Amino acids
270
Annotations
15
Features
32
PDB binders
7
Druggability
0.216
Overview
Basic information about this protein and its source genome.
- Accession
- PA0357
- Gene
- fpg PA0357 mutM
- Status
- annotated
- Amino acids
- 270
- Structure source
- AlphaFold
GO
GO:0034039 Catalysis of the removal of 8-oxo-7,8-dihydroguanine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar.
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: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:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0008270 Binding to a zinc ion (Zn).
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.
FPocket
0.216
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
2 EC
13 GO
Gene Ontology (GO)
13- GO:0034039 Catalysis of the removal of 8-oxo-7,8-dihydroguanine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar.
- 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: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:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
- GO:0008270 Binding to a zinc ion (Zn).
- 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: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:0016799 Catalysis of the hydrolysis of any N-glycosyl bond.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0003676 Binding to a nucleic acid.
- 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:0008534 Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate 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 apurinic (AP) site.
Sequence Features
Domain/signature hits from InterPro and related databases.
32 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 132 | 270 | FunFam | G3DSA:1.10.8.50:FF:000003 | Formamidopyrimidine-DNA glycosylase |
| 2 | 117 | CDD | cd08966 | EcFpg-like_N |
| 2 | 129 | FunFam | G3DSA:3.20.190.10:FF:000001 | Formamidopyrimidine-DNA glycosylase |
| 1 | 269 | NCBIfam | TIGR00577 | DNA-formamidopyrimidine glycosylase |
| 1 | 269 | InterPro | IPR020629 | Formamidopyrimidine-DNA glycosylase |
| 131 | 222 | SUPERFAMILY | SSF46946 | S13-like H2TH domain |
| 131 | 222 | InterPro | IPR010979 | Ribosomal protein S13-like, H2TH |
| 242 | 269 | Pfam | PF06827 | Zinc finger found in FPG and IleRS |
| 242 | 269 | InterPro | IPR010663 | Zinc finger, FPG/IleRS-type |
| 1 | 270 | Hamap | MF_00103 | Formamidopyrimidine-DNA glycosylase [mutM]. |
| 1 | 270 | InterPro | IPR020629 | Formamidopyrimidine-DNA glycosylase |
| 2 | 128 | Gene3D | G3DSA:3.20.190.10 | - |
| 2 | 128 | InterPro | IPR035937 | MutM-like, N-terminal |
| 2 | 113 | ProSiteProfiles | PS51068 | Formamidopyrimidine-DNA glycosylase catalytic domain profile. |
| 2 | 113 | InterPro | IPR012319 | Formamidopyrimidine-DNA glycosylase, catalytic domain |
| 236 | 270 | ProSiteProfiles | PS51066 | Zinc finger FPG-type profile. |
| 236 | 270 | InterPro | IPR000214 | Zinc finger, DNA glycosylase/AP lyase-type |
| 218 | 269 | SUPERFAMILY | SSF57716 | Glucocorticoid receptor-like (DNA-binding domain) |
| 245 | 269 | ProSitePatterns | PS01242 | Zinc finger FPG-type signature. |
| 245 | 269 | InterPro | IPR015887 | DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site |
| 1 | 115 | Pfam | PF01149 | Formamidopyrimidine-DNA glycosylase N-terminal domain |
| 1 | 115 | InterPro | IPR012319 | Formamidopyrimidine-DNA glycosylase, catalytic domain |
| 130 | 222 | SMART | SM01232 | H2TH_2 |
| 130 | 222 | InterPro | IPR015886 | DNA glycosylase/AP lyase, H2TH DNA-binding |
| 2 | 135 | SUPERFAMILY | SSF81624 | N-terminal domain of MutM-like DNA repair proteins |
| 2 | 135 | InterPro | IPR035937 | MutM-like, N-terminal |
| 130 | 220 | Pfam | PF06831 | Formamidopyrimidine-DNA glycosylase H2TH domain |
| 130 | 220 | InterPro | IPR015886 | DNA glycosylase/AP lyase, H2TH DNA-binding |
| 1 | 270 | PANTHER | PTHR22993 | FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE |
| 132 | 270 | Gene3D | G3DSA:1.10.8.50 | - |
| 2 | 116 | SMART | SM00898 | Fapy_DNA_glyco_2 |
| 2 | 116 | InterPro | IPR012319 | Formamidopyrimidine-DNA glycosylase, catalytic domain |
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...
