Protein target profile

VK055_0016

cytosine-specific methyltransferase

Genome: KpATCC43816 Gene: dcm AIK78647.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GV12

Export view

Length 464

Pocket druggability 0.205

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 67 total records

Functional annotation 1 EC 6 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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.58. 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: Hit
Human identity (%): 25.967 Lower values reduce human off-target concern.
Human E-value: 1.71e-06
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 78.043 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 92.28 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 0.205

Structure A0A0H3GV12

Pocket Pocket 22

P2Rank 0.578

Structure A0A0H3GV12

Pocket Pocket 1

ColabFold model

FPocket 0.605 · Pocket 6

P2Rank 0.613 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 107 / 4744 genomes with a hit

Prevalence 2.3%

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.

MAEQAGEDAEALLRQLMTIYDVKTLVAELVSVSEQHWSAAILKRVAALGRAAERLRPQEVAHLATLLPSPPAHHPHYGFRFIDLFAGIGGIRSGFEAIGGQCVFTSEWNKHAVRTYKANWYCDPQQHRFNEDIRDITLSQRSDVSDEEAARHIRESIPQHDVLLAGFPCQPFSLAGVSKKNAMGRAHGFACETQGTLFFDVVRIIAARQPAIFVLENVKNLKSHDQGRTFRIIMQTLDELGYEVADAGHTGPDDPKVIDGRHFLPQHRERIVLVGFRRDLQLHAGFTLRDIAAQYPAVRPTFGELLEPTVDAKFILTPVLWKYLYRYARKHQARGNGFGYGLVDPANPHSVARTLSARYYKDGAEILVDRGWDRPLGEMHFDDPLNQQRRPRRLTPRECARLMGFESPQGARFRIPVSDTQAYRQFGNSVVVPVFAAVAKLLAPRIAQAVARREADDNDGGCSR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

2.1.1.37

Gene Ontology (GO)

GO:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
GO:0003886 Catalysis of the reaction: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H+ + S-adenosyl-L-homocysteine.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0009307 A defense process found in many bacteria and archaea that protects the organism from invading foreign DNA by cleaving it with a restriction endonuclease. The organism's own DNA is protected by methylation of a specific nucleotide, which occurs immediately following replication, in the same target site as the restriction enzyme.
GO:0032259 The process in which a methyl group is covalently attached to a molecule.
GO:0044027 An epigenetic gene regulation mechanism that negatively regulates gene expression by methylation of cytosine residues in chromosomal CpG islands. CpG islands are genomic regions that contain a high frequency of the CG dinucleotide associated with the transcription start site of genes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
7	75	Gene3D	G3DSA:1.10.260.140	-
424	442	ProSitePatterns	PS00095	C-5 cytosine-specific DNA methylases C-terminal signature.
424	442	InterPro	IPR031303	DNA methylase, C-5 cytosine-specific, conserved site
79	443	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
79	443	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
297	411	Gene3D	G3DSA:3.90.120.30	-
263	276	PRINTS	PR00105	Cytosine-specific DNA methyltransferase signature
263	276	InterPro	IPR001525	C-5 cytosine methyltransferase
80	96	PRINTS	PR00105	Cytosine-specific DNA methyltransferase signature
80	96	InterPro	IPR001525	C-5 cytosine methyltransferase
209	223	PRINTS	PR00105	Cytosine-specific DNA methyltransferase signature
209	223	InterPro	IPR001525	C-5 cytosine methyltransferase
11	67	Pfam	PF18284	DNA methylase N-terminal domain
11	67	InterPro	IPR040743	DNA methylase N-terminal domain
79	429	CDD	cd00315	Cyt_C5_DNA_methylase
380	454	PANTHER	PTHR10629	CYTOSINE-SPECIFIC METHYLTRANSFERASE
79	440	Pfam	PF00145	C-5 cytosine-specific DNA methylase
79	440	InterPro	IPR001525	C-5 cytosine methyltransferase
79	449	ProSiteProfiles	PS51679	C-5 cytosine-specific DNA methylase (Dnmt) domain profile.
79	449	InterPro	IPR001525	C-5 cytosine methyltransferase
81	442	NCBIfam	TIGR00675	DNA (cytosine-5-)-methyltransferase
81	442	InterPro	IPR001525	C-5 cytosine methyltransferase
161	173	ProSitePatterns	PS00094	C-5 cytosine-specific DNA methylases active site.
161	173	InterPro	IPR018117	DNA methylase, C-5 cytosine-specific, active site
76	295	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
76	295	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily

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 · FPocket

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

Site 1 FPocket #22

0.205

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.578

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.053

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.049

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.045

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.045

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:171-171

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.613

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.085

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.08

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.045

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.037

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_A0A0H3GV12	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0016	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.

