Overview
Basic information about this protein and its source genome.
- Accession
- PA1193
- Gene
- PA1193
- Status
- annotated
- Amino acids
- 223
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- Cytoplasmic
Selected Druggability evidence
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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
4- GO:0008725 Catalysis of the reaction: DNA containing 3-methyladenine + H2O = DNA with abasic site + 3-methyladenine. This reaction is the hydrolysis of DNA by cleavage of the N-C1' glycosidic bond between the damaged DNA 3-methyladenine and the deoxyribose sugar to remove the 3-methyladenine, leaving an abasic site.
- 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:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- 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.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 37 | 182 | SUPERFAMILY | SSF48150 | DNA-glycosylase |
| 37 | 182 | InterPro | IPR011257 | DNA glycosylase |
| 34 | 151 | Gene3D | G3DSA:1.10.340.30 | Hypothetical protein; domain 2 |
| 1 | 181 | PANTHER | PTHR30037 | DNA-3-METHYLADENINE GLYCOSYLASE 1 |
| 39 | 131 | Pfam | PF03352 | Methyladenine glycosylase |
| 39 | 131 | InterPro | IPR005019 | Methyladenine glycosylase |
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...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA1193
|
AlphaFold | — | — | full sequence | — | Viewing |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
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 |
|---|---|---|---|---|---|---|---|
| 3 | 0.96 | ||||||
| 1 | 0.932 | ||||||
| 2 | 0.566 |
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.
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 |
|---|---|---|---|---|---|---|
| ADK | P05100 | 149.2 Da LogP -0.10 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
Cn1cnc(c-2ncnc12)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 |
|---|---|---|---|---|---|---|
| CHEMBL2296739 | P05100 | 6.40 | 225.3 Da LogP 1.41 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
Nc1ncn(Cc2ccccc2)c2ncnc1-2
|
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 |
|---|---|---|---|---|---|
| ZINC100200850 | 1.000 | 225.3 Da LogP 1.41 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
Nc1ncn(Cc2ccccc2)c2ncnc1-2
|
| ZINC172593 | 0.578 | 347.4 Da LogP 3.70 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
Nc1ncn(Cc2ccccc2)c2nc(SCc3ccccc3)nc1-2
|
| ZINC213544 | 0.565 | 285.4 Da LogP 2.52 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
CCSc1nc2c(N)ncn(Cc3ccccc3)c-2n1
|
| ZINC203076 | 0.561 | 225.3 Da LogP 1.46 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2Cc1ccccc1
|
| ZINC330551 | 0.558 | 240.3 Da LogP 0.84 TPSA 60.6 | ✓ Ro5 | ✓ Clean |
C[n+]1cnc2n(Cc3ccccc3)cnc(N)c1-2
|
| ZINC2858288 | 0.553 | 299.4 Da LogP 2.91 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
CC(C)Sc1nc2c(N)ncn(Cc3ccccc3)c-2n1
|
| ZINC2502928 | 0.542 | 301.4 Da LogP 1.49 TPSA 89.8 | ✓ Ro5 | ✓ Clean |
Nc1ncn(Cc2ccccc2)c2nc(SCCO)nc1-2
|
| ZINC4178551 | 0.542 | 315.4 Da LogP 1.59 TPSA 106.9 | ✓ Ro5 | ✓ Clean |
Nc1ncn(Cc2ccccc2)c2nc(SCC(=O)O)nc1-2
|
| ZINC20281793 | 0.538 | 249.3 Da LogP 3.18 TPSA 43.8 | ✓ Ro5 | ✓ Clean |
Nc1c(-c2ccccc2)ncn1Cc1ccccc1
|
| ZINC2209 | 0.514 | 203.2 Da LogP 1.33 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
CC(C)=CCn1cnc(N)c2ncnc1-2
|
| ZINC2854042 | 0.510 | 377.5 Da LogP 3.58 TPSA 78.8 | ✓ Ro5 | ✓ Clean |
Nc1ncn(Cc2ccccc2)c2nc(SCCOc3ccccc3)nc1-2
|
| ZINC1718931 | 0.500 | 239.3 Da LogP 1.72 TPSA 69.6 | ✓ Ro5 | ✓ Clean |
Cc1ccc(Cn2cnc(N)c3ncnc2-3)cc1
|
| ZINC38284775 | 0.500 | 245.3 Da LogP 1.69 TPSA 70.1 | ✓ Ro5 | ✓ Clean |
CCOC(=O)c1c(N)ncn1Cc1ccccc1
|
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.