Research workbench
Improved X-ray structure of thermoactinomyces vulgaris R-47 alpha- amylase 2
Analyse Improved X-ray structure of thermoactinomyces vulgaris R-47 alpha- amylase 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JI2
- Type
- protein
- Length
- 1,170 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase II
- EC
- 3.2.1.135
- UniProt
- Q08751
- Ligands
- CA
- Pockets
- 12 · best druggability 0.90
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-amylase II (EC 3.2.1.135) | protein | 585 | 30% helix, 27% strand | Q08751 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1125 | 0.90 | 0.92 | 132 | empty |
| 2 | 207 | 0.60 | 0.81 | 46 | empty |
| 3 | 291 | 0.58 | 0.77 | 54 | empty |
| 4 | 193 | 0.55 | 0.79 | 26 | empty |
| 5 | 213 | 0.55 | 0.79 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 2322 Ų buried · 50 hydrogen bonds · protein-protein
Compared structures
- 1JI2 · Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q08751 · AlphaFold monomer V2.0 prediction for neopullulanase 2 (Q08751) · a predicted model of the same protein · 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 Q08751
- Elsewhere: RCSB PDB 1JI2 · PDBe 1JI2 · UniProt Q08751
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