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Research workbench

Echo 18 incubated with fcrn at PH5.5

Analyse Echo 18 incubated with fcrn at PH5.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7XXJ
Type
protein
Length
798 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
VP1; VP2; VP3; VP4
Ligands
PLM
Pockets
5 · best druggability 0.77

Structure

electron microscopy · 4 distinct chains · 9% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVP1protein26910% helix, 28% strand—
BVP2protein25010% helix, 36% strand—
CVP3protein2388% helix, 26% strand—
DVP4protein417% helix, 2% strand—

Ligands and binding sites

  • PLM · Palmitic acid · ligand · chains A, C

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
11120.770.9627PLM
2990.340.7318empty
3580.320.7617empty
4700.320.7514empty
5650.310.7519empty

Interfaces

6 interfaces between chains.

  • A–C · 4352 Ų buried · 92 hydrogen bonds · protein-protein
  • A–B · 2038 Ų buried · 39 hydrogen bonds · protein-protein
  • B–C · 1719 Ų buried · 28 hydrogen bonds · protein-protein
  • A–D · 1197 Ų buried · 19 hydrogen bonds · protein-protein
  • C–D · 1033 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7XXJ · Echo 18 incubated with FcRn at pH5.5 · the same entry in another collection · chain A against A, TM-score 1.00

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