Overview
Basic information about this protein and its source genome.
- Accession
- PA3547
- Gene
- PA3547 algL
- Status
- annotated
- Amino acids
- 367
- Structure source
- Experimental + AlphaFold
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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
6- 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:0045135 Catalysis of the reaction: polysaccharides containing beta-D-mannuronate residues = oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl end. This reaction is the eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends.
- GO:0004794 Catalysis of the reaction: L-threonine = 2-oxobutanoate + NH4.
- 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).
- GO:0042122 The chemical reactions and pathways resulting in the breakdown of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
- GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 28 | 367 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 1 | 27 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 9 | 20 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 63 | 303 | Pfam | PF05426 | Alginate lyase |
| 63 | 303 | InterPro | IPR008397 | Alginate lyase domain |
| 28 | 362 | FunFam | G3DSA:1.50.10.100:FF:000002 | Alginate lyase |
| 1 | 8 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 28 | 362 | Gene3D | G3DSA:1.50.10.100 | Chondroitin AC/alginate lyase |
| 28 | 362 | InterPro | IPR008929 | Chondroitin AC/alginate lyase |
| 30 | 361 | SUPERFAMILY | SSF48230 | Chondroitin AC/alginate lyase |
| 30 | 361 | InterPro | IPR008929 | Chondroitin AC/alginate lyase |
| 5 | 367 | Hamap | MF_00557 | Alginate lyase [algL]. |
| 5 | 367 | InterPro | IPR022859 | Alginate lyase |
| 1 | 27 | SignalP_GRAM_NEGATIVE | SignalP-noTM | SignalP-noTM |
| 21 | 27 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 24 | 361 | CDD | cd00244 | AlgLyase |
| 24 | 361 | InterPro | IPR022859 | Alginate lyase |
| 1 | 27 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
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
3 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
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 | 0.607 |
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 | 41.14 | 0.965 | ||||||
| 2 | 0.83 | 0.003 |
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 | 0.615 |
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.
| Ligand | Source crystal | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| BEM | 194.1 Da LogP -3.13 TPSA 127.5 | ✓ Ro5 | ✓ Clean |
[C@@H]1([C@@H]([C@H](O[C@H]([C@H]1O)O)C(=O)O)O)O
|
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.
No PDB ligands found through similar proteins.
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 |
|---|---|---|---|---|---|
| ZINC39944742 | 0.655 | 370.3 Da LogP -5.21 TPSA 223.7 | 2 viol. | ✓ Clean |
O=C(O)[C@H]1O[C@@H](O[C@@H]2[C@@H](C(=O)O)O[C@@…
|
| ZINC39944744 | 0.655 | 370.3 Da LogP -5.21 TPSA 223.7 | 2 viol. | ✓ Clean |
O=C(O)[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C@@H]1…
|
| ZINC39944746 | 0.655 | 370.3 Da LogP -5.21 TPSA 223.7 | 2 viol. | ✓ Clean |
O=C(O)[C@H]1O[C@@H](O[C@@H]2[C@H](C(=O)O)O[C@@H…
|
| ZINC39944747 | 0.655 | 370.3 Da LogP -5.21 TPSA 223.7 | 2 viol. | ✓ Clean |
O=C(O)[C@@H]1O[C@@H](O[C@@H]2[C@H](C(=O)O)O[C@@…
|
| ZINC4095837 | 0.655 | 370.3 Da LogP -5.21 TPSA 223.7 | 2 viol. | ✓ Clean |
O=C(O)[C@H]1O[C@H](O[C@H]2[C@@H](C(=O)O)O[C@@H]…
|
| ZINC4095838 | 0.655 | 370.3 Da LogP -5.21 TPSA 223.7 | 2 viol. | ✓ Clean |
O=C(O)[C@H]1O[C@H](O[C@H]2[C@@H](C(=O)O)O[C@H](…
|
| ZINC4336491 | 0.556 | 208.2 Da LogP -3.04 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O
|
| ZINC4336492 | 0.556 | 208.2 Da LogP -3.04 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O
|
| ZINC34428338 | 0.552 | 219.2 Da LogP -1.81 TPSA 156.0 | ✓ Ro5 | Alert |
[N-]=[N+]=N[C@@H]1O[C@H](C(=O)O)[C@@H](O)[C@H](…
|
| ZINC242425547 | 0.536 | 208.2 Da LogP -2.47 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
CO[C@@H]1O[C@H](C(=O)O)[C@H](O)[C@@H](O)[C@@H]1O
|
| ZINC2575040 | 0.536 | 208.2 Da LogP -2.47 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
CO[C@H]1O[C@@H](C(=O)O)[C@H](O)[C@@H](O)[C@@H]1O
|
| ZINC3645756 | 0.536 | 208.2 Da LogP -2.47 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
CO[C@H]1O[C@H](C(=O)O)[C@H](O)[C@@H](O)[C@@H]1O
|
| ZINC4721246 | 0.536 | 208.2 Da LogP -2.47 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
CO[C@H]1O[C@@H](C(=O)O)[C@@H](O)[C@@H](O)[C@H]1O
|
| ZINC4721247 | 0.536 | 208.2 Da LogP -2.47 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
CO[C@@H]1O[C@@H](C(=O)O)[C@@H](O)[C@@H](O)[C@H]…
|
| ZINC4721248 | 0.536 | 208.2 Da LogP -2.47 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
CO[C@H]1O[C@@H](C(=O)O)[C@@H](O)[C@@H](O)[C@@H]…
|
| ZINC4721249 | 0.536 | 208.2 Da LogP -2.47 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
CO[C@@H]1O[C@@H](C(=O)O)[C@@H](O)[C@@H](O)[C@@H…
|
| ZINC5998328 | 0.536 | 208.2 Da LogP -2.47 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
CO[C@@H]1O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]1O
|
| ZINC35636281 | 0.516 | 234.2 Da LogP -2.48 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
C=CCOC(=O)[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@…
|
| ZINC69593544 | 0.516 | 234.2 Da LogP -2.48 TPSA 116.5 | ✓ Ro5 | ✓ Clean |
C=CCOC(=O)[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H…
|
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.