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Crystal structure of processing alpha-glucosidase I
Analyse Crystal structure of processing alpha-glucosidase I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J5T
- Type
- protein
- Length
- 788 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mannosyl-oligosaccharide glucosidase
- EC
- 3.2.1.106
- UniProt
- P53008
- Ligands
- NAG
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mannosyl-oligosaccharide glucosidase (EC 3.2.1.106) | protein | 788 | 38% helix, 21% strand | P53008 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 552 | 0.73 | 0.81 | 52 | empty |
| 2 | 497 | 0.67 | 0.78 | 60 | empty |
| 3 | 242 | 0.65 | 0.83 | 32 | empty |
| 4 | 158 | 0.49 | 0.78 | 21 | empty |
| 5 | 67 | 0.39 | 0.79 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 P53008
- Elsewhere: RCSB PDB 4J5T · PDBe 4J5T · UniProt P53008
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