Research workbench
Structure of cggbe in complex with maltotriose
Analyse Structure of cggbe in complex with maltotriose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P43
- Type
- protein
- Length
- 1,377 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1,4-alpha-glucan-branching enzyme
- EC
- 2.4.1.18
- UniProt
- Q6FJV0
- Ligands
- GLC
- Pockets
- 15 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1,4-alpha-glucan-branching enzyme (EC 2.4.1.18) | protein | 687 | 31% helix, 22% strand | Q6FJV0 |
| B | 1,4-alpha-glucan-branching enzyme (EC 2.4.1.18) | protein | 690 | 31% helix, 21% strand | Q6FJV0 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.76 | 0.96 | 22 | empty |
| 2 | 1076 | 0.75 | 0.77 | 99 | empty |
| 3 | 272 | 0.62 | 0.80 | 28 | empty |
| 4 | 82 | 0.59 | 0.88 | 29 | empty |
| 5 | 178 | 0.53 | 0.79 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 525 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 Q6FJV0
- Elsewhere: RCSB PDB 7P43 · PDBe 7P43 · UniProt Q6FJV0
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