67 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 17 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 14 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

DCZ PDB via homolog 227.2 Da · LogP -1.53 · TPSA 110.6 Open detail RCSB PDB

SFG PDB via homolog Detail RCSB PDB

X52 PDB via homolog Detail RCSB PDB

AW1 ChEMBL via homolog · pchembl 8.54 (~2.9 nM) Detail ChEMBL

CHEMBL1201129 ChEMBL via homolog · pchembl 7.52 (~30.2 nM) 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
DCZ RCSB PDB	2Z6Q	P05102	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO)O`
SFG RCSB PDB	3SWR	P26358	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)…`
X52 RCSB PDB	6X9J	P26358	472.6 Da LogP 2.73 TPSA 113.1	✓ Ro5	✓ Clean	`CCc1c(c(nc(c1C#N)SCc2ccc(cc2)N(C)S(=O)(=O)C)N(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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
AW1 ChEMBL	P26358	8.54 ~2.9 nM	540.7 Da LogP 2.25 TPSA 163.7	1 viol.	✓ Clean	`CC(C)[N@](CCCNC(=O)Nc1ccc(cc1)C(C)(C)C)C[C@@H]2…`
CHEMBL1201129 ChEMBL	P26358	7.52 ~30.2 nM	228.2 Da LogP -2.14 TPSA 123.5	✓ Ro5	✓ Clean	`Nc1ncn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)n1`
UXM ChEMBL	P26358	7.40 ~39.8 nM	420.5 Da LogP 2.63 TPSA 132.8	✓ Ro5	✓ Clean	`CCc1c(c(nc(c1C#N)SC(c2ccccc2)C(=O)N)N3CCC(CC3)N…`
CHEMBL4588797 ChEMBL	P26358	6.82 ~151.4 nM	408.4 Da LogP -0.96 TPSA 193.5	1 viol.	✓ Clean	`N#Cc1cn([C@@H]2O[C@H](CSCC[C@H](N)C(=O)O)[C@@H]…`
CHEMBL5723367 ChEMBL	P26358	6.64 ~229.1 nM	365.5 Da LogP 2.77 TPSA 106.8	✓ Ro5	✓ Clean	`CCc1c(C#N)c(S[C@@H](C(N)=O)c2ccccc2)nc(N(C)C)c1…`
5AE ChEMBL	P26358	6.52 ~302.0 nM	244.2 Da LogP -3.17 TPSA 143.7	✓ Ro5	✓ Clean	`C1=NC(=NC(=O)N1[C@H]2[C@@H]([C@@H]([C@H](O2)CO)…`
CHEMBL5187655 ChEMBL	P26358	6.40 ~398.1 nM	505.5 Da LogP -3.40 TPSA 241.9	3 viol.	✓ Clean	`Nc1nc(=O)n([C@H]2C[C@H](O)[C@@H](CO)O2)cc1CNC[C…`
CHEMBL5612510 ChEMBL	P26358	6.12 ~758.6 nM	609.8 Da LogP 4.23 TPSA 168.2	1 viol.	✓ Clean	`CCc1c(C#N)c(S[C@@H](C(N)=O)c2ccccc2)nc(N2CCC(CN…`
CHEMBL560106 ChEMBL	P26358	6.09 ~812.8 nM	430.9 Da LogP -0.77 TPSA 168.6	1 viol.	✓ Clean	`Nc1nc(Cl)nc2c1ncn2[C@@H]1O[C@H](CS[C@@H]2CN[C@H…`
CHEMBL5189142 ChEMBL	P26358	6.05 ~891.3 nM	550.6 Da LogP -1.48 TPSA 229.9	3 viol.	✓ Clean	`Nc1nc(=O)n([C@H]2C[C@H](O)[C@@H](CO)O2)cc1CSCCC…`
SX0 ChEMBL	P26358	6.02 ~955.0 nM	462.3 Da LogP -0.07 TPSA 169.7	✓ Ro5	✓ Clean	`c1c(c2c(ncnc2n1[C@H]3[C@@H]([C@@H]([C@H](O3)CSC…`
CHEMBL2001850 ChEMBL	P26358	—	228.2 Da LogP -2.14 TPSA 123.5	✓ Ro5	✓ Clean	`Nc1ncn(C2C[C@H](O)[C@@H](CO)O2)c(=O)n1`
CHEMBL2063061 ChEMBL	P26358	—	331.4 Da LogP 0.80 TPSA 96.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)nc1NCc1c…`
CHEMBL418052 ChEMBL	P13864	—	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)…`

