MolNFT v1 · #63627 · protein

Gi-alpha-1 mutant in GDP bound form

3FFB · Guanine nucleotide-binding protein G(I), alpha-1 subunit: “Gi-alpha-1 mutant in GDP bound form”. X-ray diffraction, 2 ligands (GDP, SO4), 3 pockets (best druggability 0.64). MolNFT v1 #63627 on GenesisL1: 3D structure, binding sites…

PDB: 3FFB
Type: protein
Length: 327 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanine nucleotide-binding protein G(I), alpha-1 subunit
UniProt: P10824
Ligands: GDP, SO4
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanine nucleotide-binding protein G(I), alpha-1 subunit	protein	327	52% helix, 12% strand	P10824

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	164	0.64	0.86	30	GDP
2	294	0.60	0.79	30	empty
3	61	0.34	0.77	14	empty

Compared structures

3FFB · Gi-alpha-1 mutant in GDP bound form · the same entry in another collection · chain A against A, TM-score 1.00
P10824 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P10824
Elsewhere: RCSB PDB 3FFB · PDBe 3FFB · UniProt P10824

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