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Free conformation AB1 of the IgE spe-7

Analyse Free conformation AB1 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
1OAQ
Type
protein
Length
230 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heavy chain; Light chain
Pockets
2 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HHeavy chainprotein1208% helix, 53% strand—
LLight chainprotein1105% helix, 56% strand—

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1890.350.7517empty
2560.270.7317empty

Interfaces

1 interface between chains.

  • H–L · 936 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1OAQ · Free conformation Ab1 of the IgE SPE-7 · the same entry in another collection · chain L against L, TM-score 1.00

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