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Crystal structure of IrCp* immobilized apo-R52H-rHLFr
Analyse Crystal structure of IrCp* immobilized apo-R52H-rHLFr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EMM
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.25
- Source
- Equus caballus
- Molecule
- Ferritin light chain
- UniProt
- P02791
- Ligands
- CD, IR, SO4, CL
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · resolution 1.25 · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferritin light chain | protein | 173 | 74% helix, 0% strand | P02791 |
Ligands and binding sites
- CD · Cadmium ion · metal · 6 copies · chains A
- IR · Iridium ion · metal · 6 copies · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.43 | 0.79 | 21 | empty |
| 2 | 64 | 0.35 | 0.77 | 19 | empty |
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 7EMM · PDBe 7EMM · UniProt P02791
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