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Crystal structure of bony fish MHC class I binding BETA2M-2 for 2.6 ångström

Analyse Crystal structure of bony fish MHC class I binding BETA2M-2 for 2.6 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LBE
Type
protein
Length
756 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MHC class I antigen; Beta-2-microglobulin; 9-mer peptide from RNA-directed RNA polymerase…
UniProt
Q65XY8, A0A3G2VUI3
Pockets
5 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 24% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMHC class I antigenprotein27429% helix, 39% strandQ65XY8
B, DBeta-2-microglobulinprotein980% helix, 51% strandA0A3G2VUI3
CMHC class I antigenprotein26827% helix, 41% strandQ65XY8
E, F9-mer peptide from RNA-directed RNA polymerase Lprotein90% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110350.760.78109empty
27600.720.7863empty
35000.670.7845empty
44940.670.7853empty
5880.570.8719empty

Interfaces

8 interfaces between chains.

  • A–B · 1838 Ų buried · 26 hydrogen bonds · protein-protein
  • C–D · 1725 Ų buried · 22 hydrogen bonds · protein-protein
  • C–F · 887 Ų buried · 14 hydrogen bonds · protein-protein
  • A–E · 883 Ų buried · 14 hydrogen bonds · protein-protein
  • A–C · 213 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 6LBE · Crystal structure of bony fish MHC class I binding beta2M-2 for 2.6 angstrom · the same entry in another collection · chain A against A, TM-score 1.00

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