Research workbench
Human mitochondrial ferritin mutant bound with gold ions
Analyse Human mitochondrial ferritin mutant bound with gold ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z91
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.004
- Source
- Homo sapiens
- Molecule
- Ferritin, mitochondrial
- EC
- 1.16.3.1
- UniProt
- Q8N4E7
- Ligands
- AU, MG
Structure
x-ray diffraction · resolution 3.004 · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferritin, mitochondrial (EC 1.16.3.1) | protein | 171 | 73% helix, 0% strand | Q8N4E7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q8N4E7
- Elsewhere: RCSB PDB 5Z91 · PDBe 5Z91 · UniProt Q8N4E7
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