Research workbench
Crystal structure of amylomaltase from corynebacterium glutamicum
Analyse Crystal structure of amylomaltase from corynebacterium glutamicum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JJH
- Type
- protein
- Length
- 704 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-alpha-glucanotransferase
- EC
- 2.4.1.25
- UniProt
- A0A0R7P4S4
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-alpha-glucanotransferase (EC 2.4.1.25) | protein | 704 | 42% helix, 18% strand | A0A0R7P4S4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.77 | 0.98 | 25 | GOL |
| 2 | 83 | 0.77 | 0.98 | 25 | empty |
| 3 | 1082 | 0.73 | 0.76 | 68 | SO4 |
| 4 | 302 | 0.53 | 0.75 | 36 | empty |
| 5 | 95 | 0.50 | 0.82 | 21 | empty |
Compared structures
- 5JJH · Crystal structure of amylomaltase from Corynebacterium glutamicum · 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 A0A0R7P4S4
- Elsewhere: RCSB PDB 5JJH · PDBe 5JJH · UniProt A0A0R7P4S4
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