Research workbench
Human gelsolin from residues GLU28 to ARG161 with calcium
Analyse Human gelsolin from residues GLU28 to ARG161 with calcium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZZ0
- Type
- protein
- Length
- 245 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gelsolin
- UniProt
- P06396
- Ligands
- CA
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G | Gelsolin | protein | 122 | 20% helix, 33% strand | P06396 |
| A | Gelsolin | protein | 123 | 20% helix, 34% strand | P06396 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains G, A
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 139 | 0.51 | 0.79 | 17 | empty |
| 2 | 58 | 0.41 | 0.81 | 17 | empty |
| 3 | 53 | 0.32 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- G–A · 682 Ų buried · 5 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 5ZZ0 · PDBe 5ZZ0 · UniProt P06396
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