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p53-specific T cell receptor

Analyse p53-specific T cell receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VTH
Type
protein
Length
867 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.36
Source
Homo sapiens
Molecule
T-cell Receptor 12-6, Alfa chain; TCR 12-6, beta chain
Ligands
SO4
Pockets
10 · best druggability 0.72

Structure

x-ray diffraction · resolution 2.36 · 4 distinct chains · 6% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AT-cell Receptor 12-6, Alfa chainprotein1925% helix, 47% strand—
BTCR 12-6, beta chainprotein2408% helix, 50% strand—
DT-cell Receptor 12-6, Alfa chainprotein1935% helix, 46% strand—
ETCR 12-6, beta chainprotein2427% helix, 50% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains B, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19390.720.7679empty
29750.710.7577empty
31470.540.8125empty
42640.470.7339empty
5770.390.7815empty

Interfaces

3 interfaces between chains.

  • A–B · 2129 Ų buried · 25 hydrogen bonds · protein-protein
  • D–E · 2119 Ų buried · 29 hydrogen bonds · protein-protein
  • B–E · 350 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 6VTH · P53-specific T cell receptor · the same entry in another collection · chain A against A, TM-score 1.00

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