Research workbench
Artificial GTPase-bse dimer of human DYNAMIN1
Analyse Artificial GTPase-bse dimer of human DYNAMIN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6S9A
- Type
- protein
- Length
- 632 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dynamin-1,DYNAMIN-1
- EC
- 3.6.5.5
- UniProt
- Q05193
- Ligands
- ZN, CL
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dynamin-1,DYNAMIN-1 (EC 3.6.5.5) | protein | 312 | 48% helix, 16% strand | Q05193 |
| B | Dynamin-1,DYNAMIN-1 (EC 3.6.5.5) | protein | 320 | 46% helix, 16% strand | Q05193 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 584 | 0.68 | 0.77 | 65 | empty |
| 2 | 559 | 0.65 | 0.76 | 72 | empty |
Interfaces
1 interface between chains.
- A–B · 740 Ų buried · 11 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 Q05193
- Elsewhere: RCSB PDB 6S9A · PDBe 6S9A · UniProt Q05193
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.