Protein target profile

KP13_01374

NADH pyrophosphatase

Genome: KpKP13 Gene: nudC AHE46925.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GHB2

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Length 257

Pocket druggability 0.07

Direct ligand evidence 0 57 total records

Functional annotation 2 EC 11 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 (%): 40.741 Lower values reduce human off-target concern.
Human E-value: 1.43e-19
Gut microbiome similarity: 2.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.6 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 0.07

Structure A0A0H3GHB2

Pocket Pocket 9

P2Rank 0.872

Structure A0A0H3GHB2

Pocket Pocket 1

ColabFold model

FPocket 0.083 · Pocket 15

P2Rank 0.824 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 116 / 4744 genomes with a hit

Prevalence 2.4%

Cross-references

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

Sequence

UniProt A0A0H3GHB2

Sequence

Primary amino-acid sequence viewer.

MDRIIEKLDRGWWVVSHEQKLWLPGGELPHGEAVNFDLVGQHALHIGEWQGESVWMVRQDRRHDMGSLRQVLDQDPGLFQLAGRGIQLAEFYRSHKFCGYCGHPMHASKSEWAMLCSHCRERYYPQIAPCIIVAIRRDDAILLAQHTRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIRVKNLRYVTSQPWPFPQSLMTAFMADYADGEIVVDKKELLTADWYRYDDLPLLPPPGTVARRLIEDTVAMCRAEFE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 11 GO

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0000210 Catalysis of the reaction: NAD+ + H2O = AMP + NMN.
GO:0046872 Binding to a metal ion.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0030145 Binding to a manganese ion (Mn).
GO:0035529 Catalysis of the reaction: NADH + H2O = AMP + NMNH + 2 H+.
GO:0110153 Catalysis of the reaction: a 5'-end NAD+-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-nicotinamide D-ribonucleotide + 2 H+.
GO:0008270 Binding to a zinc ion (Zn).
GO:0019677 The chemical reactions and pathways resulting in the breakdown of nicotinamide adenine dinucleotide (NAD+), a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions.
GO:0006742 The chemical reactions and pathways resulting in the breakdown of nicotinamide adenine dinucleotide phosphate (NADP+), a coenzyme that interconverts with its reduced form, NADPH, in many redox and biosynthetic reactions.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
1	125	Gene3D	G3DSA:3.90.79.20	-
3	96	SUPERFAMILY	SSF55811	Nudix
3	96	InterPro	IPR015797	NUDIX hydrolase-like domain superfamily
62	252	PANTHER	PTHR42904	NUDIX HYDROLASE, NUDC SUBFAMILY
126	257	Gene3D	G3DSA:3.90.79.10	Nucleoside Triphosphate Pyrophosphohydrolase
132	234	Pfam	PF00293	NUDIX domain
132	234	InterPro	IPR000086	NUDIX hydrolase domain
129	250	CDD	cd03429	NADH_pyrophosphatase
1	257	Hamap	MF_00297	NAD-capped RNA hydrolase NudC [nudC].
1	257	InterPro	IPR022925	NAD-capped RNA hydrolase NudC
125	248	ProSiteProfiles	PS51462	Nudix hydrolase domain profile.
125	248	InterPro	IPR000086	NUDIX hydrolase domain
1	125	FunFam	G3DSA:3.90.79.20:FF:000001	NADH pyrophosphatase
159	180	ProSitePatterns	PS00893	Nudix box signature.
159	180	InterPro	IPR020084	NUDIX hydrolase, conserved site
79	241	SUPERFAMILY	SSF55811	Nudix
79	241	InterPro	IPR015797	NUDIX hydrolase-like domain superfamily
93	124	Pfam	PF09297	NADH pyrophosphatase zinc ribbon domain
93	124	InterPro	IPR015376	Zinc ribbon, NADH pyrophosphatase
126	257	FunFam	G3DSA:3.90.79.10:FF:000004	NADH pyrophosphatase

