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Crystal structure of HLA-DQ2.5-CLIP2

Analyse Crystal structure of HLA-DQ2.5-CLIP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5KSV
Type
protein
Length
372 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MHC class II HLA-dq-alpha chain; MHC class II HLA-dq-beta-1; HLA class II…
UniProt
O19705, O19712
Pockets
3 · best druggability 0.54

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMHC class II HLA-dq-alpha chainprotein18014% helix, 44% strandO19705
BMHC class II HLA-dq-beta-1protein18022% helix, 46% strandO19712
CHLA class II histocompatibility antigen gamma chainprotein120% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13290.540.7453empty
2720.300.7320empty
3610.290.7418empty

Interfaces

3 interfaces between chains.

  • A–B · 2617 Ų buried · 51 hydrogen bonds · protein-protein
  • B–C · 715 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 581 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 5KSV · Crystal structure of HLA-DQ2.5-CLIP2 · the same entry in another collection · chain A against A, TM-score 1.00

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