Protein profile
VK055_4362
5'-3' exonuclease, C-terminal SAM fold family protein
Genome: KpATCC43816
Overview
Basic information about this protein and its source genome.
- Accession
- VK055_4362
- Gene
- AIK82905.1
- Status
- annotated
- Amino acids
- 251
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- DEG identity (%)
- 34.286
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 95.71
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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.
Enzyme Commission (EC)
1Gene Ontology (GO)
8- GO:0017108 Catalysis of the cleavage of a 5' flap structure in DNA, but not other DNA structures; processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis.
- 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:0033567 The DNA metabolic process, occurring during lagging strand synthesis, by which RNA primers are removed from Okazaki fragments, the resulting gaps filled by DNA polymerization, and the ends ligated to form a continuous strand.
- GO:0048256 Catalysis of the cleavage of a flap structure in DNA, but not other DNA structures; processes the ends of Okazaki fragments in lagging strand DNA synthesis.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0008409 Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 5' end.
- GO:0000287 Binding to a magnesium (Mg) ion.
- GO:0030955 Binding to a potassium ion (K+).
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 190 | 210 | Coils | Coil | Coil |
| 162 | 251 | FunFam | G3DSA:1.10.150.20:FF:000003 | DNA polymerase I |
| 162 | 234 | CDD | cd09898 | H3TH_53EXO |
| 162 | 234 | InterPro | IPR020045 | DNA polymerase I-like, H3TH domain |
| 4 | 240 | PANTHER | PTHR42646 | FLAP ENDONUCLEASE XNI |
| 4 | 240 | InterPro | IPR038969 | Flap endonuclease |
| 1 | 19 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 160 | 250 | Pfam | PF01367 | 5'-3' exonuclease, C-terminal SAM fold |
| 160 | 250 | InterPro | IPR020045 | DNA polymerase I-like, H3TH domain |
| 2 | 251 | Hamap | MF_01192 | Flap endonuclease Xni [xni]. |
| 2 | 251 | InterPro | IPR022895 | Flap endonuclease Xni |
| 1 | 161 | Gene3D | G3DSA:3.40.50.1010 | - |
| 162 | 197 | SMART | SM00279 | HhH_4 |
| 162 | 197 | InterPro | IPR008918 | Helix-hairpin-helix motif, class 2 |
| 162 | 251 | Gene3D | G3DSA:1.10.150.20 | - |
| 160 | 243 | SUPERFAMILY | SSF47807 | 5' to 3' exonuclease, C-terminal subdomain |
| 160 | 243 | InterPro | IPR036279 | 5'-3' exonuclease, C-terminal domain superfamily |
| 4 | 159 | SUPERFAMILY | SSF88723 | PIN domain-like |
| 4 | 159 | InterPro | IPR029060 | PIN-like domain superfamily |
| 7 | 154 | CDD | cd09859 | PIN_53EXO |
| 1 | 161 | FunFam | G3DSA:3.40.50.1010:FF:000011 | Flap endonuclease Xni |
| 3 | 250 | SMART | SM00475 | 53exo3 |
| 3 | 250 | InterPro | IPR002421 | 5'-3' exonuclease |
| 5 | 151 | Pfam | PF02739 | 5'-3' exonuclease, N-terminal resolvase-like domain |
| 5 | 151 | InterPro | IPR020046 | 5'-3' exonuclease, alpha-helical arch, N-terminal |
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 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GWW8
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
VK055_4362
|
ColabFold | — | — | full sequence | — | Loaded |
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 |
|---|---|---|---|---|---|---|---|
| 8 | 0.538 | ||||||
| 1 | 0.364 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 16.52 | 0.78 | ||||||
| 2 | 2.14 | 0.05 | ||||||
| 3 | 1.48 | 0.021 | ||||||
| 4 | 1.0 | 0.006 |
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 | 0.423 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 16.95 | 0.792 | ||||||
| 2 | 0.77 | 0.002 |
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.
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 |
|---|---|---|---|---|---|
| ZINC4521259 | 1.000 | 282.3 Da LogP -4.01 TPSA 145.4 | 1 viol. | ✓ Clean |
OCC(CO)(CO)NCCCNC(CO)(CO)CO
|
| ZINC115591405 | 0.636 | 373.6 Da LogP 4.55 TPSA 72.7 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCCCCCNC(CO)(CO)CO
|
| ZINC115591837 | 0.636 | 317.5 Da LogP 2.99 TPSA 72.7 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCNC(CO)(CO)CO
|
| ZINC143575268 | 0.636 | 289.5 Da LogP 2.21 TPSA 72.7 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCNC(CO)(CO)CO
|
| ZINC2322313 | 0.636 | 233.4 Da LogP 0.65 TPSA 72.7 | ✓ Ro5 | ✓ Clean |
CCCCCCCCNC(CO)(CO)CO
|
| ZINC97996983 | 0.636 | 345.6 Da LogP 3.77 TPSA 72.7 | ✓ Ro5 | ✓ Clean |
CCCCCCCCCCCCCCCCNC(CO)(CO)CO
|
| ZINC1611594 | 0.583 | 243.3 Da LogP -2.43 TPSA 127.1 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCNC(CO)(CO)CO
|
| ZINC5273895 | 0.583 | 257.3 Da LogP -2.04 TPSA 127.1 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCCNC(CO)(CO)CO
|
| ZINC114433005 | 0.571 | 231.9 Da LogP 1.58 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
CC(Br)(Br)C(=O)O
|
| ZINC98087485 | 0.533 | 228.3 Da LogP 2.54 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
CC(C)(C)/C(C(=O)O)=C(\C(=O)O)C(C)(C)C
|
| ZINC104203687 | 0.500 | 202.2 Da LogP 1.17 TPSA 99.3 | ✓ Ro5 | Alert |
CC(C)(/N=N\C(C)(C)C(=O)O)C(=O)O
|
| ZINC104203691 | 0.500 | 202.2 Da LogP 1.17 TPSA 99.3 | ✓ Ro5 | Alert |
CC(C)(/N=N/C(C)(C)C(=O)O)C(=O)O
|
| ZINC1530141 | 0.500 | 229.3 Da LogP -2.82 TPSA 127.1 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCNC(CO)(CO)CO
|
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.