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Free conformation AB2 of the IgE spe-7

Analyse Free conformation AB2 of the IgE spe-7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OCW
Type
protein
Length
230 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Immunoglobulin E
Pockets
1 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HImmunoglobulin Eprotein1200% helix, 36% strand—
LImmunoglobulin Eprotein1103% helix, 52% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1560.530.8812empty

Interfaces

1 interface between chains.

  • H–L · 997 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1OCW · Free conformation Ab2 of the IgE SPE-7 · the same entry in another collection · chain H against H, TM-score 1.00

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