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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
PA0357
|
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 |
|---|---|---|---|---|---|---|---|
| 2 | 0.216 |
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
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 |
|---|---|---|---|---|---|---|
| 2ON | P42371 | 168.2 Da LogP -0.07 TPSA 74.4 | ✓ Ro5 | ✓ Clean |
c1[nH]c2c(n1)C(=O)NC(=N2)S
|
|
| 5JL | P42371 | 200.2 Da LogP 0.97 TPSA 80.2 | ✓ Ro5 | ✓ Clean |
C12=C(NC(=S)N1)NC(=S)NC2=O
|
|
| KB5 | P42371 | 167.2 Da LogP 0.22 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
c1nc(c2c(n1)[nH]c(n2)S)N
|
|
| KBN | 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 | P42371 | 167.2 Da LogP 0.91 TPSA 64.4 | ✓ Ro5 | ✓ Clean |
c1c[nH]c2c1C(=O)NC(=S)N2
|
|
| KD8 | P42371 | 208.2 Da LogP 0.99 TPSA 74.4 | ✓ Ro5 | ✓ Clean |
Cc1c(nc2c(n1)C(=O)NC(=S)N2)C
|
|
| PED | 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 | 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 | 0.647 | 203.1 Da LogP 0.95 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
Nc1nc(C(F)(F)F)nc2[nH]cnc12
|
| ZINC9974955 | 0.625 | 215.0 Da LogP 0.41 TPSA 74.4 | ✓ Ro5 | ✓ Clean |
O=c1[nH]c(Br)nc2[nH]cnc12
|
| ZINC2384698 | 0.621 | 244.2 Da LogP -0.14 TPSA 105.5 | ✓ Ro5 | ✓ Clean |
CCOC(OCC)[C@H](O)COP(=O)(O)O
|
| ZINC4521532 | 0.621 | 244.2 Da LogP -0.14 TPSA 105.5 | ✓ Ro5 | ✓ Clean |
CCOC(OCC)[C@@H](O)COP(=O)(O)O
|
| ZINC4823831 | 0.600 | 261.0 Da LogP 0.54 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2[nH]c(I)nc12
|
| ZINC967449 | 0.600 | 214.0 Da LogP 0.70 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2[nH]c(Br)nc12
|
| ZINC96034425 | 0.595 | 218.1 Da LogP 1.38 TPSA 63.7 | ✓ Ro5 | ✓ Clean |
COc1nc(C(F)(F)F)nc2[nH]cnc12
|
| ZINC2522549 | 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 | 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 | 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 | 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 | 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 | 0.579 | 231.2 Da LogP 1.80 TPSA 66.5 | ✓ Ro5 | ✓ Clean |
CCNc1nc(C(F)(F)F)nc2[nH]cnc12
|
| ZINC17919967 | 0.563 | 207.3 Da LogP 1.28 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
Cc1nc2[nH]c(=S)nc(N)c2nc1C
|
| ZINC1532601 | 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 | 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 | 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 | 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 | 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 | 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 | 0.537 | 271.2 Da LogP 2.36 TPSA 57.7 | ✓ Ro5 | ✓ Clean |
FC(F)(F)c1nc(N2CCCCC2)c2nc[nH]c2n1
|
| ZINC4707273 | 0.537 | 279.2 Da LogP 3.12 TPSA 66.5 | ✓ Ro5 | ✓ Clean |
FC(F)(F)c1nc(Nc2ccccc2)c2nc[nH]c2n1
|
| ZINC240333519 | 0.524 | 285.3 Da LogP 3.12 TPSA 66.5 | ✓ Ro5 | ✓ Clean |
FC(F)(F)c1nc(NC2CCCCC2)c2nc[nH]c2n1
|
| ZINC252550334 | 0.524 | 273.3 Da LogP 2.97 TPSA 66.5 | ✓ Ro5 | ✓ Clean |
CCC(CC)Nc1nc(C(F)(F)F)nc2[nH]cnc12
|
| ZINC4726481 | 0.524 | 259.2 Da LogP 2.58 TPSA 66.5 | ✓ Ro5 | ✓ Clean |
CCCCNc1nc(C(F)(F)F)nc2[nH]cnc12
|
| ZINC514864831 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 0.514 | 211.3 Da LogP 0.95 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2nc(S)[nH]c(=S)c12
|
| ZINC1670205 | 0.514 | 213.2 Da LogP -0.66 TPSA 114.6 | ✓ Ro5 | ✓ Clean |
CS(=O)(=O)c1nc2c(N)ncnc2[nH]1
|
| ZINC2486839 | 0.514 | 215.2 Da LogP -0.82 TPSA 134.8 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2[nH]c(S(=O)(=O)O)nc12
|
| ZINC4773403 | 0.514 | 211.2 Da LogP 1.60 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2[nH]c(-c3ccccc3)nc12
|
| ZINC6556466 | 0.514 | 222.3 Da LogP 1.00 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
Cc1nc2[nH]c(=S)n(C)c(=O)c2nc1C
|
| ZINC5729093 | 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 | 0.512 | 273.2 Da LogP 1.21 TPSA 66.9 | ✓ Ro5 | ✓ Clean |
FC(F)(F)c1nc(N2CCOCC2)c2nc[nH]c2n1
|
| ZINC4726480 | 0.512 | 293.3 Da LogP 2.98 TPSA 66.5 | ✓ Ro5 | ✓ Clean |
FC(F)(F)c1nc(NCc2ccccc2)c2nc[nH]c2n1
|
| ZINC167345032 | 0.500 | 217.2 Da LogP 1.04 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2[nH]c(CC(F)(F)F)nc12
|
| ZINC186096 | 0.500 | 209.3 Da LogP 1.44 TPSA 80.5 | ✓ Ro5 | ✓ Clean |
CC(C)Sc1nc2c(N)ncnc2[nH]1
|
| ZINC222362492 | 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 | 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.