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Human serum transferrin

Analyse 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
1D3K
Type
protein
Length
329 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serum transferrin
UniProt
P02787
Ligands
FE, CO3
Pockets
2 · best druggability 0.74

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerum transferrinprotein32936% helix, 20% strandP02787

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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12260.740.8941empty
2840.350.7519empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 1D3K · Human serum transferrin · the same entry in another collection · chain A against A, TM-score 1.00
  • P02787 · AlphaFold monomer V2.0 prediction for serotransferrin (P02787) · a predicted model of the same protein · chain A against A, TM-score 0.98

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