Research workbench
Glycosidase wild type at PH8.0
Analyse Glycosidase wild type at PH8.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C25
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isomaltose glucohydrolase
- EC
- 3.2.1.205
- UniProt
- D2PPM8
- Ligands
- NH4
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isomaltose glucohydrolase (EC 3.2.1.205) | protein | 372 | 56% helix, 5% strand | D2PPM8 |
Ligands and binding sites
- NH4 · Ammonium ion · ion · chains A
- GOL · Glycerol · additive · 4 copies · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.63 | 0.84 | 23 | GOL |
Modifications
Observed in the structure: 1 modified (oxidation).
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 D2PPM8
- Elsewhere: RCSB PDB 7C25 · PDBe 7C25 · UniProt D2PPM8
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