KpKP13 Protein target profile

hypothetical protein

Accession: KP13_01082

Gene: AHE42525.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3H3F9
Length 351
Pocket druggability (P2Rank · AlphaFold DB model) 0.86
Functional annotation 0 EC 0 GO
Target summary

Promising target candidate with multiple supporting evidence streams.

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
1.3% 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
84.37 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) 0.86
Structure A0A0H3H3F9
Pocket Pocket 1
Druggability (FPocket) 0.855
Structure A0A0H3H3F9
Pocket Pocket 2
ColabFold model
P2Rank 0.864 · Pocket 1
FPocket 0.837 · Pocket 2
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 63 / 4744 genomes with a hit
Prevalence 1.3%

Sequence

Primary amino-acid sequence viewer.

MLGNAMAGQSSSQAASPFQWWKPALFFLVVIVGLWYVKWQPYYGKAFTAAETHSIGKSILAQADANPLMAAWDYAMVYFLAVWKAAVLGVLLGSLIQVLIPRNWLLRTLGQSRFQGTLLGAIFSLPGMMCTCCAAPVAAGMRKQQVSMGGALAFWMGNPLLNPATLVFMGFVLGWQFALVRLVAGLATVLTVATLVQKWVKEAATQPVAVPAAPSEATQGGFFSRWLRALWTLFWNTIPVYILAVLVLGAARVWLFPHADGVVDNTLFWVIAMAIAGCLFVIPTAAEIPIVQTMMLAGMGTAPALALLITLPAVSVPSLIMLRKAFPAKALWLTGGLVALCGAIVGALALV

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

Subcellular localization

Localization
CytoplasmicMembrane

No GO or EC annotations are currently loaded for this protein.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

31 records
Show feature table
Start End DB Term Name
25 209 PANTHER PTHR43299 UPF0718 PROTEIN YRAQ
178 196 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
312 330 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
38 76 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1 19 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
197 232 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
173 177 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
287 292 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
177 196 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
77 100 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
269 291 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
351 351 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
116 138 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
293 311 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
101 119 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
79 101 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
298 320 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
151 173 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
20 37 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
233 255 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
151 172 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
20 37 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
140 150 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
330 350 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
232 254 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
267 286 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
256 266 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
120 139 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
80 347 Pfam PF03773 Predicted permease
80 347 InterPro IPR005524 Predicted permease DUF318
331 350 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.

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
0.86
Likely same site as FPocket 2 0.8 Å 18 shared residues 100% of smaller site
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Surrounding area
Pocket 2 P2Rank #2
0.182
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Surrounding area
Pocket 3 P2Rank #3
0.105
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Surrounding area
Pocket 4 P2Rank #4
0.042
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Surrounding area
Pocket 5 P2Rank #5
0.013
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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 #2
0.855
Likely same site as P2Rank 1 0.8 Å 18 shared residues 100% of smaller site
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Surrounding area
Pocket 2 FPocket #31
0.343
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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_A0A0H3H3F9
AlphaFold DB full sequence Viewing
ColabFold KP13_01082
ColabFold full sequence Loaded

Cross-references

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