Research workbench

Elongation factor G in complex with GDP

Analyse Elongation factor G in complex with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DAR
Type: protein
Length: 615 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor G
UniProt: Q5SHN5
Ligands: GDP
Pockets: 5 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor G	protein	615	26% helix, 35% strand	Q5SHN5

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A

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

Pockets

5 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	429	0.65	0.78	53	empty
2	131	0.57	0.83	21	empty
3	85	0.43	0.79	19	empty
4	75	0.35	0.76	13	empty
5	53	0.33	0.77	11	empty

Compared structures

1DAR · Elongation factor G in complex with GDP · the same entry in another collection · chain A against A, TM-score 1.00
Q5SHN5 · AlphaFold monomer V2.0 prediction for elongation factor G (Q5SHN5) · a predicted model of the same protein · chain A against A, TM-score 0.79

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 Q5SHN5
Elsewhere: RCSB PDB 1DAR · PDBe 1DAR · UniProt Q5SHN5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.