Research workbench
Cryoem structure of cgas nucleosome complex
Analyse Cryoem structure of cgas nucleosome complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7A08
- Type
- protein + DNA
- Length
- 1,333 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic gmp-AMP synthase; Nucleosomal DNA strand 1; Nucleosomal DNA strand 2; Histone H2A…
- EC
- 2.7.7.86
- UniProt
- Q8C6L5, Q93077, P62807, P84243, P62805
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.76
Structure
electron microscopy · 11 distinct chains · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| a | Cyclic gmp-AMP synthase (EC 2.7.7.86) | protein | 360 | 40% helix, 13% strand | Q8C6L5 |
| I | Nucleosomal DNA strand 1 | dna | 132 | — | — |
| J | Nucleosomal DNA strand 2 | dna | 131 | — | — |
| b | Histone H2A type 1-C | protein | 105 | 44% helix, 6% strand | Q93077 |
| c | Histone H2B type 1-C/E/F/G/I | protein | 93 | 69% helix, 3% strand | P62807 |
| d | Histone H3.3 | protein | 95 | 62% helix, 4% strand | P84243 |
| e | Histone H4 | protein | 77 | 65% helix, 9% strand | P62805 |
| f | Histone H2A type 1-C | protein | 93 | 59% helix, 8% strand | Q93077 |
| g | Histone H2B type 1-C/E/F/G/I | protein | 90 | 72% helix, 4% strand | P62807 |
| h | Histone H3.3 | protein | 78 | 55% helix, 5% strand | P84243 |
| i | Histone H4 | protein | 79 | 63% helix, 9% strand | P62805 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains a
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 907 | 0.76 | 0.79 | 87 | empty |
| 2 | 469 | 0.73 | 0.83 | 49 | empty |
| 3 | 406 | 0.73 | 0.83 | 43 | empty |
| 4 | 889 | 0.72 | 0.77 | 71 | empty |
| 5 | 649 | 0.70 | 0.78 | 67 | empty |
Interfaces
39 interfaces between chains.
- I–J · 5946 Ų buried · 533 hydrogen bonds · nucleic-nucleic
- f–g · 2608 Ų buried · 18 hydrogen bonds · protein-protein
- b–c · 2591 Ų buried · 16 hydrogen bonds · protein-protein
- d–i · 2502 Ų buried · 20 hydrogen bonds · protein-protein
- e–h · 2147 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q8C6L5
- Every structure of UniProt Q93077
- Every structure of UniProt P62807
- Every structure of UniProt P84243
- Every structure of UniProt P62805
- Elsewhere: RCSB PDB 7A08 · PDBe 7A08 · UniProt Q8C6L5 · UniProt Q93077 · UniProt P62807 · UniProt P84243 · UniProt P62805
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.