Research workbench
Crystal structure of GDP-bound human gnas R201C mutant
Analyse Crystal structure of GDP-bound human gnas R201C mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AU6
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(S) subunit alpha isoforms short
- UniProt
- P63092
- Ligands
- GDP, MG, CL
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 343 | 52% helix, 13% strand | P63092 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.78 | 0.93 | 35 | GDP, MG |
| 2 | 215 | 0.65 | 0.84 | 27 | GOL |
| 3 | 95 | 0.45 | 0.79 | 18 | empty |
| 4 | 66 | 0.31 | 0.75 | 14 | empty |
Compared structures
- 6AU6 · Crystal structure of GDP-bound human GNAS R201C mutant · the same entry in another collection · chain A against A, TM-score 1.00
- P63092 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(S) subunit… · 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 P63092
- Elsewhere: RCSB PDB 6AU6 · PDBe 6AU6 · UniProt P63092
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