Research workbench
Structural characterization of cdaa-apo
Analyse Structural characterization of cdaa-apo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HVM
- Type
- protein
- Length
- 322 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diadenylate cyclase
- EC
- 2.7.7.85
- UniProt
- Q8Y5E4
- Ligands
- GLC, FRU, CL
- Pockets
- 3 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diadenylate cyclase (EC 2.7.7.85) | protein | 167 | 35% helix, 22% strand | Q8Y5E4 |
| B | Diadenylate cyclase (EC 2.7.7.85) | protein | 155 | 35% helix, 25% strand | Q8Y5E4 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains B
- FRU · beta-D-fructofuranose · sugar · chains B
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.35 | 0.75 | 15 | empty |
| 2 | 82 | 0.35 | 0.76 | 27 | empty |
| 3 | 58 | 0.33 | 0.77 | 15 | GLC, FRU |
Interfaces
1 interface between chains.
- A–B · 754 Ų buried · 13 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 Q8Y5E4
- Elsewhere: RCSB PDB 6HVM · PDBe 6HVM · UniProt Q8Y5E4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.