Research workbench
Complex structure 2 of the bacillus subtilis cdaa C-di-AMP cyclase domain (cdaacd) and the phosphoglucomutase glmm short variant (GLMMF369)
Analyse Complex structure 2 of the bacillus subtilis cdaa C-di-AMP cyclase domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OJS
- Type
- protein
- Length
- 3,084 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucosamine mutase; Cyclic di-AMP synthase cdaa
- EC
- 5.4.2.10, 2.7.7.85
- UniProt
- O34824, Q45589
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, F, A, B, G, J | Phosphoglucosamine mutase (EC 5.4.2.10) | protein | 368 | 37% helix, 20% strand | O34824 |
| H, I, D, E, K, L | Cyclic di-AMP synthase cdaa (EC 2.7.7.85) | protein | 146 | 29% helix, 25% strand | Q45589 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 476 | 0.77 | 0.85 | 58 | empty |
| 2 | 423 | 0.75 | 0.85 | 62 | empty |
| 3 | 339 | 0.73 | 0.85 | 43 | empty |
| 4 | 262 | 0.72 | 0.86 | 34 | empty |
| 5 | 253 | 0.72 | 0.87 | 38 | empty |
Interfaces
23 interfaces between chains.
- G–J · 1204 Ų buried · 12 hydrogen bonds · protein-protein
- C–F · 1195 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1179 Ų buried · 13 hydrogen bonds · protein-protein
- H–I · 774 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 767 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7OJS · Complex structure 2 of the Bacillus subtilis CdaA c-di-AMP cyclase domain (CdaACD) and… · the same entry in another collection · chain L against L, 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 O34824
- Every structure of UniProt Q45589
- Elsewhere: RCSB PDB 7OJS · PDBe 7OJS · UniProt O34824 · UniProt Q45589
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