Research workbench
Mitoneet is a uniquely folded 2FE-2S outer mitochondrial membrane protein stabilized by pioglitazone
Analyse Mitoneet is a uniquely folded 2FE-2S outer mitochondrial membrane protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QH7
- Type
- protein
- Length
- 130 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zinc finger cdgsh-type domain 1
- UniProt
- Q1X902
- Ligands
- FES
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger cdgsh-type domain 1 | protein | 65 | 18% helix, 28% strand | Q1X902 |
| B | Zinc finger cdgsh-type domain 1 | protein | 65 | 18% helix, 29% strand | Q1X902 |
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 · 1925 Ų buried · 44 hydrogen bonds · protein-protein
Compared structures
- 2QH7 · MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by… · 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
- Every structure of UniProt Q1X902
- Elsewhere: RCSB PDB 2QH7 · PDBe 2QH7 · UniProt Q1X902
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