Research workbench
Nucleotide-free human dynamin-1-like protein GTPase-ged fusion
Analyse Nucleotide-free human dynamin-1-like protein GTPase-ged fusion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H1U
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dynamin-1-like protein
- EC
- 3.6.5.5
- UniProt
- O00429
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dynamin-1-like protein (EC 3.6.5.5) | protein | 358 | 40% helix, 15% strand | O00429 |
Ligands and binding sites
- FLC · Citrate anion · additive · chains A
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 | 102 | 0.62 | 0.88 | 22 | empty |
| 2 | 274 | 0.61 | 0.80 | 45 | FLC |
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 O00429
- Elsewhere: RCSB PDB 4H1U · PDBe 4H1U · UniProt O00429
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