KpATCC43816 Protein target profile

exonuclease family protein

Accession: VK055_0088

Gene: AIK78716.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GQ46
Length 219
Pocket druggability (P2Rank · AlphaFold DB model) 0.787
Functional annotation 0 EC 4 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
No hit
Gut microbiome similarity
1.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
N
DEG identity (%)
36.667 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT
94.96 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) 0.787
Structure A0A0H3GQ46
Pocket Pocket 1
Druggability (FPocket) 0.447
Structure A0A0H3GQ46
Pocket Pocket 3
ColabFold model
P2Rank 0.761 · Pocket 1
FPocket 0.478 · Pocket 1
Core conservation Accessory gene
Roary core
CoreCruncher accessory
Gut microbiome 87 / 4744 genomes with a hit
Prevalence 1.8%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLRVIDTETCGLQGGIVEIASVDIVDGQITNPMSHLVRPDRPISPQAMAIHRITEEMVADKPWIEEIIPHYHGSPWYVAHNASFDRRVLPEMHGEWICTMKLARRLWPGIKYSNMGLYKSRKLNVTTPPGLHHHRALYDCYITAALLLDIINVSGWPPDEMADITGRPALLTTFTFGKYRGKAVAEIAENDPGYLRWLFNNLDRMSPELRLTLRHYLGE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization
Cytoplasmic

Gene Ontology (GO)

4
  • GO:0003676 Binding to a nucleic acid.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0008408 Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
  • GO:0045004 Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

12 records
Show feature table
Start End DB Term Name
4 184 SUPERFAMILY SSF53098 Ribonuclease H-like
4 184 InterPro IPR012337 Ribonuclease H-like superfamily
1 171 Gene3D G3DSA:3.30.420.10 -
1 171 InterPro IPR036397 Ribonuclease H superfamily
174 203 Pfam PF20600 Exodeoxyribonuclease X-like C-terminal
174 203 InterPro IPR046768 Exodeoxyribonuclease X-like, C-terminal
4 148 CDD cd06127 DEDDh
4 156 PANTHER PTHR30231 DNA POLYMERASE III SUBUNIT EPSILON
1 156 SMART SM00479 exoiiiendus
1 156 InterPro IPR013520 Exonuclease, RNase T/DNA polymerase III
4 147 Pfam PF00929 Exonuclease
4 147 InterPro IPR013520 Exonuclease, RNase T/DNA polymerase III

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

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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
0.787
Likely same site as FPocket 3 5.6 Å 10 shared residues 83% of smaller site
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Surrounding area
Pocket 2 P2Rank #2
0.041
Likely same site as FPocket 1 3.6 Å 9 shared residues 90% of smaller site
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Surrounding area
Pocket 3 P2Rank #3
0.024
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Surrounding area
Pocket 4 P2Rank #4
0.001
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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 #3
0.447
Likely same site as P2Rank 1 5.6 Å 10 shared residues 83% of smaller site
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Surrounding area
Pocket 2 FPocket #1
0.289 Unusual size
Likely same site as P2Rank 2 3.6 Å 9 shared residues 90% of smaller site
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_A0A0H3GQ46
AlphaFold DB full sequence Viewing
ColabFold VK055_0088
ColabFold full sequence Loaded

Cross-references

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