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The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain

Analyse The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EW0
Type
protein
Length
153 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.4
Source
Homo sapiens
Molecule
CDGSH iron sulfur domain-containing protein 1
UniProt
Q9NZ45
Ligands
FES

Structure

x-ray diffraction · resolution 1.4 · 2 distinct chains · 15% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACDGSH iron sulfur domain-containing protein 1protein7716% helix, 18% strandQ9NZ45
BCDGSH iron sulfur domain-containing protein 1protein7614% helix, 18% strandQ9NZ45

Ligands and binding sites

  • FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B

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

Interfaces

1 interface between chains.

  • A–B · 2015 Ų buried · 45 hydrogen bonds · protein-protein

Compared structures

  • 3EW0 · The novel 2FE-2S outer mitochondrial protein mitoneet displays conformational flexibility… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NZ45 · AlphaFold monomer V2.0 prediction for cdgsh iron-sulfur domain- containing protein 1… · a predicted model of the same protein · chain B against A, TM-score 0.86

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