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Crystal structure of bacterial selenocysteine-specific elongation factor ef-sec

Analyse Crystal structure of bacterial selenocysteine-specific elongation factor ef-sec in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ZU9
Type
protein
Length
582 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor selb
UniProt
O67141
Ligands
GNP, CYS, MG, SO4
Pockets
7 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AElongation factor selbprotein58235% helix, 28% strandO67141

Ligands and binding sites

  • GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
  • CYS · Cysteine · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14860.690.8064empty
21050.470.8026GNP, MG
31250.400.7526CYS
4570.320.7614empty
5510.300.7615empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

  • 4ZU9 · Crystal structure of bacterial selenocysteine-specific elongation factor EF-Sec · the same entry in another collection · chain A against A, TM-score 1.00

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