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Crystal structure of a HLA-B*35:01-hpvg-A4

Analyse Crystal structure of a HLA-B*35:01-hpvg-A4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4PRN
Type
protein
Length
386 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HLA class I histocompatibility antigen, B-35 alpha chain; Beta-2-microglobulin…
UniProt
P30685, P61769, Q1HVF7
Pockets
5 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 19% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHLA class I histocompatibility antigen, B-35 alpha chainprotein27626% helix, 39% strandP30685
BBeta-2-microglobulinprotein990% helix, 49% strandP61769
CEpstein-barr nuclear antigen 1protein1127% helix, 0% strandQ1HVF7

Ligands and binding sites

  • ACT · Acetate ion · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15860.690.7850empty
2890.420.7922empty
3990.380.7621empty
4710.370.7817empty
5590.330.7717ACT

Interfaces

2 interfaces between chains.

  • A–B · 1354 Ų buried · 25 hydrogen bonds · protein-protein
  • A–C · 954 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 4PRN · Crystal structure of a HLA-B*35:01-HPVG-A4 · 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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