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Crystal structure of FcRn at pH3

Analyse Crystal structure of FcRn at pH3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6C97
Type
protein
Length
728 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Homo sapiens
Molecule
IgG receptor FcRn large subunit p51; Beta-2-microglobulin
UniProt
P55899, P61769
Pockets
5 · best druggability 0.74

Structure

x-ray diffraction · resolution 2 · 2 distinct chains · 19% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CIgG receptor FcRn large subunit p51protein26526% helix, 42% strandP55899
B, DBeta-2-microglobulinprotein990% helix, 49% strandP61769

Ligands and binding sites

  • GOL · Glycerol · additive · 3 copies · chains A, B

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
110270.740.77112empty
21820.490.7732GOL
31820.450.7430empty
41550.430.7523empty
51140.370.7420empty

Interfaces

5 interfaces between chains.

  • A–B · 1478 Ų buried · 20 hydrogen bonds · protein-protein
  • C–D · 1447 Ų buried · 22 hydrogen bonds · protein-protein
  • A–C · 982 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 89 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 81 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 6C97 · Crystal structure of fcrn at PH3 · the same entry in another collection · chain D against D, TM-score 1.00
  • P55899 · AlphaFold monomer V2.0 prediction for IgG receptor fcrn large subunit P51 (P55899) · a predicted model of the same protein · chain A against A, TM-score 1.00
  • P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain D against A, TM-score 0.98

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