Protein profile

KP13_16605

Modification methylase EcoRII

Genome: KpKP13

Gene: ecoRIIM ANJ86658.1 Structure source: AlphaFold + ColabFold UniProt H6U1M2

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Amino acids 471

Annotations 7

Features 27

PDB binders 1

Druggability 0.11

Overview

Basic information about this protein and its source genome.

Accession: KP13_16605
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: ecoRIIM ANJ86658.1
Status: annotated
Amino acids: 471
Structure source: AlphaFold + ColabFold

2.1.1.37

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 23.81
Human E-value: 4.05e-07
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 67.793
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 92.35

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.11

Structure H6U1M2

Pocket Pocket 26

P2Rank 0.583

Structure H6U1M2

Pocket Pocket 1

ColabFold model

FPocket 0.19 · Pocket 34

P2Rank 0.512 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 101 / 4744 genomes with a hit

Normalized 0.021

Sequence

Primary amino-acid sequence viewer.

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 Features

Domain/signature hits from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
441	459	ProSitePatterns	PS00095	C-5 cytosine-specific DNA methylases C-terminal signature.
441	459	InterPro	IPR031303	DNA methylase, C-5 cytosine-specific, conserved site
96	459	CDD	cd00315	Cyt_C5_DNA_methylase
29	84	Pfam	PF18284	DNA methylase N-terminal domain
29	84	InterPro	IPR040743	DNA methylase N-terminal domain
96	459	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
96	459	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1	21	Coils	Coil	Coil
226	240	PRINTS	PR00105	Cytosine-specific DNA methyltransferase signature
226	240	InterPro	IPR001525	C-5 cytosine methyltransferase
280	293	PRINTS	PR00105	Cytosine-specific DNA methyltransferase signature
280	293	InterPro	IPR001525	C-5 cytosine methyltransferase
97	113	PRINTS	PR00105	Cytosine-specific DNA methyltransferase signature
97	113	InterPro	IPR001525	C-5 cytosine methyltransferase
26	92	Gene3D	G3DSA:1.10.260.140	-
407	458	PANTHER	PTHR10629	CYTOSINE-SPECIFIC METHYLTRANSFERASE
93	316	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
93	316	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
317	428	Gene3D	G3DSA:3.90.120.30	-
96	458	Pfam	PF00145	C-5 cytosine-specific DNA methylase
96	458	InterPro	IPR001525	C-5 cytosine methyltransferase
178	190	ProSitePatterns	PS00094	C-5 cytosine-specific DNA methylases active site.
178	190	InterPro	IPR018117	DNA methylase, C-5 cytosine-specific, active site
98	459	NCBIfam	TIGR00675	DNA (cytosine-5-)-methyltransferase
98	459	InterPro	IPR001525	C-5 cytosine methyltransferase
96	466	ProSiteProfiles	PS51679	C-5 cytosine-specific DNA methylase (Dnmt) domain profile.
96	466	InterPro	IPR001525	C-5 cytosine methyltransferase

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_H6U1M2	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_16605	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	5.48	0.261
2	2.68	0.08
3	2.08	0.047
4	2.04	0.045
5	1.46	0.02

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	3.49	0.127
2	3.21	0.11
3	1.94	0.04
4	1.49	0.021
5	1.0	0.006

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.

70 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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`

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
CHEMBL5278294	O14717	6.05	570.5 Da LogP 0.26 TPSA 229.0	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CN(CC[C@H](N)C(=O)O…`
AN6	O14717	—	395.4 Da LogP -1.85 TPSA 185.9	1 viol.	✓ Clean	`CC[N@@](CC[C@@H](C(=O)O)N)C[C@@H]1[C@H]([C@H]([…`
CHEMBL1091913	O14717	—	405.4 Da LogP -2.24 TPSA 185.9	1 viol.	✓ Clean	`C#CCN(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(N…`
CHEMBL1235825	O14717	—	381.4 Da LogP -2.24 TPSA 185.9	1 viol.	✓ Clean	`CN(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(N)nc…`
CHEMBL2018849	O14717	—	367.4 Da LogP -2.58 TPSA 194.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CNCC[C@H](N)C(=O)O)…`
CHEMBL418052	O14717	—	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)…`
CHEMBL5173405	O14717	—	457.5 Da LogP -0.67 TPSA 185.9	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CN(CC[C@H](N)C(=O)O…`
CHEMBL5173553	O14717	—	419.4 Da LogP -1.84 TPSA 185.9	1 viol.	✓ Clean	`CC#CCN(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`
CHEMBL5179717	O14717	—	449.5 Da LogP -0.68 TPSA 185.9	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CN(CC[C@H](N)C(=O)O…`
CHEMBL5182511	O14717	—	419.4 Da LogP -1.84 TPSA 185.9	1 viol.	✓ Clean	`C#CCCN(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`
CHEMBL5187166	O14717	—	419.4 Da LogP -1.85 TPSA 185.9	1 viol.	✓ Clean	`C#CC(C)N(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3…`
CHEMBL5188852	O14717	—	409.4 Da LogP -1.46 TPSA 185.9	1 viol.	✓ Clean	`CC(C)N(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(…`
CHEMBL5192893	O14717	—	433.5 Da LogP -1.46 TPSA 185.9	1 viol.	✓ Clean	`C#CC(C)(C)N(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2c…`
CHEMBL5195354	O14717	—	471.5 Da LogP -0.63 TPSA 185.9	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CN(CCc2ccccc2)CC[C@…`
CHEMBL5197627	O14717	—	421.5 Da LogP -1.46 TPSA 185.9	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CN(CC[C@H](N)C(=O)O…`
CHEMBL5202371	O14717	—	433.5 Da LogP -1.45 TPSA 185.9	1 viol.	✓ Clean	`CCC#CCN(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c…`
CHEMBL5202819	O14717	—	407.4 Da LogP -1.68 TPSA 185.9	1 viol.	✓ Clean	`C=CCN(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc3c(N…`
CHEMBL5208778	O14717	—	435.5 Da LogP -1.07 TPSA 185.9	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CN(CC[C@H](N)C(=O)O…`
SFG	O14717	—	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)…`

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	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	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	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	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…`
ZINC13650200	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)…`
ZINC1532516	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	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	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`
ZINC205994753	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	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	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)…`
ZINC33821012	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	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)…`
ZINC38192471	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	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](…`
ZINC3869837	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	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`
ZINC4217451	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…`
ZINC4228232	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	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	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	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	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	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	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	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	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	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)[…`
ZINC584905214	0.823	452.5 Da LogP -1.92 TPSA 189.1	1 viol.	✓ Clean	`CN(C)CCCN(CC[C@H](N)C(=O)O)C[C@H]1O[C@@H](n2cnc…`
ZINC34235488	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	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	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	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	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	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	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	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`
ZINC13522400	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	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…`
ZINC43771806	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	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`
ZINC1775937521	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	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…`
ZINC49014951	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	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…`
ZINC12503924	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	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	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	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	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.