Overview
Basic information about this protein and its source genome.
- Accession
- KP13_00664
- Gene
- glgX AHE42283.1
- Status
- annotated
- Amino acids
- 626
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 44.286
- DEG E-value
- 5e-177
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 97.53
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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:0005980 The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
- 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:0004553 Catalysis of the hydrolysis of any O-glycosyl bond.
- GO:0004133 OBSOLETE. Catalysis of the cleavage of branch points in branched glycogen polymers.
- GO:0004135 Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin. Limit dextrin is the highly branched core that remains after exhaustive treatment of glycogen with glycogen phosphorylase. It is formed because these enzymes cannot hydrolyze the (1->6) glycosidic linkages present.
- GO:0120549 Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 101 | Gene3D | G3DSA:2.60.40.10 | Immunoglobulins |
| 1 | 101 | InterPro | IPR013783 | Immunoglobulin-like fold |
| 1 | 602 | NCBIfam | TIGR02100 | glycogen debranching protein GlgX |
| 1 | 602 | InterPro | IPR011837 | Glycogen debranching enzyme, GlgX type |
| 103 | 540 | Gene3D | G3DSA:3.20.20.80 | Glycosidases |
| 103 | 533 | SUPERFAMILY | SSF51445 | (Trans)glycosidases |
| 103 | 533 | InterPro | IPR017853 | Glycoside hydrolase superfamily |
| 2 | 594 | PANTHER | PTHR43002 | GLYCOGEN DEBRANCHING ENZYME |
| 153 | 255 | Pfam | PF00128 | Alpha amylase, catalytic domain |
| 153 | 255 | InterPro | IPR006047 | Glycosyl hydrolase, family 13, catalytic domain |
| 98 | 526 | SMART | SM00642 | aamy |
| 98 | 526 | InterPro | IPR006047 | Glycosyl hydrolase, family 13, catalytic domain |
| 541 | 625 | Gene3D | G3DSA:2.60.40.1180 | - |
| 541 | 625 | InterPro | IPR013780 | Glycosyl hydrolase, all-beta |
| 2 | 64 | Pfam | PF02922 | Carbohydrate-binding module 48 (Isoamylase N-terminal domain) |
| 2 | 64 | InterPro | IPR004193 | Glycoside hydrolase, family 13, N-terminal |
| 104 | 529 | CDD | cd11326 | AmyAc_Glg_debranch |
| 1 | 101 | CDD | cd02856 | E_set_GDE_Isoamylase_N |
| 1 | 101 | InterPro | IPR044505 | Glycogen debranching enzyme GlgX/isoamylase, N-terminal Early set domain |
| 2 | 112 | SUPERFAMILY | SSF81296 | E set domains |
| 2 | 112 | InterPro | IPR014756 | Immunoglobulin E-set |
| 539 | 623 | Pfam | PF18390 | Glycogen debranching enzyme C-terminal domain |
| 539 | 623 | InterPro | IPR040784 | Glycogen debranching enzyme, C-terminal 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 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GYH9
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_00664
|
ColabFold | — | — | full sequence | — | Loaded |
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 |
|---|---|---|---|---|---|---|---|
| 8 | 0.651 | ||||||
| 7 | 0.583 |
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 | 18.57 | 0.825 | ||||||
| 2 | 4.66 | 0.203 | ||||||
| 3 | 4.33 | 0.18 | ||||||
| 4 | 2.77 | 0.085 | ||||||
| 5 | 2.28 | 0.057 |
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 | 0.254 | ||||||
| 25 | 0.218 |
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 | 19.78 | 0.845 | ||||||
| 2 | 10.21 | 0.549 | ||||||
| 3 | 6.21 | 0.31 | ||||||
| 4 | 4.75 | 0.209 | ||||||
| 5 | 4.1 | 0.165 |
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 |
|---|---|---|---|---|---|---|
| TAM | A0A0C5GWS2 | 163.2 Da LogP -1.17 TPSA 86.7 | ✓ Ro5 | ✓ Clean |
C(CO)C(CCO)(CCO)N
|
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 |
|---|---|---|---|---|---|
| ZINC2575038 | 0.625 | 205.3 Da LogP 0.00 TPSA 86.7 | ✓ Ro5 | ✓ Clean |
NC(CCCO)(CCCO)CCCO
|
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.