2AO7

Adam10 Disintegrin and cysteine- rich domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.261 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans.

Janes, P.W.Saha, N.Barton, W.A.Kolev, M.V.Wimmer-Kleikamp, S.H.Nievergall, E.Blobel, C.P.Himanen, J.-P.Lackmann, M.Nikolov, D.B.

(2005) Cell 123: 291-304

  • DOI: https://doi.org/10.1016/j.cell.2005.10.004
  • Primary Citation of Related Structures:  
    2AO7

  • PubMed Abstract: 

    Ephrin ligands presented on one cell surface associate with their receptors on the surface of a juxtaposed cell, often resulting in cell-cell repulsion. In this issue of Cell, Janes et al. (2005) show that the ephrin ligand can be proteolytically released from its membrane tether by a complex on the opposing cell composed of the ephrin receptor and an ADAM metalloprotease.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ADAM 10192Bos taurusMutation(s): 0 
Gene Names: ADAM10MADM
EC: 3.4.24.81
Membrane Entity: Yes 
UniProt
Find proteins for Q10741 (Bos taurus)
Explore Q10741 
Go to UniProtKB:  Q10741
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ10741
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.261 
  • Space Group: I 41 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 146.78α = 90
b = 146.78β = 90
c = 146.78γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
autoSHARPphasing
DMmodel building
CNSrefinement
DMphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2006-08-08
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance