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Gs-alpha complexed with GTP-gamma-S

Analyse Gs-alpha complexed with GTP-gamma-S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AZT
Type: protein
Length: 675 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gs-alpha
UniProt: P04896
Ligands: GSP, MG, PO4
Pockets: 8 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gs-alpha	protein	335	50% helix, 12% strand	P04896
B	Gs-alpha	protein	340	51% helix, 12% strand	P04896

Ligands and binding sites

GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B
PO4 · Phosphate ion · ion · 16 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	925	0.83	0.85	67	PO4
2	703	0.80	0.84	81	MG, PO4, GSP
3	623	0.77	0.83	61	MG, PO4, GSP
4	112	0.50	0.81	23	PO4
5	131	0.48	0.79	21	empty

Interfaces

1 interface between chains.

A–B · 1410 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1AZT · Gs-alpha complexed with GTP-gamma-S · the same entry in another collection · chain A against A, TM-score 1.00
P04896 · 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 0.99

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 P04896
Elsewhere: RCSB PDB 1AZT · PDBe 1AZT · UniProt P04896

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