6G9Q

Ternary complex of P14 TCR with murine MHC class I H-2 Db in complex with self-antigen derived from dopamine monooxygenase.

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.89 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

Structural basis for CD8+ T cells auto-reactivity in LCMV infection

Allerbring, E., Duru, A.D., Nygren, P.A., Sandalova, T., Achour, A.

To be published.

Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
H-2 class I histocompatibility antigen, D-B alpha chain276Mus musculusMutation(s): 0 
Gene Names: H2-D1
UniProt
Find proteins for P01899 (Mus musculus)
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UniProt GroupP01899
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-2-microglobulin119Mus musculusMutation(s): 1 
Gene Names: B2m
UniProt & NIH Common Fund Data Resources
Find proteins for P01887 (Mus musculus)
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IMPC:  MGI:88127
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UniProt GroupP01887
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
T cell receptor alpha variable 14-1,T-cell receptor alpha chain C regionC [auth G]205Mus musculusMutation(s): 0 
Gene Names: Trav14-1, Tcra
UniProt
Find proteins for A0A0G2JF94 (Mus musculus)
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UniProt GroupA0A0G2JF94
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
T-cell receptor beta chain V region C5,T-cell receptor beta-1 chain C regionD [auth H]238Mus musculusMutation(s): 0 
UniProt
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Find proteins for P01852 (Mus musculus)
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UniProt GroupsP01852P04213
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Dopamine beta-hydroxylaseE [auth P]9Mus musculusMutation(s): 1 
EC: 1.14.17.1
UniProt
Find proteins for Q64237 (Mus musculus)
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Entity Groups  
UniProt GroupQ64237
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GOL
Query on GOL
Download Ideal Coordinates CCD File 
F [auth A]GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.89 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 256.383α = 90
b = 46.622β = 94.2
c = 90.059γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-04-24
    Type: Initial release
  • Version 1.1: 2024-01-17
    Changes: Data collection, Database references, Refinement description