Research workbench
Crystal structure of the novel alpha-amylase amyc from thermotoga maritima
Analyse Crystal structure of the novel alpha-amylase amyc from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B5D
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase
- EC
- 3.2.1.1
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Alpha-amylase (EC 3.2.1.1) | protein | 518 | 54% helix, 10% strand | — |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 535 | 0.74 | 0.82 | 86 | empty |
| 2 | 137 | 0.65 | 0.87 | 21 | empty |
| 3 | 152 | 0.50 | 0.78 | 20 | empty |
| 4 | 80 | 0.41 | 0.79 | 22 | empty |
Compared structures
- 2B5D · Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima · the same entry in another collection · chain X against X, 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
- Elsewhere: RCSB PDB 2B5D · PDBe 2B5D
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.