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Crystal structure of HLA Class I antigen

Analyse Crystal structure of HLA Class I antigen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XS3
Type
protein
Length
378 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.5
Source
Homo sapiens
Molecule
Heavy Chain; Light Chain; P
Pockets
4 · best druggability 0.67

Structure

x-ray diffraction · resolution 2.5 · 3 distinct chains · 19% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeavy Chainprotein27127% helix, 41% strand—
BLight Chainprotein980% helix, 50% strand—
CPprotein90% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15470.670.7750empty
21650.440.7534empty
3810.350.7518empty
4660.290.7414empty

Interfaces

2 interfaces between chains.

  • A–B · 1253 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 959 Ų buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 5XS3 · Crystal structure of HLA class I antigen · the same entry in another collection · chain A against A, TM-score 1.00

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