Protein target profile

KP13_00801

Uracil-DNA glycosylase

Genome: KpKP13 Gene: AHE43166.1 ung 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTU7

Export view

Length 237

Pocket druggability 0.357

Direct ligand evidence 0 67 total records

Functional annotation 1 EC 6 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 (%): 64.848 Lower values reduce human off-target concern.
Human E-value: 1.46e-72
Gut microbiome similarity: 42.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 71.628 Higher values support similarity to known essential genes.
DEG E-value: 3.34e-113 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.24 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 0.357

Structure A0A0H3GTU7

Pocket Pocket 5

P2Rank 0.429

Structure A0A0H3GTU7

Pocket Pocket 1

ColabFold model

FPocket 0.214 · Pocket 10

P2Rank 0.341 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2006 / 4744 genomes with a hit

Prevalence 42.3%

Cross-references

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

Sequence

UniProt A0A0H3GTU7

Chemistry

ChEMBL CHEMBL4129274

Sequence

Primary amino-acid sequence viewer.

MTLLQESKMTTPLTWHDVLADEKQQPYFLNTLKTVAEERQSGITIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGVAIPPSLLNMYKELEATIPGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVIALINEHCEGVVFLLWGSHAQKKGAIIDRQRHCVLKAPHPSPLSAHRGFFGCNHFVQTNQWLVDRGETPIDWMPVLPAESE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

3.2.2.27

Gene Ontology (GO)

GO:0006284 In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
GO:0004844 Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine.
GO:0016799 Catalysis of the hydrolysis of any N-glycosyl bond.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0097510 A base-excision repair, AP site formation process occurring via excision of a deaminated base.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
11	237	Gene3D	G3DSA:3.40.470.10	-
11	237	InterPro	IPR036895	Uracil-DNA glycosylase-like domain superfamily
57	218	SMART	SM00987	UDG_2_a
27	228	CDD	cd10027	UDG-F1-like
27	228	InterPro	IPR002043	Uracil-DNA glycosylase family 1
57	218	SMART	SM00986	UDG_2
57	218	InterPro	IPR005122	Uracil-DNA glycosylase-like
12	228	SUPERFAMILY	SSF52141	Uracil-DNA glycosylase-like
12	228	InterPro	IPR036895	Uracil-DNA glycosylase-like domain superfamily
5	232	FunFam	G3DSA:3.40.470.10:FF:000001	Uracil-DNA glycosylase
14	221	NCBIfam	TIGR00628	uracil-DNA glycosylase
14	221	InterPro	IPR002043	Uracil-DNA glycosylase family 1
12	229	Hamap	MF_00148	Uracil-DNA glycosylase [ung].
12	229	InterPro	IPR002043	Uracil-DNA glycosylase family 1
4	230	PANTHER	PTHR11264	URACIL-DNA GLYCOSYLASE
4	230	InterPro	IPR002043	Uracil-DNA glycosylase family 1
65	74	ProSitePatterns	PS00130	Uracil-DNA glycosylase signature.
65	74	InterPro	IPR018085	Uracil-DNA glycosylase, active site
63	217	Pfam	PF03167	Uracil DNA glycosylase superfamily
63	217	InterPro	IPR005122	Uracil-DNA glycosylase-like

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 #5

0.357

Likely same site as P2Rank 3 2.4 Å 3 shared residues 75% of smaller site

Show in viewer

Surrounding area

Site 2 FPocket #3

0.252

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.429

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.012

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.012

Likely same site as FPocket 5 2.4 Å 3 shared residues 75% of smaller site

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.004

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:64-64 Proton acceptor

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.341

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.058

Likely same site as FPocket 10 0.9 Å 8 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.01

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_A0A0H3GTU7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00801	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 16 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

