KpKP13 Protein target profile

Glycogen debranching enzyme

Accession: KP13_00664

Gene: AHE42283.1 glgX 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GYH9
Length 626
Pocket druggability (P2Rank · AlphaFold DB model) 0.871
Direct ligand evidence 0 2 total records
Functional annotation 1 EC 6 GO
Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target
No hit
Gut microbiome similarity
2.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
Y
DEG identity (%)
44.286 Higher values support similarity to known essential genes.
DEG E-value
5e-177 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT
97.53 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.871
Structure A0A0H3GYH9
Pocket Pocket 1
Druggability (FPocket) 0.651
Structure A0A0H3GYH9
Pocket Pocket 8
ColabFold model
P2Rank 0.904 · Pocket 1
FPocket 0.254 · Pocket 4
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 128 / 4744 genomes with a hit
Prevalence 2.7%

Sequence

Primary amino-acid sequence viewer.

MELCVFDEQGNEQRFDLPARSGDIWHGWLAAAGPGLRYGYRVHGPWDPAQGHRFNPAKLLIDPSAHRVEGDLPDDERLHGGMWQPDRRDSAAVAPKSQVVDLRYDWRGDKPPRTPWGETVIYEAHVKGLTLLNPQLPEAIRGTYKALGHPAMIAYFKSLGISALELLPVAQFASEPRLQRMGLSNYWGYNPLAWFALDPRYASDPDRALDEFRDAVKALHAAGIEVILDIVLNHSAEIDLEGPTVSLRGIDNRSYYWVREDGDYHNWTGCGNTLNLSHPGVVEWARQCLRFWVDECHVDGFRFDLASVMGRTPEFRQDAPLFEAIRRDSVLSQVKLIAEPWDIGPGGYQVGNFPPLFAEWNDHFRDSARRFWLQQNVSLGDFAQRFAASSDLFARDGKPPSATVNLVTAHDGFTLRDCVCFNQKHNEANGEENRDGTNNNYSNNHGIEGLEANFAVIERRRASAHALLTTLLLAQGTPMLLAGDEQGHSQHGNNNAYCQDNALTWLDWRQANPGLTAFTAALIHLRRRIPALTRNRWWQEGDGNVRWLNRNAQPLTAAEWQQGAACMQIQLSDRWLLTLNATAEVVDMVLPEGEWRAVPPFAGEDNPVIMAVWHGPAHGVCVFQRS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization
Cytoplasmic

Enzyme Commission (EC)

1

Gene 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 domains and features

Domain and signature matches imported from InterPro and related databases.

23 records
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; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low
How colors and pocket overlays are used
Uniform protein color marks the displayed model as a single molecular object.
Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.
Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.
'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.
'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.
'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.
Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1
0.871
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Surrounding area
Pocket 2 P2Rank #2
0.389
Likely same site as FPocket 8 2.2 Å 15 shared residues 100% of smaller site
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Surrounding area
Pocket 3 P2Rank #3
0.26
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Surrounding area
Pocket 4 P2Rank #4
0.207
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Surrounding area
Pocket 5 P2Rank #5
0.125
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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #8
0.651 Unusual size
Likely same site as P2Rank 2 2.2 Å 15 shared residues 100% of smaller site
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Surrounding area
Pocket 2 FPocket #7
0.583
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Surrounding area
Residue sets
UniProt: Active site:336-336 Nucleophile
UniProt: Active site:371-371 Proton donor
UniProt: Site:443-443 Transition state stabilizer
All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold DB AF_A0A0H3GYH9
AlphaFold DB full sequence Viewing
ColabFold KP13_00664
ColabFold full sequence Loaded

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.

2 records
Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records
Transferred evidence 1 records from similar proteins
Structural ligands 1 0 loaded crystals
Measured bioactivity 0 direct and transferred ChEMBL records
Proposed compounds 1 similarity-based ZINC candidates
Best available ligand signal
TAM PDB via homolog 163.2 Da · LogP -1.17 · TPSA 86.7 Open detail RCSB PDB
ZINC2575038 ZINC proposed compound · Tanimoto 0.625 Detail ZINC

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
TAM RCSB PDB A0A0C5GWS2 163.2 Da LogP -1.17 TPSA 86.7 ✓ Ro5 ✓ Clean C(CO)C(CCO)(CCO)N

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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.