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Crystal structure of elongation factor G (efg)

Analyse Crystal structure of elongation factor G (efg) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MYT
Type: protein
Length: 656 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor G
UniProt: P13551
Ligands: GDP, MG
Pockets: 10 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor G	protein	656	26% helix, 27% strand	P13551

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1165	0.80	0.81	97	empty
2	114	0.70	0.91	29	empty
3	145	0.53	0.80	19	empty
4	170	0.47	0.76	23	empty
5	67	0.36	0.77	12	empty

Compared structures

4MYT · Crystal structure of elongation factor G (EFG) · the same entry in another collection · chain A against A, TM-score 1.00
P13551 · AlphaFold monomer V2.0 prediction for elongation factor G (P13551) · a predicted model of the same protein · chain A against A, TM-score 0.78

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 P13551
Elsewhere: RCSB PDB 4MYT · PDBe 4MYT · UniProt P13551

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