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Crystal structure of the first class MHC mamu and tat-TL8 complex

Analyse Crystal structure of the first class MHC mamu and tat-TL8 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZVS
Type
protein
Length
770 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MHC class I antigen; Beta-2-microglobulin; Tat-TL8
UniProt
P61769
Pockets
11 · best druggability 0.78

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DMHC class I antigenprotein27827% helix, 38% strand—
B, EBeta-2-microglobulinprotein990% helix, 49% strandP61769
C, FTat-TL8protein80% helix, 0% strand—

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15110.780.8574empty
27340.700.7765empty
33680.680.8142empty
41210.450.7823empty
5810.440.8121empty

Interfaces

7 interfaces between chains.

  • A–B · 1239 Ų buried · 22 hydrogen bonds · protein-protein
  • D–E · 1233 Ų buried · 21 hydrogen bonds · protein-protein
  • A–C · 762 Ų buried · 20 hydrogen bonds · protein-protein
  • D–F · 736 Ų buried · 20 hydrogen bonds · protein-protein
  • A–D · 523 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1ZVS · Crystal structure of the first class MHC mamu and Tat-Tl8 complex · the same entry in another collection · chain F against F, TM-score 1.00
  • P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain E against A, TM-score 0.98

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