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Hepcidin-Fab complex

Analyse Hepcidin-Fab complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3H0T
Type
protein
Length
461 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab fragment, light chain; Fab fragment, heavy chain; Hepcidin
UniProt
P81172
Pockets
5 · best druggability 0.66

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFab fragment, light chainprotein2169% helix, 50% strand—
BFab fragment, heavy chainprotein2239% helix, 53% strand—
CHepcidinprotein220% helix, 41% strandP81172

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16980.660.7561empty
21470.440.7625empty
31000.410.7718empty
4970.370.7517empty
5580.270.7418empty

Interfaces

3 interfaces between chains.

  • A–B · 1752 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 460 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 321 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 3H0T · Hepcidin-Fab complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P81172 · AlphaFold monomer V2.0 prediction for hepcidin (P81172) · a predicted model of the same protein · chain C against A, TM-score 0.49

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