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

0.872

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Surrounding area

Site 2 P2Rank #2

0.016

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Surrounding area

Site 3 P2Rank #3

0.002

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Surrounding area

Residue sets

UniProt: Binding site:101-101

UniProt: Binding site:111-111

UniProt: Binding site:116-116

UniProt: Binding site:119-119

UniProt: Binding site:124-124

UniProt: Binding site:158-158

UniProt: Binding site:174-174

UniProt: Binding site:178-178

UniProt: Binding site:192-199

UniProt: Binding site:219-219

UniProt: Binding site:241-241

UniProt: Binding site:69-69

UniProt: Binding site:98-98

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.824

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Surrounding area

Site 2 P2Rank #2

0.059

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Surrounding area

Site 3 P2Rank #3

0.008

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Surrounding area

Site 4 P2Rank #4

0.003

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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_A0A0H3GHB2	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01374	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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2ME PDB via homolog 60.1 Da · LogP 0.65 · TPSA 9.2 Open detail RCSB PDB

8DG PDB via homolog Detail RCSB PDB

GPP PDB via homolog Detail RCSB PDB

IPR PDB via homolog Detail RCSB PDB

MGP 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
2ME RCSB PDB	5WWD	Q9CA40	60.1 Da LogP 0.65 TPSA 9.2	✓ Ro5	✓ Clean	`CCOC`
8DG RCSB PDB	6FL4	Q9CA40	523.2 Da LogP -2.01 TPSA 298.8	3 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C3=C(C(=O)NC(=N3)N)NC2=…`
GPP RCSB PDB	5GP0	Q9CA40	314.2 Da LogP 2.91 TPSA 113.3	✓ Ro5	✓ Clean	`CC(=CCC/C(=C/CO[P@@](=O)(O)OP(=O)(O)O)/C)C`
IPR RCSB PDB	6DBZ	Q9CA40	248.1 Da LogP 1.26 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)CCO[P@@](=O)(O)OP(=O)(O)O`
MGP RCSB PDB	6SCX	Q9BQG2	538.2 Da LogP -2.91 TPSA 290.1	3 viol.	✓ Clean	`C[n+]1cn(c2c1C(=O)NC(=N2)N)[C@H]3[C@@H]([C@@H](…`
NH4 RCSB PDB	5WWD	Q9CA40	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
NMN RCSB PDB	5IW5	P32664	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(…`

