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Structure of the N-terminal MIF4G domain from S. cerevisiae UPF2, a protein involved in the degradation of mrnas containing premature stop codons

Analyse Structure of the N-terminal MIF4G domain from S. cerevisiae UPF2, a protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LUN
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nonsense-mediated mRNA decay protein 2
UniProt: P38798
Ligands: CL
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
U	Nonsense-mediated mRNA decay protein 2	protein	311	67% helix, 1% strand	P38798

Ligands and binding sites

CL · Chloride ion · ion · chains U

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	76	0.40	0.79	17	empty

Compared structures

4LUN · Structure of the N-terminal mIF4G domain from S. cerevisiae Upf2, a protein involved in… · the same entry in another collection · chain U against U, TM-score 1.00
P38798 · AlphaFold monomer V2.0 prediction for nonsense-mediated mRNA decay protein 2 (P38798) · a predicted model of the same protein · chain U against A, TM-score 0.99

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 P38798
Elsewhere: RCSB PDB 4LUN · PDBe 4LUN · UniProt P38798

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