Research workbench
Crystal structure of the sulfolobus solfataricus alpha- glucosidase mala
Analyse Crystal structure of the sulfolobus solfataricus alpha- glucosidase mala in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G3M
- Type
- protein
- Length
- 4,147 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-glucosidase
- EC
- 3.2.1.20
- UniProt
- O59645
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Alpha-glucosidase (EC 3.2.1.20) | protein | 691 | 26% helix, 31% strand | O59645 |
| F | Alpha-glucosidase (EC 3.2.1.20) | protein | 692 | 25% helix, 30% strand | O59645 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1188 | 0.86 | 0.87 | 144 | empty |
| 2 | 680 | 0.82 | 0.86 | 82 | empty |
| 3 | 608 | 0.82 | 0.87 | 76 | empty |
| 4 | 573 | 0.81 | 0.87 | 76 | empty |
| 5 | 464 | 0.80 | 0.88 | 68 | empty |
Interfaces
12 interfaces between chains.
- E–F · 1605 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 1579 Ų buried · 24 hydrogen bonds · protein-protein
- D–E · 1563 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 1549 Ų buried · 23 hydrogen bonds · protein-protein
- D–F · 1541 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 2G3M · Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA · 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 O59645
- Elsewhere: RCSB PDB 2G3M · PDBe 2G3M · UniProt O59645
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