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Structure of titanium-bound human serum transferrin

Analyse Structure of titanium-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
5H52
Type
protein
Length
650 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serotransferrin
UniProt
P02787
Ligands
4TI
Pockets
6 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerotransferrinprotein65038% helix, 19% strandP02787

Ligands and binding sites

  • 4TI · Titanium ion · metal · 2 copies · chains A
  • MLI · Malonate ion · additive · chains A
  • CIT · Citric acid · 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
18570.790.8180MLI
26660.760.8165empty
32030.580.8021empty
41100.370.74274TI, CIT
5750.360.7615empty

Modifications

Observed in the structure: 17 disulfide (disulfide).

Compared structures

  • 5H52 · Structure of Titanium-bound 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 0.82

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