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HLA*A2402 complexed with HIV NEF138 8MER epitope

Analyse HLA*A2402 complexed with HIV NEF138 8MER epitope in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HGB
Type
protein
Length
1,528 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HLA class I histocompatibility antigen, a-24 alpha chain; Beta-2-microglobulin; Protein…
UniProt
P05534, P61769, P18801
Pockets
20 · best druggability 0.82

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, G, JHLA class I histocompatibility antigen, a-24 alpha chainprotein27427% helix, 40% strandP05534
B, E, H, KBeta-2-microglobulinprotein1000% helix, 48% strandP61769
C, F, I, LProtein nefprotein80% helix, 0% strandP18801

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111970.820.84115empty
25240.740.8262empty
34780.710.8147empty
45250.670.7853empty
55560.670.7754empty

Interfaces

19 interfaces between chains.

  • G–H · 1352 Ų buried · 22 hydrogen bonds · protein-protein
  • A–B · 1334 Ų buried · 18 hydrogen bonds · protein-protein
  • D–E · 1329 Ų buried · 20 hydrogen bonds · protein-protein
  • J–K · 1284 Ų buried · 18 hydrogen bonds · protein-protein
  • G–I · 967 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 5HGB · HLA*A2402 complexed with HIV nef138 8mer epitope · the same entry in another collection · chain L against L, TM-score 1.00

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