Research workbench
Crystal structure of the C2 domain of the human regulator of G-protein signaling 3 isoform 6 (RGP3), northeast structural genomics consortium target HR5550A
Analyse Crystal structure of the C2 domain of the human regulator of G-protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FBK
- Type
- protein
- Length
- 276 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulator of G-protein signaling 3
- UniProt
- P49796
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulator of G-protein signaling 3 | protein | 138 | 9% helix, 45% strand | P49796 |
| B | Regulator of G-protein signaling 3 | protein | 138 | 9% helix, 45% strand | P49796 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
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 | 244 | 0.84 | 0.96 | 37 | empty |
| 2 | 119 | 0.46 | 0.78 | 24 | empty |
| 3 | 128 | 0.46 | 0.78 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1156 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3FBK · Crystal structure of the C2 domain of the human regulator of G-protein signaling 3… · the same entry in another collection · chain A against A, TM-score 1.00
- P49796 · AlphaFold monomer V2.0 prediction for regulator of G-protein signaling 3 (P49796) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 3FBK · PDBe 3FBK · UniProt P49796
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