Research workbench
Mutant R59M recombinant horse spleen apoferritin cocrystallized with haemin in basic conditions
Analyse Mutant R59M recombinant horse spleen apoferritin cocrystallized with haemin in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V2O
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin light chain
- UniProt
- P02791
- Ligands
- CD, SO4
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferritin light chain | protein | 171 | 76% helix, 0% strand | P02791 |
Ligands and binding sites
- CD · Cadmium ion · metal · 9 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2V2O · Mutant R59M recombinant horse spleen apoferritin cocrystallized with haemin in basic… · the same entry in another collection · chain A against A, TM-score 1.00
- P02791 · AlphaFold monomer V2.0 prediction for ferritin light chain (P02791) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 2V2O · PDBe 2V2O · UniProt P02791
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