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Crystal Structure of Reconstructed Bacterial Elongation Factor Node 168

Analyse Crystal Structure of Reconstructed Bacterial Elongation Factor Node 168 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5W76
Type: protein
Length: 384 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.152
Source: synthetic construct
Molecule: Ancestral Elogation Factor N153
Ligands: GDP, MG, SO4
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · resolution 2.152 · 1 distinct chain · 23% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ancestral Elogation Factor N153	protein	384	23% helix, 39% strand	—

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
PGE · Triethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.50	0.75	31	empty
2	115	0.38	0.75	22	empty

Compared structures

5W76 · Crystal structure of reconstructed bacterial elongation factor node 168 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 5W76 · PDBe 5W76

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