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
ZINC11612315 ZINC	1.000	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)n1`
ZINC12501055 ZINC	1.000	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	1.000	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	1.000	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	1.000	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)…`
ZINC18286010 ZINC	1.000	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](CO)O2)c(=O)n1`
ZINC18286013 ZINC	1.000	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)n1`
ZINC1857524021 ZINC	1.000	365.5 Da LogP 2.77 TPSA 106.8	✓ Ro5	✓ Clean	`CCc1c(C#N)c(S[C@@H](C(N)=O)c2ccccc2)nc(N(C)C)c1…`
ZINC1857792959 ZINC	1.000	365.5 Da LogP 2.77 TPSA 106.8	✓ Ro5	✓ Clean	`CCc1c(C#N)c(S[C@H](C(N)=O)c2ccccc2)nc(N(C)C)c1C…`
ZINC2114745131 ZINC	1.000	420.5 Da LogP 2.63 TPSA 132.8	✓ Ro5	✓ Clean	`CCc1c(C#N)c(S[C@H](C(N)=O)c2ccccc2)nc(N2CCC(N)C…`
ZINC2114745132 ZINC	1.000	420.5 Da LogP 2.63 TPSA 132.8	✓ Ro5	✓ Clean	`CCc1c(C#N)c(S[C@@H](C(N)=O)c2ccccc2)nc(N2CCC(N)…`
ZINC33821012 ZINC	1.000	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	1.000	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)…`
ZINC3869837 ZINC	1.000	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@H](CO)O2)c(=O)n1`
ZINC3869838 ZINC	1.000	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@H](CO)O2)c(=O)n1`
ZINC4228232 ZINC	1.000	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)…`
ZINC4253 ZINC	1.000	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@H](CO)O2)c(=O)n1`
ZINC45789230 ZINC	1.000	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	1.000	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)[…`
ZINC5239365 ZINC	1.000	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)n1`
ZINC57290 ZINC	1.000	227.2 Da LogP -1.53 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO)O2)c(=O)n1`
ZINC13522378 ZINC	0.833	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	0.833	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	0.833	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	0.833	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)[…`
ZINC34235488 ZINC	0.810	226.2 Da LogP -1.57 TPSA 116.4	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2ccc(N)nc2=O)C[C@@H]1O`
ZINC2004224 ZINC	0.791	226.2 Da LogP -1.57 TPSA 116.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](N)[C@H](CO)O2)c(=O)n1`
ZINC5551931 ZINC	0.791	226.2 Da LogP -1.57 TPSA 116.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](N)[C@H](CO)O2)c(=O)n1`
ZINC5551934 ZINC	0.791	226.2 Da LogP -1.57 TPSA 116.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](N)[C@H](CO)O2)c(=O)n1`
ZINC5551938 ZINC	0.791	226.2 Da LogP -1.57 TPSA 116.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](N)[C@H](CO)O2)c(=O)n1`
ZINC5784279 ZINC	0.791	226.2 Da LogP -1.57 TPSA 116.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](N)[C@@H](CO)O2)c(=O)n1`
ZINC5765920 ZINC	0.773	229.2 Da LogP -0.56 TPSA 90.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](F)[C@H](CO)O2)c(=O)n1`
ZINC5765921 ZINC	0.773	229.2 Da LogP -0.56 TPSA 90.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](F)[C@H](CO)O2)c(=O)n1`
ZINC19867703 ZINC	0.755	337.4 Da LogP 2.29 TPSA 129.6	✓ Ro5	✓ Clean	`CCc1c(C#N)c(N)nc(S[C@@H](C(N)=O)c2ccccc2)c1C#N`
ZINC19867707 ZINC	0.755	337.4 Da LogP 2.29 TPSA 129.6	✓ Ro5	✓ Clean	`CCc1c(C#N)c(N)nc(S[C@H](C(N)=O)c2ccccc2)c1C#N`
ZINC43771806 ZINC	0.727	243.3 Da LogP -0.16 TPSA 93.5	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=S)n1`
ZINC43771808 ZINC	0.727	243.3 Da LogP -0.16 TPSA 93.5	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=S)n1`
ZINC13650200 ZINC	0.724	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	0.724	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	0.724	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	0.724	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	0.724	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	0.724	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	0.724	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…`
ZINC12503923 ZINC	0.723	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC12503924 ZINC	0.723	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532581 ZINC	0.723	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC3645374 ZINC	0.723	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC3869816 ZINC	0.723	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869817 ZINC	0.723	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`

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_0016

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