Research workbench
Crystal structure of the candida glabrata glycogen debranching enzyme (D535N) in complex with maltotetrose
Analyse Crystal structure of the candida glabrata glycogen debranching enzyme (D535N)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EKW
- Type
- protein
- Length
- 3,046 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-alpha-glucanotransferase
- EC
- 2.4.1.25, 3.2.1.33
- UniProt
- Q6FSK0
- Ligands
- GLC
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-alpha-glucanotransferase (EC 2.4.1.25, 3.2.1.33) | protein | 1520 | 36% helix, 16% strand | Q6FSK0 |
| B | 4-alpha-glucanotransferase (EC 2.4.1.25, 3.2.1.33) | protein | 1526 | 35% helix, 16% strand | Q6FSK0 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 835 | 0.85 | 0.87 | 88 | empty |
| 2 | 860 | 0.84 | 0.86 | 80 | empty |
| 3 | 555 | 0.72 | 0.80 | 64 | empty |
| 4 | 110 | 0.72 | 0.93 | 32 | empty |
| 5 | 578 | 0.72 | 0.80 | 68 | empty |
Interfaces
1 interface between chains.
- A–B · 206 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7EKW · Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (D535N) in complex… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q6FSK0
- Elsewhere: RCSB PDB 7EKW · PDBe 7EKW · UniProt Q6FSK0
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