Research workbench

Crystal structure of staphylococcus aureus elongation factor G with mutations M16I and F88L

Analyse Crystal structure of staphylococcus aureus elongation factor G with mutations… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZZU
Type: protein
Length: 1,296 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor G
UniProt: P68790
Pockets: 20 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Elongation factor G	protein	648	30% helix, 31% strand	P68790

Pockets

20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1015	0.75	0.78	91	empty
2	849	0.75	0.79	99	empty
3	135	0.55	0.82	24	empty
4	125	0.55	0.82	19	empty
5	177	0.50	0.77	33	empty

Interfaces

1 interface between chains.

A–B · 458 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3ZZU · Crystal structure of Staphylococcus aureus elongation factor G with mutations M16I and… · the same entry in another collection · chain A against A, TM-score 1.00
P68790 · AlphaFold monomer V2.0 prediction for elongation factor G (P68790) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 P68790
Elsewhere: RCSB PDB 3ZZU · PDBe 3ZZU · UniProt P68790

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