Research workbench
Role of ethe mobile loop in the mehanism of human salivary amylase
Analyse Role of ethe mobile loop in the mehanism of human salivary amylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JXK
- Type
- protein
- Length
- 491 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase, salivary
- EC
- 3.2.1.1
- UniProt
- P04745
- Ligands
- CA, CL
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-amylase, salivary (EC 3.2.1.1) | protein | 491 | 27% helix, 24% strand | P04745 |
Ligands and binding sites
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 | 220 | 0.51 | 0.76 | 24 | empty |
| 2 | 72 | 0.32 | 0.75 | 14 | empty |
| 3 | 72 | 0.31 | 0.75 | 24 | empty |
Modifications
Observed in the structure: 5 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 1JXK · Role of ethe mobile loop in the mehanism of human salivary amylase · 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 P04745
- Elsewhere: RCSB PDB 1JXK · PDBe 1JXK · UniProt P04745
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