Research workbench
The cryo-EM structure of the VAG8-C1 inhibitor complex
Analyse The cryo-EM structure of the VAG8-C1 inhibitor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AKV
- Type
- protein
- Length
- 799 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Plasma protease C1 inhibitor; VAG8
- UniProt
- P05155, O66044
- Pockets
- 5 · best druggability 0.78
Structure
electron microscopy · 2 distinct chains · 13% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Plasma protease C1 inhibitor | protein | 378 | 28% helix, 24% strand | P05155 |
| G | VAG8 | protein | 421 | 0% helix, 30% strand | O66044 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 949 | 0.78 | 0.81 | 77 | empty |
| 2 | 151 | 0.52 | 0.79 | 27 | empty |
| 3 | 113 | 0.52 | 0.81 | 18 | empty |
| 4 | 122 | 0.49 | 0.79 | 30 | empty |
| 5 | 52 | 0.24 | 0.72 | 12 | empty |
Interfaces
1 interface between chains.
- A–G · 902 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 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 P05155
- Every structure of UniProt O66044
- Elsewhere: RCSB PDB 7AKV · PDBe 7AKV · UniProt P05155 · UniProt O66044
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