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Crystal structure of HLA B*3508LPEP-P5ALA , peptide mutant P5-ala

Analyse Crystal structure of HLA B*3508LPEP-P5ALA , peptide mutant P5-ala in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VFS
Type
protein
Length
388 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MHC class I antigen; Beta-2-microglobulin; Lpep peptide from EBV, P5A, lpepapqgqltay
UniProt
C5MK56, P61769
Pockets
5 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 19% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMHC class I antigenprotein27626% helix, 39% strandC5MK56
BBeta-2-microglobulinprotein990% helix, 49% strandP61769
CLpep peptide from EBV, P5A, lpepapqgqltayprotein130% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16360.690.7854empty
2650.590.9020empty
3840.420.7923empty
4950.380.7623empty
5780.370.7716empty

Interfaces

2 interfaces between chains.

  • A–B · 1376 Ų buried · 22 hydrogen bonds · protein-protein
  • A–C · 956 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 3VFS · crystal structure of HLA B*3508LPEP-P5Ala , peptide mutant P5-ala · the same entry in another collection · chain C against C, TM-score 1.00
  • P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain B against A, TM-score 0.98

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