MolNFT v1 · #11806 · protein
Role of ethe mobile loop in the mehanism of human salivary amylase
1JXK · Alpha-amylase, salivary: “Role of ethe mobile loop in the mehanism of human salivary amylase”. X-ray diffraction, 2 ligands (CA, CL), 3 pockets (best druggability 0.51). MolNFT v1 #11806 on GenesisL1: 3D structure, binding sites and…
- 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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