KpKP13 Protein target profile

Endonuclease 8 bifunctional protein

Accession: KP13_03284

Gene: AHE45663.1 nei 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GU47

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Length 263

Pocket druggability (P2Rank · AlphaFold DB model) 0.074

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 (%): 32.773 Lower values reduce human off-target concern.
Human E-value: 3.75e-07
Gut microbiome similarity: 1.7% 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.

Structure confidence

ColabFold pLDDT: 95.53 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.074

Structure A0A0H3GU47

Pocket Pocket 1

Druggability (FPocket) 0.243

Structure A0A0H3GU47

Pocket Pocket 5

ColabFold model

P2Rank 0.077 · Pocket 1

FPocket 0.303 · Pocket 7

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 81 / 4744 genomes with a hit

Prevalence 1.7%

Sequence

Primary amino-acid sequence viewer.

MPEGPEIRRAADKLEAAIKGEPLTNVWFAFPQLQPYQTQLTGQRVTHIATRGKALLTHFSGGLTLYSHNQLYGVWRVVDAGVEPQSNRVLRVRLQTASKAILLYSASDIDILTAEQVANHPFLLRVGPDVLDMTLTAEQVKARLLSAKFRNRQFSGLLLDQAFLAGLGNYLRVEILWQVGLSGKRKAAELSDSQLDALAHALLDIPRLSYRTRGLVDDNKHHGALFRFKVFHRDGERCERCGGIIEKTTLSSRPFYWCPGCQH

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 11 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0008270 Binding to a zinc ion (Zn).
GO:0003684 Binding to damaged DNA.
GO:0003906 Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
GO:0003676 Binding to a nucleic acid.
GO:0140078 Catalysis of the cleavage of an AP site 3' of the baseless site by a beta-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate.
GO:0000703 Catalysis of the removal oxidized pyrimidine bases by cleaving the N-C1' glycosidic bond between the oxidized pyrimidine and the deoxyribose sugar. The reaction involves formation of a covalent enzyme-pyrimidine base intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apyrimidinic (AP) site.
GO:0016799 Catalysis of the hydrolysis of any N-glycosyl bond.
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:0019104 Catalysis of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site.
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:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

31 records

Show feature table

Start	End	DB	Term	Name
2	116	CDD	cd08965	EcNei-like_N
2	116	InterPro	IPR044091	Nei, N-terminal
2	110	SMART	SM00898	Fapy_DNA_glyco_2
2	110	InterPro	IPR012319	Formamidopyrimidine-DNA glycosylase, catalytic domain
126	214	SUPERFAMILY	SSF46946	S13-like H2TH domain
126	214	InterPro	IPR010979	Ribosomal protein S13-like, H2TH
226	262	SUPERFAMILY	SSF57716	Glucocorticoid receptor-like (DNA-binding domain)
128	263	Gene3D	G3DSA:1.10.8.50	-
2	104	ProSiteProfiles	PS51068	Formamidopyrimidine-DNA glycosylase catalytic domain profile.
2	104	InterPro	IPR012319	Formamidopyrimidine-DNA glycosylase, catalytic domain
127	263	FunFam	G3DSA:1.10.8.50:FF:000005	Endonuclease 8
238	262	ProSitePatterns	PS01242	Zinc finger FPG-type signature.
238	262	InterPro	IPR015887	DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site
126	221	SMART	SM01232	H2TH_2
126	221	InterPro	IPR015886	DNA glycosylase/AP lyase, H2TH DNA-binding
1	262	PANTHER	PTHR42697	ENDONUCLEASE 8
235	263	Pfam	PF06827	Zinc finger found in FPG and IleRS
235	263	InterPro	IPR010663	Zinc finger, FPG/IleRS-type
2	127	Gene3D	G3DSA:3.20.190.10	-
2	127	InterPro	IPR035937	MutM-like, N-terminal
2	127	FunFam	G3DSA:3.20.190.10:FF:000002	Endonuclease 8
2	125	SUPERFAMILY	SSF81624	N-terminal domain of MutM-like DNA repair proteins
2	125	InterPro	IPR035937	MutM-like, N-terminal
1	263	Hamap	MF_01253	Endonuclease 8 [nei].
1	263	InterPro	IPR023713	Endonuclease VIII
127	205	Pfam	PF06831	Formamidopyrimidine-DNA glycosylase H2TH domain
127	205	InterPro	IPR015886	DNA glycosylase/AP lyase, H2TH DNA-binding
1	103	Pfam	PF01149	Formamidopyrimidine-DNA glycosylase N-terminal domain
1	103	InterPro	IPR012319	Formamidopyrimidine-DNA glycosylase, catalytic domain
229	263	ProSiteProfiles	PS51066	Zinc finger FPG-type profile.
229	263	InterPro	IPR000214	Zinc finger, DNA glycosylase/AP lyase-type

