Research workbench
Crystal structure of SEPT2 G-domain
Analyse Crystal structure of SEPT2 G-domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QA5
- Type
- protein
- Length
- 467 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Septin-2
- UniProt
- Q15019
- Ligands
- GDP
- Pockets
- 6 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Septin-2 | protein | 233 | 44% helix, 21% strand | Q15019 |
| B | Septin-2 | protein | 234 | 45% helix, 20% strand | Q15019 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 384 | 0.65 | 0.79 | 38 | GDP |
| 2 | 303 | 0.62 | 0.79 | 33 | GDP |
| 3 | 147 | 0.46 | 0.77 | 26 | empty |
| 4 | 129 | 0.44 | 0.76 | 18 | empty |
| 5 | 73 | 0.36 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 912 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
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 Q15019
- Elsewhere: RCSB PDB 2QA5 · PDBe 2QA5 · UniProt Q15019
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.