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Crystal structure of EHA2 (23-185)

Analyse Crystal structure of EHA2 (23-185) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1QU1
Type
protein
Length
874 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (influenza recombinant HA2 chain)
UniProt
P03437
Pockets
7 · best druggability 0.48

Structure

x-ray diffraction · 5 distinct chains · 63% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (influenza recombinant HA2 chain)protein13367% helix, 0% strandP03437
BProtein (influenza recombinant HA2 chain)protein14463% helix, 7% strandP03437
CProtein (influenza recombinant HA2 chain)protein15061% helix, 1% strandP03437
D, EProtein (influenza recombinant HA2 chain)protein14665% helix, 3% strandP03437
FProtein (influenza recombinant HA2 chain)protein15560% helix, 4% strandP03437

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11340.480.7922empty
21160.430.7723empty
31100.420.7719empty
41030.390.7619empty
5880.380.7617empty

Interfaces

6 interfaces between chains.

  • D–F · 2410 Ų buried · 31 hydrogen bonds · protein-protein
  • D–E · 2354 Ų buried · 33 hydrogen bonds · protein-protein
  • B–C · 2315 Ų buried · 33 hydrogen bonds · protein-protein
  • E–F · 2293 Ų buried · 32 hydrogen bonds · protein-protein
  • A–B · 2263 Ų buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1QU1 · Crystal structure of EHA2 (23-185) · the same entry in another collection · chain A against A, TM-score 1.00

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