Research workbench
TRIS/MALTOTRIOSE complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A
Analyse TRIS/MALTOTRIOSE complex of chimaeric amylase from B. amyloliquefaciens and B.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E40
- Type
- protein
- Length
- 483 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase
- EC
- 3.2.1.1
- UniProt
- P00692, P06278
- Ligands
- GLC, CA, NA
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-amylase (EC 3.2.1.1) | protein | 483 | 27% helix, 25% strand | P00692, P06278 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 3 copies · chains A
- CA · Calcium ion · metal · 4 copies · chains A
- NA · Sodium ion · metal · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.53 | 0.79 | 24 | TRS |
| 2 | 58 | 0.34 | 0.77 | 13 | empty |
| 3 | 66 | 0.28 | 0.73 | 26 | GLC |
Compared structures
- 1E40 · Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B.… · the same entry in another collection · chain A against A, TM-score 1.00
- P00692 · AlphaFold monomer V2.0 prediction for alpha-amylase (P00692) · a predicted model of the same protein · chain A against A, TM-score 1.00
- P06278 · AlphaFold monomer V2.0 prediction for alpha-amylase (P06278) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00692
- Every structure of UniProt P06278
- Elsewhere: RCSB PDB 1E40 · PDBe 1E40 · UniProt P00692 · UniProt P06278
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