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

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.074

Likely same site as FPocket 5 1.8 Å 9 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.046

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Surrounding area

Pocket 3 P2Rank #3

0.025

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Surrounding area

Pocket 4 P2Rank #4

0.015

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #5

0.243

Likely same site as P2Rank 1 1.8 Å 9 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:2-2 Schiff-base intermediate with DNA

UniProt: Active site:253-253 Proton donor; for delta-elimination activity

UniProt: Active site:3-3 Proton donor

UniProt: Active site:53-53 Proton donor; for beta-elimination activity

UniProt: Binding site:125-125

UniProt: Binding site:169-169

UniProt: Binding site:70-70

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.077

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Surrounding area

Pocket 2 P2Rank #2

0.024

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Surrounding area

Pocket 3 P2Rank #3

0.019

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Surrounding area

Pocket 4 P2Rank #4

0.016

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Surrounding area

Pocket 5 P2Rank #5

0.009

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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_A0A0H3GU47	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03284	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

2ON PDB via homolog 168.2 Da · LogP -0.07 · TPSA 74.4 Open detail RCSB PDB

5JL PDB via homolog Detail RCSB PDB

KB5 PDB via homolog Detail RCSB PDB

KBN PDB via homolog Detail RCSB PDB

KBQ 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
2ON RCSB PDB	6RO2	P42371	168.2 Da LogP -0.07 TPSA 74.4	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)C(=O)NC(=N2)S`
5JL RCSB PDB	6ROK	P42371	200.2 Da LogP 0.97 TPSA 80.2	✓ Ro5	✓ Clean	`C12=C(NC(=S)N1)NC(=S)NC2=O`
KB5 RCSB PDB	6RNM	P42371	167.2 Da LogP 0.22 TPSA 80.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)[nH]c(n2)S)N`
KBN RCSB PDB	6RNR	P42371	220.2 Da LogP 1.66 TPSA 54.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(nc(n2)C(F)(F)F)S`
KBQ RCSB PDB	6RNO	P42371	167.2 Da LogP 0.91 TPSA 64.4	✓ Ro5	✓ Clean	`c1c[nH]c2c1C(=O)NC(=S)N2`
KD8 RCSB PDB	6RP7	P42371	208.2 Da LogP 0.99 TPSA 74.4	✓ Ro5	✓ Clean	`Cc1c(nc2c(n1)C(=O)NC(=S)N2)C`
PED RCSB PDB	2OQ4	P50465	200.1 Da LogP -0.77 TPSA 107.2	✓ Ro5	✓ Clean	`CC[C@@H]([C@@H](COP(=O)(O)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).

