GL1X · GenesisL1 explorer

Research workbench

Crystal structures of murine MHC class I H-2 db and kb molecules in complex with ctl epitopes from influenza a virus: implications for TCR repertoire selection and immunodominance

Analyse Crystal structures of murine MHC class I H-2 db and kb molecules in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WBX
Type
protein
Length
384 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
H-2 class I histocompatibility antigen, D-B alpha chain; Beta-2MICROGLOBULIN; Influenza a…
UniProt
P01899, P01887, P26140
Pockets
3 · best druggability 0.66

Structure

x-ray diffraction · 3 distinct chains · 20% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AH-2 class I histocompatibility antigen, D-B alpha chainprotein27527% helix, 40% strandP01899
BBeta-2MICROGLOBULINprotein990% helix, 49% strandP01887
CInfluenza a peptideprotein100% helix, 0% strandP26140

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16130.660.7656empty
21410.480.7831empty
3930.450.8017empty

Interfaces

2 interfaces between chains.

  • A–B · 1289 Ų buried · 22 hydrogen bonds · protein-protein
  • A–C · 976 Ų buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1WBX · CRYSTAL STRUCTURES OF MURINE MHC CLASS I H-2 Db AND Kb MOLECULES IN COMPLEX WITH CTL… · the same entry in another collection · chain A against A, TM-score 1.00
  • P01887 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P01887) · a predicted model of the same protein · chain B against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.