Research workbench
Crystal structure of GH65 alpha-1,2-glucosidase from flavobacterium johnsoniae in complex with glucose
Analyse Crystal structure of GH65 alpha-1,2-glucosidase from flavobacterium johnsoniae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FE4
- Type
- protein
- Length
- 1,977 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Candidate alpha glycoside phosphorylase glycoside hydrolase family 65
- UniProt
- A5FBJ5
- Ligands
- BGC
- Pockets
- 19 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Candidate alpha glycoside phosphorylase glycoside hydrolase family 65 | protein | 659 | 33% helix, 27% strand | A5FBJ5 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 12 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 625 | 0.72 | 0.80 | 63 | empty |
| 2 | 674 | 0.72 | 0.79 | 73 | empty |
| 3 | 621 | 0.71 | 0.79 | 69 | empty |
| 4 | 164 | 0.60 | 0.83 | 35 | empty |
| 5 | 163 | 0.56 | 0.81 | 33 | BGC |
Interfaces
3 interfaces between chains.
- A–C · 1098 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1089 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1075 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 7FE4 · Crystal structure of GH65 alpha-1,2-glucosidase from Flavobacterium johnsoniae 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 A5FBJ5
- Elsewhere: RCSB PDB 7FE4 · PDBe 7FE4 · UniProt A5FBJ5
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