Research workbench
Structure of CBM26 from bacillus halodurans amylase in complex with maltose
Analyse Structure of CBM26 from bacillus halodurans amylase in complex with maltose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C3H
- Type
- protein
- Length
- 737 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase G-6
- UniProt
- Q9KFR4
- Ligands
- GLC, SO4
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 2% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-amylase G-6 | protein | 93 | 3% helix, 44% strand | Q9KFR4 |
| B | Alpha-amylase G-6 | protein | 94 | 3% helix, 45% strand | Q9KFR4 |
| C, F | Alpha-amylase G-6 | protein | 91 | 0% helix, 46% strand | Q9KFR4 |
| D, E, G, H | Alpha-amylase G-6 | protein | 92 | 3% helix, 46% strand | Q9KFR4 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 17 copies · chains A, E, B, F, H, C, D, G
- SO4 · Sulfate ion · ion · 9 copies · chains A, B, C, E, F, H, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 880 | 0.78 | 0.81 | 77 | GLC |
| 2 | 922 | 0.77 | 0.79 | 74 | GLC, SO4 |
| 3 | 185 | 0.68 | 0.86 | 37 | SO4 |
| 4 | 148 | 0.67 | 0.88 | 32 | empty |
| 5 | 226 | 0.67 | 0.84 | 41 | SO4 |
Interfaces
13 interfaces between chains.
- F–H · 462 Ų buried · 17 hydrogen bonds · protein-protein
- D–E · 452 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 438 Ų buried · 8 hydrogen bonds · protein-protein
- B–G · 434 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 263 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2C3H · Structure of CBM26 from Bacillus halodurans amylase in complex with maltose · 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 Q9KFR4
- Elsewhere: RCSB PDB 2C3H · PDBe 2C3H · UniProt Q9KFR4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.