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
ZINC5975509 ZINC	0.654	202.1 Da LogP -2.19 TPSA 127.5	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H](O)[C@H](O)CO`
ZINC5606355 ZINC	0.647	203.1 Da LogP 0.95 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(C(F)(F)F)nc2[nH]cnc12`
ZINC9974955 ZINC	0.625	215.0 Da LogP 0.41 TPSA 74.4	✓ Ro5	✓ Clean	`O=c1[nH]c(Br)nc2[nH]cnc12`
ZINC2384698 ZINC	0.621	244.2 Da LogP -0.14 TPSA 105.5	✓ Ro5	✓ Clean	`CCOC(OCC)[C@H](O)COP(=O)(O)O`
ZINC4521532 ZINC	0.621	244.2 Da LogP -0.14 TPSA 105.5	✓ Ro5	✓ Clean	`CCOC(OCC)[C@@H](O)COP(=O)(O)O`
ZINC4823831 ZINC	0.600	261.0 Da LogP 0.54 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1ncnc2[nH]c(I)nc12`
ZINC967449 ZINC	0.600	214.0 Da LogP 0.70 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1ncnc2[nH]c(Br)nc12`
ZINC96034425 ZINC	0.595	218.1 Da LogP 1.38 TPSA 63.7	✓ Ro5	✓ Clean	`COc1nc(C(F)(F)F)nc2[nH]cnc12`
ZINC2522549 ZINC	0.586	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`O=CC[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4543673 ZINC	0.586	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`O=CC[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC4543675 ZINC	0.586	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`O=CC[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC4543677 ZINC	0.586	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`O=CC[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC222362348 ZINC	0.583	360.4 Da LogP 4.33 TPSA 74.4	✓ Ro5	✓ Clean	`Cc1ccc(-c2nc3[nH]c(=S)[nH]c(=O)c3nc2-c2ccc(C)cc…`
ZINC4726700 ZINC	0.579	231.2 Da LogP 1.80 TPSA 66.5	✓ Ro5	✓ Clean	`CCNc1nc(C(F)(F)F)nc2[nH]cnc12`
ZINC17919967 ZINC	0.563	207.3 Da LogP 1.28 TPSA 80.5	✓ Ro5	✓ Clean	`Cc1nc2[nH]c(=S)nc(N)c2nc1C`
ZINC1532601 ZINC	0.552	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC2516111 ZINC	0.552	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)CO`
ZINC2522704 ZINC	0.552	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC32786787 ZINC	0.552	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3869812 ZINC	0.552	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC8614702 ZINC	0.545	216.3 Da LogP 2.34 TPSA 63.2	✓ Ro5	✓ Clean	`S=c1[nH]c(=S)c2[nH]c(=S)[nH]c2[nH]1`
ZINC301097517 ZINC	0.537	271.2 Da LogP 2.36 TPSA 57.7	✓ Ro5	✓ Clean	`FC(F)(F)c1nc(N2CCCCC2)c2nc[nH]c2n1`
ZINC4707273 ZINC	0.537	279.2 Da LogP 3.12 TPSA 66.5	✓ Ro5	✓ Clean	`FC(F)(F)c1nc(Nc2ccccc2)c2nc[nH]c2n1`
ZINC240333519 ZINC	0.524	285.3 Da LogP 3.12 TPSA 66.5	✓ Ro5	✓ Clean	`FC(F)(F)c1nc(NC2CCCCC2)c2nc[nH]c2n1`
ZINC252550334 ZINC	0.524	273.3 Da LogP 2.97 TPSA 66.5	✓ Ro5	✓ Clean	`CCC(CC)Nc1nc(C(F)(F)F)nc2[nH]cnc12`
ZINC4726481 ZINC	0.524	259.2 Da LogP 2.58 TPSA 66.5	✓ Ro5	✓ Clean	`CCCCNc1nc(C(F)(F)F)nc2[nH]cnc12`
ZINC514864831 ZINC	0.524	278.2 Da LogP 1.55 TPSA 91.8	✓ Ro5	✓ Clean	`O=C(O)CSc1nc(C(F)(F)F)nc2[nH]cnc12`
ZINC1529626 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1530556 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532567 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532851 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC22116391 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC30320708 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC3606137 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3869426 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC3870277 ZINC	0.516	310.1 Da LogP -2.50 TPSA 191.0	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC8551307 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC8551308 ZINC	0.516	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1556567 ZINC	0.514	211.3 Da LogP 0.95 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1ncnc2nc(S)[nH]c(=S)c12`
ZINC1670205 ZINC	0.514	213.2 Da LogP -0.66 TPSA 114.6	✓ Ro5	✓ Clean	`CS(=O)(=O)c1nc2c(N)ncnc2[nH]1`
ZINC2486839 ZINC	0.514	215.2 Da LogP -0.82 TPSA 134.8	✓ Ro5	✓ Clean	`Nc1ncnc2[nH]c(S(=O)(=O)O)nc12`
ZINC4773403 ZINC	0.514	211.2 Da LogP 1.60 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1ncnc2[nH]c(-c3ccccc3)nc12`
ZINC6556466 ZINC	0.514	222.3 Da LogP 1.00 TPSA 63.6	✓ Ro5	✓ Clean	`Cc1nc2[nH]c(=S)n(C)c(=O)c2nc1C`
ZINC5729093 ZINC	0.514	332.4 Da LogP 3.71 TPSA 74.4	✓ Ro5	✓ Clean	`O=c1[nH]c(=S)[nH]c2nc(-c3ccccc3)c(-c3ccccc3)nc12`
ZINC301069237 ZINC	0.512	273.2 Da LogP 1.21 TPSA 66.9	✓ Ro5	✓ Clean	`FC(F)(F)c1nc(N2CCOCC2)c2nc[nH]c2n1`
ZINC4726480 ZINC	0.512	293.3 Da LogP 2.98 TPSA 66.5	✓ Ro5	✓ Clean	`FC(F)(F)c1nc(NCc2ccccc2)c2nc[nH]c2n1`
ZINC167345032 ZINC	0.500	217.2 Da LogP 1.04 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1ncnc2[nH]c(CC(F)(F)F)nc12`
ZINC186096 ZINC	0.500	209.3 Da LogP 1.44 TPSA 80.5	✓ Ro5	✓ Clean	`CC(C)Sc1nc2c(N)ncnc2[nH]1`
ZINC222362492 ZINC	0.500	368.4 Da LogP 3.99 TPSA 74.4	✓ Ro5	✓ Clean	`O=c1[nH]c(=S)[nH]c2nc(-c3ccc(F)cc3)c(-c3ccc(F)c…`
ZINC238628781 ZINC	0.500	213.2 Da LogP 0.71 TPSA 87.3	✓ Ro5	✓ Clean	`O=c1[nH]c(-c2ccccn2)nc2[nH]cnc12`

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.

Cross-references

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

Sequence

UniProt A0A0H3GU47

Endonuclease 8 bifunctional protein

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

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence