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Structural evidence for a pH-sensitive di-lysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release

Analyse Structural evidence for a pH-sensitive di-lysine trigger in the hen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1NNT
Type
protein
Length
328 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ovotransferrin
UniProt
P02789
Ligands
FE, CO3
Pockets
5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOvotransferrinprotein32831% helix, 21% strandP02789

Ligands and binding sites

  • FE · Fe (III) ion · metal · chains A
  • CO3 · Carbonate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12390.800.9334empty
21210.490.8020empty
3940.370.7520empty
4730.310.7414empty
5630.290.7316empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1NNT · Structural evidence for a pH-sensitive di-lysine trigger in the hen ovotransferrin… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02789 · AlphaFold monomer V2.0 prediction for ovotransferrin (P02789) · a predicted model of the same protein · chain A against A, TM-score 0.99

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