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Crystal structure of AU(50EQ)-apo-R168H/L169C-rhlfr

Analyse Crystal structure of AU(50EQ)-apo-R168H/L169C-rhlfr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VIQ
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
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerritin light chainprotein17177% helix, 0% strandP02791

Ligands and binding sites

  • AU · Gold ion · metal · 8 copies · chains A
  • CD · Cadmium ion · metal · 4 copies · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1590.360.7911empty

Compared structures

  • 7VIQ · Crystal structure of Au(50EQ)-apo-R168H/L169C-rHLFr · 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 0.91

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