Research workbench
Crystal structure of the PDZ domain from human rgs-3
Analyse Crystal structure of the PDZ domain from human rgs-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F5Y
- Type
- protein
- Length
- 164 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulator of G-protein signalling 3 isoform 1
- UniProt
- P49796
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Regulator of G-protein signalling 3 isoform 1 | protein | 82 | 17% helix, 41% strand | P49796 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.53 | 0.79 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 422 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 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 P49796
- Elsewhere: RCSB PDB 2F5Y · PDBe 2F5Y · UniProt P49796
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.