Research workbench
Horse spleen apoferritin under 2 kbar of argon
Analyse Horse spleen apoferritin under 2 kbar of argon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RA8
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin light chain
- UniProt
- P02791
- Ligands
- CD, SO4, AR
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferritin light chain | protein | 173 | 73% helix, 0% strand | P02791 |
Ligands and binding sites
- CD · Cadmium ion · metal · 7 copies · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- AR · Argon · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (oxidation).
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 P02791
- Elsewhere: RCSB PDB 6RA8 · PDBe 6RA8 · UniProt P02791
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