Amino acids
543
Annotations
4
Features
32
PDB binders
0
Druggability
0.516
Overview
Basic information about this protein and its source genome.
- Accession
- PA3545
- Gene
- PA3545 algG
- Status
- annotated
- Amino acids
- 543
- Structure source
- AlphaFold
EC
GO
GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
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:0042121 The chemical reactions and pathways resulting in the formation of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- Periplasmic
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
0.516
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
3 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
3- GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
- 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:0042121 The chemical reactions and pathways resulting in the formation of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
Sequence Features
Domain/signature hits from InterPro and related databases.
32 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 35 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 262 | 422 | SMART | SM00722 | complete |
| 262 | 422 | InterPro | IPR006633 | Carbohydrate-binding/sugar hydrolysis domain |
| 20 | 543 | NCBIfam | NF038177 | mannuronan 5-epimerase AlgG |
| 1 | 35 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 283 | 304 | SMART | SM00710 | pbh1 |
| 283 | 304 | InterPro | IPR006626 | Parallel beta-helix repeat |
| 329 | 352 | SMART | SM00710 | pbh1 |
| 329 | 352 | InterPro | IPR006626 | Parallel beta-helix repeat |
| 354 | 376 | SMART | SM00710 | pbh1 |
| 354 | 376 | InterPro | IPR006626 | Parallel beta-helix repeat |
| 401 | 423 | SMART | SM00710 | pbh1 |
| 401 | 423 | InterPro | IPR006626 | Parallel beta-helix repeat |
| 243 | 270 | SMART | SM00710 | pbh1 |
| 243 | 270 | InterPro | IPR006626 | Parallel beta-helix repeat |
| 305 | 327 | SMART | SM00710 | pbh1 |
| 305 | 327 | InterPro | IPR006626 | Parallel beta-helix repeat |
| 378 | 400 | SMART | SM00710 | pbh1 |
| 378 | 400 | InterPro | IPR006626 | Parallel beta-helix repeat |
| 1 | 18 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 76 | 499 | Gene3D | G3DSA:2.160.20.10 | - |
| 76 | 499 | InterPro | IPR012334 | Pectin lyase fold |
| 164 | 465 | SUPERFAMILY | SSF51126 | Pectin lyase-like |
| 164 | 465 | InterPro | IPR011050 | Pectin lyase fold/virulence factor |
| 19 | 30 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 35 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 288 | 438 | Pfam | PF05048 | Periplasmic copper-binding protein (NosD) |
| 288 | 438 | InterPro | IPR007742 | Periplasmic copper-binding protein NosD, beta helix domain |
| 31 | 35 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 36 | 543 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 395 | 437 | NCBIfam | TIGR03804 | parallel beta-helix repeat (two copies) |
| 395 | 437 | InterPro | IPR022441 | Parallel beta-helix repeat-2 |
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
PA3545
|
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 |
|---|---|---|---|---|---|---|---|
| 4 | 0.516 | ||||||
| 7 | 0.208 | ||||||
| 2 | 0.203 |