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Osmium-bound human serum transferrin

Analyse Osmium-bound human serum transferrin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7FFU
Type
protein
Length
649 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serotransferrin
UniProt
P02787
Ligands
FE, OS
Pockets
6 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerotransferrinprotein64936% helix, 20% strandP02787

Ligands and binding sites

  • FE · Fe (III) ion · metal · chains A
  • OS · Osmium ion · metal · chains A
  • MLI · Malonate ion · additive · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18590.780.8183MLI
26650.760.8253empty
31810.560.8020empty
41330.400.7427empty
5760.330.7415empty

Modifications

Observed in the structure: 17 disulfide (disulfide).

Compared structures

  • 7FFU · Osmium-bound human serum transferrin · the same entry in another collection · chain A against A, TM-score 1.00

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