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Crystal structure of calcium free human gelsolin amyloid mutant G167R
Analyse Crystal structure of calcium free human gelsolin amyloid mutant G167R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JEG
- Type
- protein
- Length
- 1,432 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gelsolin
- UniProt
- P06396
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gelsolin | protein | 714 | 27% helix, 28% strand | P06396 |
| B | Gelsolin | protein | 718 | 26% helix, 27% strand | P06396 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1140 | 0.82 | 0.83 | 114 | empty |
| 2 | 607 | 0.79 | 0.85 | 71 | empty |
| 3 | 806 | 0.78 | 0.82 | 83 | empty |
| 4 | 1077 | 0.77 | 0.79 | 88 | GOL |
| 5 | 234 | 0.62 | 0.81 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 718 Ų buried · 6 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 P06396
- Elsewhere: RCSB PDB 6JEG · PDBe 6JEG · UniProt P06396
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