Research workbench
The structure of amylosucrase from D. radiodurans
Analyse The structure of amylosucrase from D. radiodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AYS
- Type
- protein
- Length
- 589 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amylosucrase
- EC
- 2.4.1.4
- UniProt
- Q9RVT9
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amylosucrase (EC 2.4.1.4) | protein | 589 | 46% helix, 17% strand | Q9RVT9 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 447 | 0.63 | 0.77 | 58 | empty |
| 2 | 186 | 0.47 | 0.75 | 21 | empty |
| 3 | 78 | 0.37 | 0.77 | 20 | empty |
| 4 | 71 | 0.35 | 0.77 | 22 | empty |
| 5 | 64 | 0.29 | 0.74 | 14 | empty |
Compared structures
- 4AYS · The Structure of Amylosucrase from D. radiodurans · 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 Q9RVT9
- Elsewhere: RCSB PDB 4AYS · PDBe 4AYS · UniProt Q9RVT9
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