302 PDB via homolog 346.3 Da · LogP 0.16 · TPSA 146.2 Open detail RCSB PDB

3FI PDB via homolog Detail RCSB PDB

3FL PDB via homolog Detail RCSB PDB

5NU PDB via homolog Detail RCSB PDB

5UC 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
302 RCSB PDB	2HXM	P13051	346.3 Da LogP 0.16 TPSA 146.2	✓ Ro5	✓ Clean	`c1cc(ccc1\C=N\OCCO/N=C/C2=CC(=O)NC(=O)N2)C(=O)O`
3FI RCSB PDB	3FCI	P13051	346.3 Da LogP 0.29 TPSA 136.6	✓ Ro5	✓ Clean	`c1cc(cc(c1)C(=O)O)\C=N\OCCCNCC2=CC(=O)NC(=O)N2`
3FL RCSB PDB	3FCL	P13051	346.4 Da LogP 0.42 TPSA 127.1	✓ Ro5	✓ Clean	`c1cc(cc(c1)C(=O)O)CNCCCCNCC2=CC(=O)NC(=O)N2`
5NU RCSB PDB	4WS4	P9WFQ9	157.1 Da LogP -1.03 TPSA 108.9	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1)[N+](=O)[O-]`
5UC RCSB PDB	4WS7	P9WFQ9	146.5 Da LogP -0.28 TPSA 65.7	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1)Cl`
6UA RCSB PDB	4WS2	P9WFQ9	127.1 Da LogP -1.02 TPSA 84.5	✓ Ro5	✓ Clean	`C1C(=NC(=O)NC1=O)N`
DUR RCSB PDB	2C53	P10186	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=O)NC2=O)CO)O`
FCF RCSB PDB	3FCF	P13051	346.3 Da LogP 0.16 TPSA 146.2	✓ Ro5	✓ Clean	`c1cc(cc(c1)C(=O)O)\C=N\OCCO/N=C/C2=CC(=O)NC(=O)…`
FCK RCSB PDB	3FCK	P13051	346.3 Da LogP 0.29 TPSA 136.6	✓ Ro5	✓ Clean	`c1cc(cc(c1)C(=O)O)CNCCCON=CC2=CC(=O)NC(=O)N2`
FLC RCSB PDB	3A7N	P9WFQ9	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
QU4 RCSB PDB	6VBA	P13051	422.3 Da LogP 2.45 TPSA 169.4	✓ Ro5	✓ Clean	`c1cc(c(cc1C(=C2C=CC(=O)C(=C2)C(=O)O)c3ccc(c(c3)…`
TUL RCSB PDB	4WS8	P9WFQ9	128.2 Da LogP 0.43 TPSA 48.6	✓ Ro5	✓ Clean	`C1=CNC(=S)NC1=O`
URA RCSB PDB	1FLZ	P12295	112.1 Da LogP -0.94 TPSA 65.7	✓ Ro5	✓ Clean	`C1=CNC(=O)NC1=O`
URB RCSB PDB	3CXM	D0VWU0	191.0 Da LogP -0.17 TPSA 65.7	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1)Br`
URF RCSB PDB	4WRY	P9WFQ9	130.1 Da LogP -0.80 TPSA 65.7	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1)F`
WBU RCSB PDB	4WS6	P9WFQ9	127.1 Da LogP -1.35 TPSA 91.7	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1)N`

