Research workbench
Crystal structure of trimeric frataxin from the yeast saccharomyces cerevisiae, complexed with ferrous
Analyse Crystal structure of trimeric frataxin from the yeast saccharomyces cerevisiae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EC2
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frataxin homolog, mitochondrial
- EC
- 1.16.3.1
- UniProt
- Q07540
- Ligands
- FE2
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Frataxin homolog, mitochondrial (EC 1.16.3.1) | protein | 112 | 22% helix, 29% strand | Q07540 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4EC2 · Crystal structure of trimeric frataxin from the yeast Saccharomyces cerevisiae, complexed… · the same entry in another collection · chain A against A, TM-score 1.00
- Q07540 · AlphaFold monomer V2.0 prediction for frataxin homolog, mitochondrial (Q07540) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 Q07540
- Elsewhere: RCSB PDB 4EC2 · PDBe 4EC2 · UniProt Q07540
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