2OQ1

Tandem SH2 domains of ZAP-70 with 19-mer zeta1 peptide

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.209 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Molecular basis for the interaction of ZAP-70 with the T-cell receptor

Hatada, M.H., Lu, X., Laird, E.R., Green, J., Morgenstern, J.P., Lou, M., Marr, C., Phillips, T.B., Ram, M.K., Theriault, K.

(1995) Nature 377: 32-38

  • DOI: https://doi.org/10.1038/377032a0
  • Primary Citation of Related Structures:  
    2OQ1

  • PubMed Abstract: 

    The crystal structure of the tandem SH2 domains of human ZAP-70 in complex with a peptide derived from the zeta-subunit of the T-cell receptor reveals an unanticipated interaction between the two domains. A coiled coil of alpha-helices connects the two SH2 domains, producing an interface that constitutes one of the two critical phosphotyrosine binding sites. These and other unique features provide the molecular basis for highly selective association of ZAP-70 with the T-cell receptor.

    • Organizational Affiliation: 

    ARIAD Pharmaceuticals, Inc., Cambridge, Massachusetts 02139-4234, USA.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Tyrosine-protein kinase ZAP-70254Homo sapiensMutation(s): 3 
EC: 2.7.10.2
UniProt & NIH Common Fund Data Resources
Find proteins for P43403 (Homo sapiens)
Explore P43403 
Go to UniProtKB:  P43403
PHAROS:  P43403
GTEx:  ENSG00000115085 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP43403
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
T-cell surface glycoprotein CD3 zeta chain19N/AMutation(s): 2 
UniProt & NIH Common Fund Data Resources
Find proteins for P20963 (Homo sapiens)
Explore P20963 
Go to UniProtKB:  P20963
PHAROS:  P20963
GTEx:  ENSG00000198821 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP20963
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PB
Query on PB
Download Ideal Coordinates CCD File 
C [auth A]LEAD (II) ION
Pb
RVPVRDXYQKGNMQ-UHFFFAOYSA-N
Modified Residues  2 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
PTR
Query on PTR
B
L-PEPTIDE LINKINGC9 H12 N O6 PTYR
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.209 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.11α = 90
b = 63.37β = 114.44
c = 54γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement
PDB_EXTRACTdata extraction
CrystalCleardata collection
DENZOdata reduction
SCALEPACKdata scaling
MLPHAREphasing
CNSrefinement

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-03-06
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-07-24
    Changes: Data collection, Derived calculations, Refinement description
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references, Derived calculations