Protein profile
PA2151
alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
Genome: NC_002516.2
Overview
Basic information about this protein and its source genome.
- Accession
- PA2151
- Gene
- PA2151 glgE
- Status
- annotated
- Amino acids
- 664
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- 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:0004556 Catalysis of the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more alpha-(1->4)-linked D-glucose units.
- GO:0016758 Catalysis of the transfer of a hexosyl group from one compound (donor) to another (acceptor).
- GO:0030979 The chemical reactions and pathways resulting in the formation of alpha-glucans, compounds composed of glucose residues linked by alpha-D-glucosidic bonds.
- GO:0009313 The chemical reactions and pathways resulting in the breakdown of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
- GO:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
- GO:0004553 Catalysis of the hydrolysis of any O-glycosyl bond.
- GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 21 | 202 | Gene3D | G3DSA:2.60.40.10 | Immunoglobulins |
| 21 | 202 | InterPro | IPR013783 | Immunoglobulin-like fold |
| 213 | 651 | SMART | SM00642 | aamy |
| 213 | 651 | InterPro | IPR006047 | Glycosyl hydrolase, family 13, catalytic domain |
| 195 | 646 | PANTHER | PTHR47786 | ALPHA-1,4-GLUCAN:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE |
| 199 | 565 | SUPERFAMILY | SSF51445 | (Trans)glycosidases |
| 199 | 565 | InterPro | IPR017853 | Glycoside hydrolase superfamily |
| 21 | 203 | Pfam | PF11896 | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase, domain N/S |
| 21 | 203 | InterPro | IPR021828 | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase, domain N/S |
| 18 | 661 | Hamap | MF_02124 | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase [glgE]. |
| 18 | 661 | InterPro | IPR026585 | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase |
| 205 | 567 | Gene3D | G3DSA:3.20.20.80 | Glycosidases |
| 570 | 664 | Gene3D | G3DSA:2.60.40.1180 | - |
| 570 | 664 | InterPro | IPR013780 | Glycosyl hydrolase, all-beta |
| 208 | 562 | CDD | cd11344 | AmyAc_GlgE_like |
| 108 | 184 | Gene3D | G3DSA:1.20.58.80 | - |
| 227 | 340 | Pfam | PF00128 | Alpha amylase, catalytic domain |
| 227 | 340 | InterPro | IPR006047 | Glycosyl hydrolase, family 13, catalytic domain |
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
PA2151
|
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 | 0.202 |
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.
No PDB structure with a co-crystallized ligand found for this exact protein.
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.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| ARE | Q08751 | 807.7 Da LogP -10.74 TPSA 400.3 | 3 viol. | ✓ Clean |
C[C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O[C@@H]2[C@…
|
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).
| Ligand | UniProt (homolog) | pchembl | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| CHEMBL404271 | P94451 | 6.47 | 645.6 Da LogP -8.56 TPSA 321.2 | 3 viol. | ✓ Clean |
C[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@@H](O[…
|
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 |
|---|---|---|---|---|---|
| ZINC1857787936 | 0.581 | 497.5 Da LogP -6.75 TPSA 253.0 | 2 viol. | ✓ Clean |
OCC1=C[C@@H](N[C@@H]2C[C@@H](CO)[C@H](O[C@H]3O[…
|
| ZINC2053528368 | 0.581 | 497.5 Da LogP -6.75 TPSA 253.0 | 2 viol. | ✓ Clean |
OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…
|
| ZINC2053528371 | 0.581 | 497.5 Da LogP -6.75 TPSA 253.0 | 2 viol. | ✓ Clean |
OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…
|
| ZINC2053528373 | 0.581 | 497.5 Da LogP -6.75 TPSA 253.0 | 2 viol. | ✓ Clean |
OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…
|
| ZINC2053528375 | 0.581 | 497.5 Da LogP -6.75 TPSA 253.0 | 2 viol. | ✓ Clean |
OCC1=C[C@@H](N[C@@H]2C[C@H](CO)[C@@H](O[C@H]3O[…
|
| ZINC8437016 | 0.581 | 497.5 Da LogP -6.75 TPSA 253.0 | 2 viol. | ✓ Clean |
OCC1=C[C@H](N[C@H]2C[C@H](CO)[C@@H](O[C@@H]3O[C…
|
| ZINC642771928 | 0.544 | 483.5 Da LogP -6.55 TPSA 249.9 | 2 viol. | ✓ Clean |
C[C@H]1O[C@H](O[C@H]([C@H](O)CO)[C@H](O)[C@@H](…
|
| ZINC100055151 | 0.500 | 488.4 Da LogP -6.55 TPSA 248.4 | 2 viol. | ✓ Clean |
C[C@@H]1O[C@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)O…
|
| ZINC100055153 | 0.500 | 488.4 Da LogP -6.55 TPSA 248.4 | 2 viol. | ✓ Clean |
C[C@@H]1O[C@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)O…
|
| ZINC100055156 | 0.500 | 488.4 Da LogP -6.55 TPSA 248.4 | 2 viol. | ✓ Clean |
C[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](CO)O[C@@H…
|
| ZINC100055157 | 0.500 | 488.4 Da LogP -6.55 TPSA 248.4 | 2 viol. | ✓ Clean |
C[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](CO)O[C@@H…
|
| ZINC2362797719 | 0.500 | 488.4 Da LogP -6.55 TPSA 248.4 | 2 viol. | ✓ Clean |
C[C@@H]1O[C@@H](O[C@H]2[C@H](O[C@H]3[C@@H](O)[C…
|
| ZINC55537584 | 0.500 | 488.4 Da LogP -6.55 TPSA 248.4 | 2 viol. | ✓ Clean |
C[C@@H]1O[C@@H](O[C@H]2[C@H](O[C@@H]3[C@@H](CO)…
|
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.