Research workbench
Cdaa-apo Y187A mutant
Analyse Cdaa-apo Y187A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HVN
- Type
- protein
- Length
- 334 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 0.34
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diadenylate cyclase (EC 2.7.7.85) | protein | 175 | 35% helix, 21% strand | Q8Y5E4 |
| B | Diadenylate cyclase (EC 2.7.7.85) | protein | 159 | 36% helix, 23% strand | Q8Y5E4 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains A
- FRU · beta-D-fructofuranose · sugar · chains A
- CL · Chloride ion · ion · 8 copies · chains A, B
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 | 71 | 0.34 | 0.76 | 13 | FRU |
| 2 | 55 | 0.32 | 0.77 | 15 | empty |
| 3 | 50 | 0.31 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 768 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 6HVN · PDBe 6HVN · UniProt Q8Y5E4
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