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Immune receptor

Analyse Immune receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MDJ
Type
protein
Length
383 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HLA class II histocompatibility antigen, dr alpha chain; HLA class II histocompatibility…
UniProt
P01903, P13760, P08670
Ligands
NAG
Pockets
3 · best druggability 0.43

Structure

x-ray diffraction · 3 distinct chains · 16% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHLA class II histocompatibility antigen, dr alpha chainprotein17914% helix, 47% strandP01903
BHLA class II histocompatibility antigen, DRB1-4 beta chainprotein19118% helix, 44% strandP13760
CVimentinprotein130% helix, 8% strandP08670

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11400.430.7632empty
21420.410.7421empty
3730.290.7219empty

Interfaces

3 interfaces between chains.

  • A–B · 2485 Ų buried · 43 hydrogen bonds · protein-protein
  • B–C · 643 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 534 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

  • 4MDJ · Immune Receptor · the same entry in another collection · chain A against A, TM-score 1.00
  • P01903 · AlphaFold monomer V2.0 prediction for HLA class II histocompatibility antigen, dr alpha… · a predicted model of the same protein · chain A against A, TM-score 0.96

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