Protein profile

KP13_00581

6-phosphofructokinase

Genome: KpKP13

Gene: AHE47056.1 pfkA Structure source: AlphaFold + ColabFold UniProt A0A0H3GGY4

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Amino acids 320

Annotations 14

Features 38

PDB binders 6

Druggability 0.066

Overview

Basic information about this protein and its source genome.

Accession: KP13_00581
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE47056.1 pfkA
Status: annotated
Amino acids: 320
Structure source: AlphaFold + ColabFold

2.7.1.11

GO:0008443 Catalysis of the transfer of a phosphate group, usually from ATP, to a phosphofructose substrate molecule. GO:0006002 The chemical reactions and pathways involving fructose 6-phosphate, also known as F6P. The D-enantiomer is an important intermediate in glycolysis, gluconeogenesis, and fructose metabolism. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0003872 Catalysis of the reaction: ATP + D-fructose-6-phosphate = ADP + D-fructose 1,6-bisphosphate. GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. GO:0005945 A protein complex that possesses 6-phosphofructokinase activity; homodimeric, homooctameric, and allosteric homotetrameric forms are known.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 57.778
Human E-value: 6.1e-09
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 72.188
DEG E-value: 8.46e-173
Localization: Cytoplasmic
ColabFold pLDDT: 96.17

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 0.066

Structure A0A0H3GGY4

Pocket Pocket 7

P2Rank 0.544

Structure A0A0H3GGY4

Pocket Pocket 1

ColabFold model

FPocket 0.547 · Pocket 6

P2Rank 0.652 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1016 / 4744 genomes with a hit

Normalized 0.214

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Enzyme Commission (EC)

2.7.1.11

Gene Ontology (GO)

GO:0008443 Catalysis of the transfer of a phosphate group, usually from ATP, to a phosphofructose substrate molecule.
GO:0006002 The chemical reactions and pathways involving fructose 6-phosphate, also known as F6P. The D-enantiomer is an important intermediate in glycolysis, gluconeogenesis, and fructose metabolism.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0003872 Catalysis of the reaction: ATP + D-fructose-6-phosphate = ADP + D-fructose 1,6-bisphosphate.
GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
GO:0005945 A protein complex that possesses 6-phosphofructokinase activity; homodimeric, homooctameric, and allosteric homotetrameric forms are known.
GO:0016208 Binding to AMP, adenosine monophosphate.
GO:0070095 Binding to fructose 6-phosphate.
GO:0042802 Binding to an identical protein or proteins.
GO:0046872 Binding to a metal ion.
GO:0048029 Binding to a monosaccharide. Monosaccharides are the simplest carbohydrates; they are polyhydroxy aldehydes H[CH(OH)]nC(=O)H or polyhydroxy ketones H[CHOH]nC(=O)[CHOH]mH with three or more carbon atoms. They form the constitutional repeating units of oligo- and polysaccharides.
GO:0061621 The glycolytic process that begins with the conversion of glucose to glucose-6-phosphate by glucokinase activity. Glycolytic processes are the chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP.
GO:0030388 The chemical reactions and pathways involving fructose 1,6-bisphosphate, also known as FBP. The D enantiomer is a metabolic intermediate in glycolysis and gluconeogenesis.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
3	320	CDD	cd00763	Bacterial_PFK
3	320	InterPro	IPR012828	ATP-dependent 6-phosphofructokinase, prokaryotic
3	311	SUPERFAMILY	SSF53784	Phosphofructokinase
3	311	InterPro	IPR035966	Phosphofructokinase superfamily
244	262	ProSitePatterns	PS00433	Phosphofructokinase signature.
244	262	InterPro	IPR015912	Phosphofructokinase, conserved site
4	276	Pfam	PF00365	Phosphofructokinase
4	276	InterPro	IPR000023	Phosphofructokinase domain
2	320	Hamap	MF_00339	ATP-dependent 6-phosphofructokinase [pfkA].
2	320	InterPro	IPR012828	ATP-dependent 6-phosphofructokinase, prokaryotic
4	301	NCBIfam	TIGR02482	6-phosphofructokinase
4	301	InterPro	IPR012828	ATP-dependent 6-phosphofructokinase, prokaryotic
3	305	PANTHER	PTHR13697	PHOSPHOFRUCTOKINASE
143	252	Gene3D	G3DSA:3.40.50.460	Phosphofructokinase domain
143	252	InterPro	IPR035966	Phosphofructokinase superfamily
4	168	FunFam	G3DSA:3.40.50.450:FF:000001	ATP-dependent 6-phosphofructokinase
4	280	Gene3D	G3DSA:3.40.50.450	-
1	320	PIRSF	PIRSF000532	ATP_PFK_prok
1	320	InterPro	IPR012003	ATP-dependent 6-phosphofructokinase, prokaryotic-type
7	26	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
7	26	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
32	45	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
32	45	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
139	157	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
139	157	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
213	225	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
213	225	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
177	194	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
177	194	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
240	262	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
240	262	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
159	175	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
159	175	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
94	110	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
94	110	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
121	138	PRINTS	PR00476	ATP-dependent phosphofructokinase family signature
121	138	InterPro	IPR022953	ATP-dependent 6-phosphofructokinase
143	252	FunFam	G3DSA:3.40.50.460:FF:000002	ATP-dependent 6-phosphofructokinase

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_A0A0H3GGY4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00581	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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				6.49	0.328
2				1.53	0.023

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
6				0.547
2				0.285

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				7.84	0.416
2				1.39	0.017

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.

59 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
ACP	4RH3	Q01813	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP	5XZ6	Q2FXM8	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
F6P	5XZ7	P99165	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)O)O)O)OP(=O)(…`
FLC	5XZA	P99165	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
PEP	4I4I	P00512	168.0 Da LogP -0.31 TPSA 104.1	✓ Ro5	✓ Clean	`C=C(C(=O)O)OP(=O)(O)O`
PGA	6PFK	P00512	156.0 Da LogP -0.82 TPSA 104.1	✓ Ro5	✓ Clean	`C(C(=O)O)OP(=O)(O)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
DWT	Q01813	8.24	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
CHEMBL2336325	Q01813	6.01	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@@H]4C)nc(N4CCOC…`
CHEMBL4129274	P08237	—	851.5 Da LogP 4.76 TPSA 183.3	3 viol.	Alert	`C=CC(=O)Nc1ccccc1Nc1nc(Nc2ccc(N3CCN(CCOCCOCCOCC…`

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
ZINC100351924	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@](O)(CO)[C@@H](O)[C@H]1O`
ZINC115560110	1.000	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@@H]4C)nc(N4CCOC…`
ZINC12504372	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O`
ZINC138814335	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@](O)(CO)[C@H](O)[C@H]1O`
ZINC139563465	1.000	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@H]4C)nc(N4CCOC[…`
ZINC1532531	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@](O)(CO)[C@H](O)[C@H]1O`
ZINC1532847	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@](O)(CO)[C@H](O)[C@@H]1O`
ZINC208949769	1.000	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@H]4C)nc(N4CCOC[…`
ZINC3869919	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@](O)(CO)[C@@H](O)[C@@H]1O`
ZINC4096690	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O`
ZINC56874962	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@](O)(CO)[C@H](O)[C@@H]1O`
ZINC59258964	1.000	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@@H]4C)nc(N4CCOC…`
ZINC12494841	0.909	290.2 Da LogP -3.74 TPSA 177.1	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@H](O)[…`
ZINC199142139	0.909	290.2 Da LogP -3.74 TPSA 177.1	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@](O)(CO)[C@H](O)[C@@H](O)…`
ZINC257392909	0.909	290.2 Da LogP -3.74 TPSA 177.1	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@](O)(CO)[C@H](O)[C@H](O)[…`
ZINC257392910	0.909	290.2 Da LogP -3.74 TPSA 177.1	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@](O)(CO)[C@H](O)[C@H](O)[…`
ZINC257392911	0.909	290.2 Da LogP -3.74 TPSA 177.1	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@](O)(CO)[C@H](O)[C@@H](O)…`
ZINC1857603320	0.844	474.6 Da LogP 2.64 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4[C@H]5CC[C@H]4COC5)nc(…`
ZINC169051710	0.831	449.5 Da LogP 2.84 TPSA 100.9	✓ Ro5	✓ Clean	`C[C@H]1COCCN1c1nc(N2CCOC[C@@H]2C)c2ccc(-c3cccc(…`
ZINC12360002	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC11680412	0.771	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@](O)(COP(=O)(O)O)[C@H](O)[…`
ZINC11680415	0.771	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@](O)(COP(=O)(O)O)[C@H](O)[…`
ZINC3869914	0.771	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@](O)(COP(=O)(O)O)[C@@H](O…`
ZINC3869915	0.771	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@](O)(COP(=O)(O)O)[C@@H](…`
ZINC3869916	0.771	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@](O)(COP(=O)(O)O)[C@@H](O…`
ZINC3869917	0.771	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@](O)(COP(=O)(O)O)[C@@H](…`
ZINC4096694	0.771	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@](O)(COP(=O)(O)O)[C@@H](O)…`
ZINC13518964	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](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.