MolNFT v1 · #189498 · protein
Crystal structure of AU(100EQ)-apo-R168H/L169C-rhlfr
7VIR · Ferritin light chain: “Crystal structure of AU(100EQ)-apo-R168H/L169C-rhlfr”. X-ray diffraction, 3 ligands (AU, CD, SO4), 2 pockets (best druggability 0.40). MolNFT v1 #189498 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7VIR
- 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
- AU, CD, SO4
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferritin light chain | protein | 171 | 77% helix, 0% strand | P02791 |
Ligands and binding sites
- AU · Gold ion · metal · 8 copies · chains A
- CD · Cadmium ion · metal · 4 copies · chains A
- SO4 · Sulfate ion · ion · 3 copies · 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 | 66 | 0.40 | 0.79 | 11 | empty |
| 2 | 51 | 0.32 | 0.77 | 18 | 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 7VIR · PDBe 7VIR · UniProt P02791
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