Research workbench
Crystal structure of human gelsolin amyloid mutant A551P
Analyse Crystal structure of human gelsolin amyloid mutant A551P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P2B
- Type
- protein
- Length
- 1,426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gelsolin
- UniProt
- P06396
- Ligands
- SO4, CL
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gelsolin | protein | 717 | 25% helix, 28% strand | P06396 |
| B | Gelsolin | protein | 709 | 25% helix, 28% strand | P06396 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
- CL · Chloride ion · ion · chains B
- GOL · Glycerol · additive · 8 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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1112 | 0.83 | 0.84 | 127 | SO4 |
| 2 | 869 | 0.80 | 0.83 | 99 | SO4 |
| 3 | 391 | 0.79 | 0.88 | 50 | empty |
| 4 | 907 | 0.77 | 0.80 | 77 | GOL |
| 5 | 858 | 0.75 | 0.79 | 67 | GOL |
Interfaces
1 interface between chains.
- A–B · 1214 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 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 P06396
- Elsewhere: RCSB PDB 7P2B · PDBe 7P2B · UniProt P06396
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