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Complex of echo 18 and fcrn at PH7.4

Analyse Complex of echo 18 and fcrn at PH7.4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7XXA
Type
protein
Length
950 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
VP1; IgG receptor fcrn large subunit P51; VP2; VP3; VP4
UniProt
P55899
Pockets
7 · best druggability 0.62

Structure

electron microscopy · 5 distinct chains · 14% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVP1protein27610% helix, 26% strand—
EIgG receptor fcrn large subunit P51protein14439% helix, 33% strandP55899
BVP2protein25010% helix, 36% strand—
CVP3protein2388% helix, 30% strand—
DVP4protein4214% helix, 2% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11570.620.8536empty
22570.620.8040empty
31030.420.7717empty
4560.410.8214empty
5540.350.7913empty

Interfaces

9 interfaces between chains.

  • A–C · 4445 Ų buried · 79 hydrogen bonds · protein-protein
  • A–B · 2096 Ų buried · 35 hydrogen bonds · protein-protein
  • B–C · 1698 Ų buried · 27 hydrogen bonds · protein-protein
  • A–D · 1239 Ų buried · 24 hydrogen bonds · protein-protein
  • C–D · 1018 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7XXA · Complex of Echo 18 and FcRn at pH7.4 · the same entry in another collection · chain A against A, 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 E against A, TM-score 0.98

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