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The crystal structure of human eefsec in complex with gdpnp

Analyse The crystal structure of human eefsec in complex with gdpnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IZM
Type
protein
Length
955 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Selenocysteine-specific elongation factor
UniProt
P57772
Ligands
GNP, MN
Pockets
9 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASelenocysteine-specific elongation factorprotein46016% helix, 30% strandP57772
BSelenocysteine-specific elongation factorprotein49516% helix, 35% strandP57772

Ligands and binding sites

  • GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · 2 copies · chains A, B
  • MN · Manganese (II) ion · metal · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15230.660.7769empty
24070.640.7860MN, GNP
33980.620.7747empty
43620.610.7841empty
5550.420.8213empty

Interfaces

1 interface between chains.

  • A–B · 503 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 29 modified (engineered).

Compared structures

  • 5IZM · The crystal structure of human eEFSec in complex with GDPNP · the same entry in another collection · chain A against A, TM-score 1.00
  • P57772 · AlphaFold monomer V2.0 prediction for selenocysteine-specific elongation factor (P57772) · a predicted model of the same protein · chain A against A, TM-score 0.95

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