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Structure of the DP10.7 TCR

Analyse Structure of the DP10.7 TCR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MNH
Type
protein
Length
863 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
T-cell receptor gamma chain V region pt-gamma-1/2, human nkt TCR beta chain; Human nkt…
UniProt
K7N5M4, Q6PJ56
Pockets
10 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 5% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AT-cell receptor gamma chain V region pt-gamma-1/2, human nkt TCR beta chainprotein2317% helix, 48% strandK7N5M4
BHuman nkt TCR alpha chainprotein1972% helix, 41% strandQ6PJ56
CT-cell receptor gamma chain V region pt-gamma-1/2, human nkt TCR beta chainprotein2367% helix, 48% strandK7N5M4
DHuman nkt TCR alpha chainprotein1993% helix, 42% strandQ6PJ56

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19680.710.7677empty
28260.670.7567empty
34280.640.7848empty
4710.430.8017empty
51400.430.7528empty

Interfaces

5 interfaces between chains.

  • C–D · 2302 Ų buried · 29 hydrogen bonds · protein-protein
  • A–B · 2252 Ų buried · 22 hydrogen bonds · protein-protein
  • B–D · 315 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 195 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 27 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 4MNH · Structure of the DP10.7 TCR · the same entry in another collection · chain A against A, TM-score 1.00

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