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Structure of GTP-binding protein

Analyse Structure of GTP-binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GIT
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: G protein gi alpha 1
UniProt: P10824
Ligands: GDP, PO4
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	G protein gi alpha 1	protein	317	51% helix, 15% strand	P10824

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
PO4 · Phosphate ion · ion · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	166	0.72	0.90	33	PO4, GDP
2	238	0.59	0.80	28	empty
3	107	0.39	0.75	23	empty
4	76	0.36	0.76	13	empty

Compared structures

1GIT · Structure of GTP-binding protein · 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 0.97

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 1GIT · PDBe 1GIT · UniProt P10824

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