)C(=O)O)C3=C4C=CC(=…`
OGQ RCSB PDB	6Y8P	E5BBQ0	534.6 Da LogP 5.24 TPSA 85.8	2 viol.	✓ Clean	`Cc1ccc(cc1)CNC(=O)c2ccc(c(c2)C3=C4C=CC(=[N+](C)…`
PBO RCSB PDB	3GYH	Q9UTN9	149.2 Da LogP 2.06 TPSA 30.0	✓ Ro5	✓ Clean	`CCCC(=O)c1cccnc1`

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
ZINC100071118 ZINC	0.758	205.3 Da LogP 3.62 TPSA 30.0	✓ Ro5	✓ Clean	`CCCCCCCC(=O)c1cccnc1`
ZINC100071122 ZINC	0.758	219.3 Da LogP 4.01 TPSA 30.0	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)c1cccnc1`
ZINC22054134 ZINC	0.723	431.5 Da LogP 3.70 TPSA 94.0	✓ Ro5	✓ Clean	`CN(C)c1ccc2c(-c3cc(C(=O)O)ccc3C(=O)O)c3ccc(=[N+…`
ZINC5030658 ZINC	0.683	376.3 Da LogP 3.67 TPSA 125.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2c3ccc(=O)cc-3oc3cc(O)ccc23)c(C(=…`
ZINC28630842 ZINC	0.681	489.5 Da LogP 4.34 TPSA 154.1	✓ Ro5	✓ Clean	`O=C(O)CCCCCNC(=O)c1ccc(-c2c3ccc(=O)cc-3oc3cc(O)…`
ZINC100083979 ZINC	0.667	226.2 Da LogP 1.93 TPSA 59.9	✓ Ro5	✓ Clean	`O=C(CC(=O)c1cccnc1)c1cccnc1`
ZINC2379080 ZINC	0.667	207.2 Da LogP 1.61 TPSA 56.3	✓ Ro5	✓ Clean	`CCOC(=O)CCC(=O)c1cccnc1`
ZINC70915012 ZINC	0.647	203.2 Da LogP 2.61 TPSA 30.0	✓ Ro5	✓ Clean	`O=C(CCC(F)(F)F)c1cccnc1`
ZINC2379083 ZINC	0.632	221.3 Da LogP 2.00 TPSA 56.3	✓ Ro5	✓ Clean	`CCOC(=O)CCCC(=O)c1cccnc1`
ZINC34274984 ZINC	0.629	211.3 Da LogP 2.90 TPSA 30.0	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)c1cccnc1`
ZINC100077468 ZINC	0.625	225.2 Da LogP 2.54 TPSA 47.0	✓ Ro5	✓ Clean	`O=C(CC(=O)c1cccnc1)c1ccccc1`
ZINC169722656 ZINC	0.622	458.4 Da LogP 4.40 TPSA 165.6	✓ Ro5	Alert	`[N-]=[N+]=NCCCNC(=O)c1ccc(C(=O)O)c(-c2c3ccc(=O)…`
ZINC161862 ZINC	0.611	211.3 Da LogP 2.82 TPSA 30.0	✓ Ro5	✓ Clean	`Cc1ccc(CC(=O)c2cccnc2)cc1`
ZINC37992322 ZINC	0.611	211.3 Da LogP 2.82 TPSA 30.0	✓ Ro5	✓ Clean	`Cc1ccccc1CC(=O)c1cccnc1`
ZINC5248684 ZINC	0.594	376.3 Da LogP 3.67 TPSA 125.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)O)c(-c2c3ccc(=O)cc-3oc3cc(O)cc…`
ZINC6562820 ZINC	0.590	220.3 Da LogP 1.52 TPSA 50.3	✓ Ro5	✓ Clean	`CC(=O)N(C)CCCC(=O)c1cccnc1`
ZINC3872582 ZINC	0.587	332.3 Da LogP 3.97 TPSA 87.7	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1-c1c2ccc(=O)cc-2oc2cc(O)ccc12`
ZINC1592410 ZINC	0.586	212.2 Da LogP 1.54 TPSA 59.9	✓ Ro5	Alert	`O=C(C(=O)c1cccnc1)c1cccnc1`
ZINC100103222 ZINC	0.583	217.1 Da LogP 1.79 TPSA 47.0	✓ Ro5	✓ Clean	`O=C(CC(=O)C(F)(F)F)c1cccnc1`
ZINC394078 ZINC	0.583	206.3 Da LogP 2.34 TPSA 33.2	✓ Ro5	✓ Clean	`CCCN(CCC)C(=O)c1cccnc1`
ZINC4430794 ZINC	0.583	205.3 Da LogP 2.27 TPSA 47.0	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)CC(=O)c1cccnc1`
ZINC84193868 ZINC	0.583	213.2 Da LogP 2.21 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(Cc1ccc(O)cc1)c1cccnc1`
ZINC238651069 ZINC	0.579	208.2 Da LogP 0.46 TPSA 93.3	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)c1cccnc1)C(=O)O`
ZINC238665102 ZINC	0.579	208.2 Da LogP 0.46 TPSA 93.3	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)c1cccnc1)C(=O)O`
