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Crystal structure of ELS4 TCR at 1.4A

Analyse Crystal structure of ELS4 TCR at 1.4A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NW2
Type
protein
Length
439 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ELS4 TCR alpha chain; ELS4 TCR beta chain
UniProt
Q6P4G7, Q32P21
Pockets
5 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AELS4 TCR alpha chainprotein1965% helix, 45% strandQ6P4G7
BELS4 TCR beta chainprotein2437% helix, 51% strandQ32P21

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110250.700.7483empty
2530.310.7617empty
3530.310.7617empty
4540.290.7514empty
5520.260.7418empty

Interfaces

1 interface between chains.

  • A–B · 2224 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 2NW2 · Crystal structure of ELS4 TCR at 1.4A · the same entry in another collection · chain A against A, TM-score 1.00

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