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Crystal structure of C-terminal half of lactoferrin obtained by limited proteolysis using pepsin at 2.6 A resolution

Analyse Crystal structure of C-terminal half of lactoferrin obtained by limited… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EVQ
Type
protein
Length
696 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.6
Source
Bos taurus
Molecule
Lactotransferrin
EC
3.4.21.-
UniProt
P24627
Ligands
BCT, NAG, BMA, FE
Pockets
8 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.6 · 1 distinct chain · 35% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLactotransferrin (EC 3.4.21.-)protein34835% helix, 18% strandP24627

Ligands and binding sites

  • BCT · Bicarbonate ion · ligand · 2 copies · chains A, B
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 4 copies · chains A, B
  • FE · Fe (III) ion · metal · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13680.690.8260empty
22210.680.8541empty
32880.570.7740empty
41460.470.7730empty
51090.360.7315empty

Interfaces

1 interface between chains.

  • A–B · 546 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide, 6 glycan (disulfide, N-glycosylation).

Compared structures

  • 7EVQ · Crystal structure of C-terminal half of lactoferrin obtained by limited proteolysis using… · the same entry in another collection · chain A against A, TM-score 1.00

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