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Giant panda MHC class I complexes

Analyse Giant panda MHC class I complexes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DC6
Type
protein
Length
765 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MHC class I antigen; Beta-2-microglobulin; Ccv-NGY9 peptide from spike protein
UniProt
B2KT53, D2GW37, Q65984
Pockets
10 · best druggability 0.73

Structure

x-ray diffraction · 4 distinct chains · 14% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CMHC class I antigenprotein27524% helix, 39% strandB2KT53
BBeta-2-microglobulinprotein990% helix, 49% strandD2GW37
DBeta-2-microglobulinprotein980% helix, 52% strandD2GW37
E, FCcv-NGY9 peptide from spike proteinprotein90% helix, 0% strandQ65984

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15880.730.8170empty
24790.660.7848empty
34020.660.7947empty
41600.570.8238empty
51270.510.8020empty

Interfaces

7 interfaces between chains.

  • A–B · 1396 Ų buried · 19 hydrogen bonds · protein-protein
  • C–D · 1291 Ų buried · 21 hydrogen bonds · protein-protein
  • C–F · 1015 Ų buried · 21 hydrogen bonds · protein-protein
  • A–E · 950 Ų buried · 20 hydrogen bonds · protein-protein
  • B–D · 322 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 7DC6 · Giant panda MHC class I complexes · the same entry in another collection · chain A against A, TM-score 1.00

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