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
ZINC12503278 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@@H…`
ZINC1532667 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@H]2O[C@@H](COP(=O)(O)O)[C@H]…`
ZINC2545161 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@@H](COP(=O)(O)O)[C@H…`
ZINC2579357 ZINC	1.000	248.1 Da LogP 1.26 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)CCO[P@](=O)(O)OP(=O)(O)O`
ZINC3870109 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@@H](COP(=O)(O)O)[C@@…`
ZINC40465856 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@H]…`
ZINC40762833 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC4228273 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@@H…`
ZINC77311638 ZINC	1.000	335.2 Da LogP -2.20 TPSA 163.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@H]…`
ZINC8215849 ZINC	1.000	314.2 Da LogP 2.91 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CO[P@@](=O)(O)OP(=O)(O)O`
ZINC12494625 ZINC	0.969	382.3 Da LogP 4.63 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CC/C(C)=C/CO[P@@](=O)(O)OP(=O)…`
ZINC2356589248 ZINC	0.969	382.3 Da LogP 4.63 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)=CCCC(C)=CCCC(C)=CCO[P@](=O)(O)OP(=O)(O)O`
ZINC34661063 ZINC	0.939	394.2 Da LogP 3.02 TPSA 159.8	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CO[P@@](=O)(O)O[P@@](=O)(O)OP(…`
ZINC8218174 ZINC	0.912	462.3 Da LogP 4.75 TPSA 159.8	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CC/C(C)=C/CO[P@@](=O)(O)O[P@@]…`
ZINC4095572 ZINC	0.809	336.2 Da LogP -1.60 TPSA 157.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@@H…`
ZINC77311659 ZINC	0.809	336.2 Da LogP -1.60 TPSA 157.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@H]…`
ZINC77311660 ZINC	0.809	336.2 Da LogP -1.60 TPSA 157.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@H]…`
ZINC77311661 ZINC	0.809	336.2 Da LogP -1.60 TPSA 157.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc[n+]([C@@H]2O[C@H](COP(=O)(O)O)[C@@H…`
ZINC25756940 ZINC	0.760	331.3 Da LogP 0.35 TPSA 123.0	✓ Ro5	✓ Clean	`C[C@@H]1[C@@H](COP(=O)(O)O)O[C@@H]([n+]2cccc(C(…`
ZINC1532829 ZINC	0.758	234.2 Da LogP 2.79 TPSA 66.8	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/COP(=O)(O)O`
ZINC2556391 ZINC	0.735	302.4 Da LogP 4.51 TPSA 66.8	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/CC/C(C)=C/COP(=O)(O)O`
ZINC8215740 ZINC	0.719	246.1 Da LogP 1.18 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)=CCO[P@@](=O)(O)OP(=O)(O)O`
ZINC12503703 ZINC	0.708	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC8215878 ZINC	0.708	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC1776011316 ZINC	0.700	333.3 Da LogP -1.74 TPSA 154.2	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CCP(=O)(O)O)[C@@H…`
ZINC14613564 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO)[C@@H](O)[C@@H…`
ZINC34633968 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@H]2O[C@H](CO)[C@@H](O)[C@H]2…`
ZINC4096036 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO)[C@@H](O)[C@H]…`
ZINC65748069 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO)[C@H](O)[C@H]2…`
ZINC65748073 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO)[C@H](O)[C@@H]…`
ZINC901659 ZINC	0.681	255.2 Da LogP -2.32 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc[n+]([C@H]2O[C@@H](CO)[C@H](O)[C@@H]…`
ZINC71769106 ZINC	0.676	326.1 Da LogP 1.30 TPSA 159.8	✓ Ro5	✓ Clean	`CC(C)=CCO[P@@](=O)(O)O[P@@](=O)(O)OP(=O)(O)O`
ZINC12502182 ZINC	0.667	283.2 Da LogP -2.36 TPSA 159.2	✓ Ro5	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2C[C@@H](O)[C@@H](CO)O…`
ZINC12502183 ZINC	0.667	283.2 Da LogP -2.36 TPSA 159.2	✓ Ro5	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@H]2C[C@@H](O)[C@@H](CO)O2…`
ZINC12502185 ZINC	0.667	283.2 Da LogP -2.36 TPSA 159.2	✓ Ro5	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2C[C@H](O)[C@@H](CO)O2…`
ZINC16051666 ZINC	0.667	283.2 Da LogP -2.36 TPSA 159.2	✓ Ro5	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@H]2C[C@H](O)[C@@H](CO)O2)…`
ZINC2510814 ZINC	0.667	283.2 Da LogP -2.36 TPSA 159.2	✓ Ro5	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2C[C@@H](O)[C@H](CO)O2…`
ZINC4533532 ZINC	0.667	283.2 Da LogP -2.36 TPSA 159.2	✓ Ro5	✓ Clean	`Nc1nc2c([nH]c(=O)n2[C@@H]2C[C@H](O)[C@H](CO)O2)…`
ZINC71404870 ZINC	0.657	230.3 Da LogP 4.23 TPSA 26.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C/COP(C)(C)=O`
ZINC8436838 ZINC	0.657	262.1 Da LogP 0.15 TPSA 133.5	✓ Ro5	✓ Clean	`C/C(=C\CO[P@@](=O)(O)OP(=O)(O)O)CO`
ZINC13539354 ZINC	0.632	332.2 Da LogP 3.20 TPSA 113.3	✓ Ro5	✓ Clean	`CC(C)=CCC/C(C)=C(\F)CO[P@](=O)(O)OP(=O)(O)O`
ZINC5811921 ZINC	0.604	333.2 Da LogP -0.94 TPSA 159.5	✓ Ro5	✓ Clean	`NC(=O)c1cccc([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC5811924 ZINC	0.604	333.2 Da LogP -0.94 TPSA 159.5	✓ Ro5	✓ Clean	`NC(=O)c1cccc([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC5811925 ZINC	0.604	333.2 Da LogP -0.94 TPSA 159.5	✓ Ro5	✓ Clean	`NC(=O)c1cccc([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC5811926 ZINC	0.604	333.2 Da LogP -0.94 TPSA 159.5	✓ Ro5	✓ Clean	`NC(=O)c1cccc([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC12296728 ZINC	0.597	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)…`
ZINC13527599 ZINC	0.597	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O…`
ZINC13527603 ZINC	0.597	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)…`
ZINC3869846 ZINC	0.597	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O…`
ZINC3869847 ZINC	0.597	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2…`

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_01374

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

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Structural evidence

Ligand evidence