ZINC303011 ZINC	0.575	283.3 Da LogP 3.07 TPSA 71.1	✓ Ro5	✓ Clean	`CCCC(=O)Nc1ccc(NC(=O)c2cccnc2)cc1`
ZINC5239470 ZINC	0.575	207.2 Da LogP 1.66 TPSA 62.6	✓ Ro5	✓ Clean	`CN(CCCC(=O)c1cccnc1)N=O`
ZINC5030632 ZINC	0.571	332.3 Da LogP 3.97 TPSA 87.7	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2c3ccc(=O)cc-3oc3cc(O)ccc23)cc1`
ZINC100035725 ZINC	0.569	473.4 Da LogP 3.19 TPSA 151.4	✓ Ro5	✓ Clean	`O=C(ON1C(=O)CCC1=O)c1ccc(-c2c3ccc(=O)cc-3oc3cc(…`
ZINC25762071 ZINC	0.569	362.3 Da LogP 3.13 TPSA 139.8	✓ Ro5	✓ Clean	`Nc1cc(C(=O)O)c(-c2c3ccc(=O)cc-3oc3cc(O)ccc23)cc…`
ZINC100003502 ZINC	0.568	207.2 Da LogP 0.40 TPSA 73.3	✓ Ro5	✓ Clean	`COC(=O)C(=O)CC(=O)c1cccnc1`
ZINC37992319 ZINC	0.568	231.7 Da LogP 3.16 TPSA 30.0	✓ Ro5	✓ Clean	`O=C(Cc1ccc(Cl)cc1)c1cccnc1`
ZINC37992320 ZINC	0.568	215.2 Da LogP 2.65 TPSA 30.0	✓ Ro5	✓ Clean	`O=C(Cc1ccc(F)cc1)c1cccnc1`
ZINC37992321 ZINC	0.568	276.1 Da LogP 3.27 TPSA 30.0	✓ Ro5	✓ Clean	`O=C(Cc1ccc(Br)cc1)c1cccnc1`
ZINC100083975 ZINC	0.564	267.3 Da LogP 3.46 TPSA 47.0	✓ Ro5	✓ Clean	`Cc1cc(C)c(C(=O)CC(=O)c2cccnc2)c(C)c1`
ZINC100085501 ZINC	0.564	221.2 Da LogP 0.79 TPSA 73.3	✓ Ro5	✓ Clean	`CCOC(=O)C(=O)CC(=O)c1cccnc1`
ZINC37464014 ZINC	0.564	211.3 Da LogP 2.82 TPSA 30.0	✓ Ro5	✓ Clean	`Cc1cccc(CC(=O)c2cccnc2)c1`
ZINC38125314 ZINC	0.564	227.3 Da LogP 2.52 TPSA 39.2	✓ Ro5	✓ Clean	`COc1ccc(CC(=O)c2cccnc2)cc1`
ZINC22063503 ZINC	0.561	221.3 Da LogP 2.05 TPSA 62.6	✓ Ro5	✓ Clean	`CN(CCCCC(=O)c1cccnc1)N=O`
ZINC1667326 ZINC	0.553	384.4 Da LogP 1.90 TPSA 112.5	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](C(=O)c1cccnc1)[C@H](C(=O)OCC)C(=O…`
ZINC1667329 ZINC	0.553	384.4 Da LogP 1.90 TPSA 112.5	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](C(=O)c1cccnc1)[C@@H](C(=O)OCC)C(…`
ZINC17299137 ZINC	0.553	384.4 Da LogP 1.90 TPSA 112.5	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](C(=O)c1cccnc1)[C@@H](C(=O)OCC)C(=…`
ZINC2765515 ZINC	0.553	234.3 Da LogP 3.12 TPSA 33.2	✓ Ro5	✓ Clean	`CCCCN(CCCC)C(=O)c1cccnc1`
ZINC36941212 ZINC	0.553	225.3 Da LogP 3.27 TPSA 30.0	✓ Ro5	✓ Clean	`CCCc1ccc(C(=O)c2cccnc2)cc1`
ZINC380074941 ZINC	0.550	222.2 Da LogP 0.66 TPSA 88.9	✓ Ro5	✓ Clean	`COC(=O)C(CC(=O)c1cccnc1)=NO`
ZINC88616762 ZINC	0.550	222.2 Da LogP 0.66 TPSA 88.9	✓ Ro5	✓ Clean	`COC(=O)/C(CC(=O)c1cccnc1)=N/O`
ZINC575443691 ZINC	0.548	268.4 Da LogP 3.18 TPSA 33.2	✓ Ro5	✓ Clean	`CN(CCCC(=O)c1cccnc1)Cc1ccccc1`
ZINC584908924 ZINC	0.548	251.3 Da LogP 1.62 TPSA 65.5	✓ Ro5	✓ Clean	`COCCCOC(=O)CCC(=O)c1cccnc1`
ZINC45028802 ZINC	0.543	211.3 Da LogP 2.93 TPSA 30.0	✓ Ro5	✓ Clean	`Cc1cccc(C)c1C(=O)c1cccnc1`
ZINC25781561 ZINC	0.542	421.4 Da LogP 3.13 TPSA 137.8	✓ Ro5	✓ Clean	`NNC(=S)Nc1ccc(-c2c3ccc(=O)cc-3oc3cc(O)ccc23)c(C…`
ZINC22121726 ZINC	0.541	211.3 Da LogP 2.88 TPSA 30.0	✓ Ro5	✓ Clean	`CCc1ccc(C(=O)c2cccnc2)cc1`

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 A0A0H3GSX7

Pathways

KEGG R04314 BioCyc 2.1.1.63-RXN BioCyc RXN-17824