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Crystal structure of elongation factor G MUTANT(EFG)

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

PDB: 4MYU
Type: protein
Length: 655 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: 6 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor G	protein	655	27% helix, 34% 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

6 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	873	0.78	0.81	76	empty
2	63	0.54	0.88	22	empty
3	157	0.53	0.80	23	empty
4	248	0.51	0.75	30	empty
5	62	0.38	0.79	16	empty

Compared structures

4MYU · Crystal structure of elongation factor G mutant(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 0.72

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 4MYU · PDBe 4MYU · UniProt P13551

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