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
CHEMBL4129274 ChEMBL	P13051	—	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
ZINC105325 ZINC	1.000	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]1`
ZINC155696 ZINC	1.000	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]1`
ZINC2556389 ZINC	1.000	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]1`
ZINC3635934 ZINC	1.000	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]1`
ZINC3833863 ZINC	1.000	422.3 Da LogP 2.45 TPSA 169.4	✓ Ro5	✓ Clean	`O=C(O)C1=CC(=C(c2ccc(O)c(C(=O)O)c2)c2ccc(O)c(C(…`
ZINC3869842 ZINC	1.000	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]1`
ZINC4124398 ZINC	1.000	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]1`
ZINC56350 ZINC	1.000	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]1`
ZINC8613701 ZINC	1.000	228.2 Da LogP -1.82 TPSA 104.6	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]1`
ZINC4918789 ZINC	0.850	258.2 Da LogP -2.46 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=…`
ZINC4918794 ZINC	0.850	258.2 Da LogP -2.46 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O…`
ZINC4918798 ZINC	0.850	258.2 Da LogP -2.46 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(…`
ZINC4918802 ZINC	0.850	258.2 Da LogP -2.46 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=…`
ZINC103421486 ZINC	0.762	244.3 Da LogP -0.45 TPSA 87.5	✓ Ro5	✓ Clean	`O=c1[nH]c(=S)ccn1[C@H]1C[C@@H](O)[C@@H](CO)O1`
ZINC1081178 ZINC	0.762	230.2 Da LogP -0.85 TPSA 84.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](F)[C@@H](CO)O2)c(=O)[nH]1`
ZINC17173289 ZINC	0.762	244.3 Da LogP -0.45 TPSA 87.5	✓ Ro5	✓ Clean	`O=c1[nH]c(=S)ccn1[C@H]1C[C@H](O)[C@@H](CO)O1`
ZINC2556998 ZINC	0.762	230.2 Da LogP -0.85 TPSA 84.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](F)[C@H](CO)O2)c(=O)[nH]1`
ZINC29544850 ZINC	0.762	230.2 Da LogP -0.85 TPSA 84.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](F)[C@@H](CO)O2)c(=O)[nH]1`
ZINC33505015 ZINC	0.762	244.3 Da LogP -0.45 TPSA 87.5	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=S)[nH]1`
ZINC3792179 ZINC	0.762	230.2 Da LogP -0.85 TPSA 84.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](F)[C@@H](CO)O2)c(=O)[nH]1`
ZINC4975368 ZINC	0.762	230.2 Da LogP -0.85 TPSA 84.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](F)[C@H](CO)O2)c(=O)[nH]1`
ZINC2054344316 ZINC	0.756	300.3 Da LogP 2.01 TPSA 111.9	✓ Ro5	✓ Clean	`CC(=C1C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1`
ZINC28092924 ZINC	0.756	300.3 Da LogP 2.01 TPSA 111.9	✓ Ro5	✓ Clean	`C/C(=C1/C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1`
ZINC36748824 ZINC	0.756	300.3 Da LogP 2.01 TPSA 111.9	✓ Ro5	✓ Clean	`C/C(=C1\C=CC(=O)C(C(=O)O)=C1)c1ccc(O)c(C(=O)O)c1`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC13514392 ZINC	0.696	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)…`
ZINC1532629 ZINC	0.696	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c…`
ZINC3869888 ZINC	0.696	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC3869889 ZINC	0.696	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869890 ZINC	0.696	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC4228260 ZINC	0.696	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC6524723 ZINC	0.696	308.2 Da LogP -1.71 TPSA 151.1	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC3787626 ZINC	0.681	253.2 Da LogP -0.50 TPSA 133.1	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@@…`
ZINC5663432 ZINC	0.681	253.2 Da LogP -0.50 TPSA 133.1	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1C[C@@H](n2ccc(=O)[nH]c2=O)O[C@…`
ZINC5663433 ZINC	0.681	253.2 Da LogP -0.50 TPSA 133.1	✓ Ro5	Alert	`[N-]=[N+]=N[C@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@H…`
ZINC5663434 ZINC	0.681	253.2 Da LogP -0.50 TPSA 133.1	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1C[C@@H](n2ccc(=O)[nH]c2=O)O[C…`
ZINC5663435 ZINC	0.681	253.2 Da LogP -0.50 TPSA 133.1	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@…`
ZINC6524816 ZINC	0.681	253.2 Da LogP -0.50 TPSA 133.1	✓ Ro5	Alert	`[N-]=[N+]=N[C@@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@…`
ZINC38322194 ZINC	0.667	254.2 Da LogP -1.26 TPSA 134.6	✓ Ro5	Alert	`N=[N+]=N[C@@H]1C[C@@H](n2ccc(=O)[nH]c2=O)O[C@H]…`
ZINC38322195 ZINC	0.667	254.2 Da LogP -1.26 TPSA 134.6	✓ Ro5	Alert	`N=[N+]=N[C@@H]1C[C@H](n2ccc(=O)[nH]c2=O)O[C@H]1…`
ZINC3870698 ZINC	0.667	212.2 Da LogP -0.80 TPSA 84.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2ccc(=O)[nH]c2=O)C[C@@H]1O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC13519035 ZINC	0.651	229.2 Da LogP -2.43 TPSA 117.4	✓ Ro5	✓ Clean	`O=c1ncn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]1`
ZINC64708385 ZINC	0.644	467.4 Da LogP 0.44 TPSA 214.5	1 viol.	✓ Clean	`NOC(=O)C1=CC(=C(c2ccc(O)c(C(=O)ON)c2)c2ccc(O)c(…`
ZINC8217150 ZINC	0.640	388.2 Da LogP -1.59 TPSA 197.6	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(…`
ZINC2522522 ZINC	0.636	244.2 Da LogP -2.12 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@@H](O)[C@H](CO)O2)cc1O`
ZINC405339 ZINC	0.636	244.2 Da LogP -2.12 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@H]2C[C@H](O)[C@H](CO)O2)cc1O`
ZINC4897037 ZINC	0.636	244.2 Da LogP -2.12 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2C[C@H](O)[C@H](CO)O2)cc1O`

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_00801

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 · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence