Protein target profile

KP13_00581

6-phosphofructokinase

Genome: KpKP13 Gene: pfkA AHE47056.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GGY4

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Length 320

Pocket druggability 0.066

Direct ligand evidence 0 59 total records

Functional annotation 1 EC 13 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.

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 (%): 57.778 Lower values reduce human off-target concern.
Human E-value: 6.1e-09
Gut microbiome similarity: 21.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 72.188 Higher values support similarity to known essential genes.
DEG E-value: 8.46e-173 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.17 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 0.066

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

Prevalence 21.4%

Cross-references

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

Sequence

UniProt A0A0H3GGY4

Chemistry

ChEMBL DWT ChEMBL CHEMBL2336325 ChEMBL CHEMBL4129274

Sequence

Primary amino-acid sequence viewer.

MIKKIGVLTSGGDAPGMNAAIRGVVRAALTEGLEVFGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFREEHIRAVAIENMKKRGLDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFIMVPEVEYTRDDLVAEIKAGIAKGKKHAIVAITEHMCDVDELASYIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIELLLQGHGGRCVGIQNEKLVHHDIIDAIENMKRPFKNDWLDCAKKLY

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 domains and features

Domain and signature matches imported 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; 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 · P2Rank

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

Site 1 P2Rank #1

0.544

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.034

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:128-128 Proton acceptor

UniProt: Binding site:103-106

UniProt: Binding site:104-104

UniProt: Binding site:12-12

UniProt: Binding site:126-128 in other chain

UniProt: Binding site:155-155 in other chain

UniProt: Binding site:163-163

UniProt: Binding site:170-172 in other chain

UniProt: Binding site:186-188 in other chain

UniProt: Binding site:212-212 in other chain

UniProt: Binding site:214-216 in other chain

UniProt: Binding site:22-26

UniProt: Binding site:223-223 in other chain

UniProt: Binding site:244-244

UniProt: Binding site:250-253 in other chain

UniProt: Binding site:55-60

UniProt: Binding site:73-74

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_A0A0H3GGY4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00581	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.

59 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 3 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ACP PDB via homolog 505.2 Da · LogP -1.52 · TPSA 269.9 Open detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

F6P PDB via homolog Detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

PEP PDB via homolog Detail RCSB PDB

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
ACP RCSB PDB	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 RCSB PDB	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 RCSB PDB	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 RCSB PDB	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 RCSB PDB	4I4I	P00512	168.0 Da LogP -0.31 TPSA 104.1	✓ Ro5	✓ Clean	`C=C(C(=O)O)OP(=O)(O)O`
PGA RCSB PDB	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 ChEMBL	Q01813	8.24 ~5.8 nM	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
CHEMBL2336325 ChEMBL	Q01813	6.01 ~977.2 nM	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@@H]4C)nc(N4CCOC…`
CHEMBL4129274 ChEMBL	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 ZINC	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 ZINC	1.000	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@@H]4C)nc(N4CCOC…`
ZINC12504372 ZINC	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 ZINC	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 ZINC	1.000	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@H]4C)nc(N4CCOC[…`
ZINC1532531 ZINC	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 ZINC	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 ZINC	1.000	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@H]4C)nc(N4CCOC[…`
ZINC3869919 ZINC	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 ZINC	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 ZINC	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 ZINC	1.000	462.6 Da LogP 2.50 TPSA 92.7	✓ Ro5	✓ Clean	`CNC(=O)c1cccc(-c2ccc3c(N4CCOC[C@@H]4C)nc(N4CCOC…`
ZINC12494841 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	0.831	449.5 Da LogP 2.84 TPSA 100.9	✓ Ro5	✓ Clean	`C[C@H]1COCCN1c1nc(N2CCOC[C@@H]2C)c2ccc(-c3cccc(…`
ZINC12360002 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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.

KP13_00581

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Chemistry

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence