Overview
Basic information about this protein and its source genome.
- Accession
- PA5422
- Gene
- PA5422
- Status
- annotated
- Amino acids
- 318
- 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.
Enzyme Commission (EC)
1Gene Ontology (GO)
7- GO:0030246 Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
- GO:0047938 Catalysis of the reaction: alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate.
- GO:0008976 Catalysis of the reaction: ATP + phosphate(n) = ADP + phosphate(n+1).
- GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
- GO:0006798 The chemical reactions and pathways resulting in the breakdown of a polyphosphate, the anion or salt of polyphosphoric acid.
- GO:0016853 Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
- 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.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 36 | 311 | Pfam | PF01263 | Aldose 1-epimerase |
| 36 | 311 | InterPro | IPR008183 | Aldose 1-/Glucose-6-phosphate 1-epimerase |
| 21 | 309 | SUPERFAMILY | SSF74650 | Galactose mutarotase-like |
| 21 | 309 | InterPro | IPR011013 | Galactose mutarotase-like domain superfamily |
| 39 | 292 | PANTHER | PTHR11122 | APOSPORY-ASSOCIATED PROTEIN C-RELATED |
| 9 | 312 | PIRSF | PIRSF016020 | PHexose_mutarotase |
| 9 | 312 | InterPro | IPR025532 | Glucose-6-phosphate 1-epimerase |
| 9 | 311 | Gene3D | G3DSA:2.70.98.10 | - |
| 9 | 311 | InterPro | IPR014718 | Glycoside hydrolase-type carbohydrate-binding |
| 33 | 310 | CDD | cd09020 | D-hex-6-P-epi_like |
| 33 | 310 | InterPro | IPR025532 | Glucose-6-phosphate 1-epimerase |
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
PA5422
|
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.755 |