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Crystal structure a major allergen from dust mite

Analyse Crystal structure a major allergen from dust mite in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3UV1
Type
protein
Length
380 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Der F 7 allergen
UniProt
A1KXH4
Pockets
3 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BDer F 7 allergenprotein19029% helix, 45% strandA1KXH4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11280.450.7727empty
21080.360.7421empty
3760.340.7619empty

Interfaces

1 interface between chains.

  • A–B · 1420 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 3UV1 · Crystal structure a major allergen from dust mite · the same entry in another collection · chain A against A, TM-score 1.00

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