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Crystal structure of HLA B*3508LPEP-P6ALA, peptide mutant P6-ala

Analyse Crystal structure of HLA B*3508LPEP-P6ALA, peptide mutant P6-ala in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VFT
Type
protein
Length
389 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, P6A, lpeplaqgqltay
UniProt
C5MK56, P61769
Pockets
7 · 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-microglobulinprotein1000% helix, 49% strandP61769
CLpep peptide from EBV, P6A, lpeplaqgqltayprotein130% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16660.690.7755empty
2500.650.9617empty
3990.410.7721empty
4770.390.7822empty
5800.390.7816empty

Interfaces

2 interfaces between chains.

  • A–B · 1421 Ų buried · 23 hydrogen bonds · protein-protein
  • A–C · 939 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 3VFT · crystal structure of HLA B*3508LPEP-P6Ala, peptide mutant P6-ala · the same entry in another collection · chain A against A, 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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