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Conformational switch in polymorphic H-2K molecules containing an HSV peptide

Analyse Conformational switch in polymorphic H-2K molecules containing an HSV peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1T0M
Type
protein
Length
770 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
H-2 class I histocompatibility antigen, K-B alpha chain; Beta-2-microglobulin…
UniProt
P01901, P01887, P06436
Pockets
8 · best druggability 0.68

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DH-2 class I histocompatibility antigen, K-B alpha chainprotein27828% helix, 38% strandP01901
B, EBeta-2-microglobulinprotein990% helix, 49% strandP01887
P, QGlycoprotein Bprotein80% helix, 0% strandP06436

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17970.680.7560empty
25610.630.7550empty
31340.420.7527empty
41270.410.7527empty
5800.400.7817empty

Interfaces

5 interfaces between chains.

  • A–B · 1246 Ų buried · 22 hydrogen bonds · protein-protein
  • D–E · 1241 Ų buried · 20 hydrogen bonds · protein-protein
  • D–Q · 844 Ų buried · 20 hydrogen bonds · protein-protein
  • A–P · 843 Ų buried · 19 hydrogen bonds · protein-protein
  • A–D · 366 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1T0M · Conformational switch in polymorphic H-2K molecules containing an HSV peptide · the same entry in another collection · chain Q against Q, 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

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